|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
2-376 |
0e+00 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 728.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 2 THEVIALAQALIQRESVTPEDAGCQSMMNERLKALGFNIESLFFTDTLNTWARKGNQSPHFCFAGHTDVVPTGPAQNWQH 81
Cdd:PRK13009 1 MSDVLELAQDLIRRPSVTPDDAGCQDLLAERLEALGFTCERMDFGDVKNLWARRGTEGPHLCFAGHTDVVPPGDLEAWTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 82 PPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGPFINGTTKVIDTLEARGEKIDMCLV 161
Cdd:PRK13009 81 PPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGTVKVLEWLKARGEKIDYCIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 162 GEPSSRDVLGDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDNGNEFFPATSFQVSNINGGT 241
Cdd:PRK13009 161 GEPTSTERLGDVIKNGRRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAATEWDEGNEFFPPTSLQITNIDAGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 242 GAGNVIPGELEVQFNFRFSTEVTHQQLQERVNAILQTHDLNYELSWIVNGLPFITEHGPLVDATVNAIKSVTGLTTNLET 321
Cdd:PRK13009 241 GATNVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGLDYTLEWTLSGEPFLTPPGKLVDAVVAAIEAVTGITPELST 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 940685535 322 TGGTSDGRFIAQTGAKVIELGPNNATIHKVDECVSTDDLIALADIYEQILEQLLT 376
Cdd:PRK13009 321 SGGTSDARFIADYGAQVVEFGPVNATIHKVNECVSVADLEKLTRIYERILERLLA 375
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
6-371 |
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: 658.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 6 IALAQALIQRESVTPEDAGCQSMMNERLKALGFNIESLFFTDTLNTWARKGNQSPHFCFAGHTDVVPTGPAQNWQHPPFS 85
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCERLEFGGVKNLWARRGTGGPHLCFAGHTDVVPPGDLEGWSSDPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 86 GLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGPFINGTTKVIDTLEARGEKIDMCLVGEPS 165
Cdd:cd03891 81 PTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKARGEKIDYCIVGEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 166 SRDVLGDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDNGNEFFPATSFQVSNINGGTGAGN 245
Cdd:cd03891 161 SEKKLGDTIKIGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTATVLDEGNEFFPPSSLQITNIDVGNGATN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 246 VIPGELEVQFNFRFSTEVTHQQLQERVNAILQTHDLNYELSWIVNGLPFITEHGPLVDATVNAIKSVTGLTTNLETTGGT 325
Cdd:cd03891 241 VIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLSGEPFLTKPGKLVDAVSAAIKEVTGITPELSTSGGT 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 940685535 326 SDGRFIAQTGAKVIELGPNNATIHKVDECVSTDDLIALADIYEQIL 371
Cdd:cd03891 321 SDARFIASYGCPVVEFGLVNATIHKVNERVSVADLEKLTDIYERIL 366
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
5-374 |
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: 572.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 5 VIALAQALIQRESVTPEDAGCQSMMNERLKALGFNIESLFFTDTLNTWARKGNQSPHFCFAGHTDVVPTGPAQNWQHPPF 84
Cdd:TIGR01246 1 VTELAKELISRPSVTPNDAGCQDIIAERLEKLGFEIEWMHFGDTKNLWATRGTGEPVLAFAGHTDVVPAGPEEQWSSPPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 85 SGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGPFINGTTKVIDTLEARGEKIDMCLVGEP 164
Cdd:TIGR01246 81 EPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKVVETLMARDELIDYCIVGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 165 SSRDVLGDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDNGNEFFPATSFQVSNINGGTGAG 244
Cdd:TIGR01246 161 SSVKKLGDVIKNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELTAIKWDEGNEFFPPTSLQITNIHAGTGAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 245 NVIPGELEVQFNFRFSTEVTHQQLQERVNAILQTHDLNYELSWIVNGLPFITEHGPLVDATVNAIKSVTGLTTNLETTGG 324
Cdd:TIGR01246 241 NVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLSGEPFLTNDGKLIDKAREAIEETNGIKPELSTGGG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 940685535 325 TSDGRFIAQTGAKVIELGPNNATIHKVDECVSTDDLIALADIYEQILEQL 374
Cdd:TIGR01246 321 TSDGRFIALMGAEVVEFGPVNATIHKVNECVSIEDLEKLSDVYQDLLENL 370
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
4-375 |
4.21e-125 |
|
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 365.36 E-value: 4.21e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 4 EVIALAQALIQRESVTPEDAGCQSMMNERLKALGFNIESLFFTDTL-NTWAR-KGNQS-PHFCFAGHTDVVPTGPAQNWQ 80
Cdd:COG0624 13 EALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVPPGRpNLVARrPGDGGgPTLLLYGHLDVVPPGDLELWT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 81 HPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGPFiNGTTKVIDTLeARGEKIDMCL 160
Cdd:COG0624 93 SDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGS-PGARALVEEL-AEGLKADAAI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 161 VGEPSSrdvlGDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDNG-NEFFPATSFQVSNING 239
Cdd:COG0624 171 VGEPTG----VPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDGRaDPLFGRTTLNVTGIEG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 240 GTgAGNVIPGELEVQFNFRFSTEVTHQQLQERVNAILQTH--DLNYELSWIVNGL-PFIT-EHGPLVDATVNAIKSVTGL 315
Cdd:COG0624 247 GT-AVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAapGVEVEVEVLGDGRpPFETpPDSPLVAAARAAIREVTGK 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940685535 316 TTNLETTGGTSDGRFIAQT-GAKVIELGP-NNATIHKVDECVSTDDLIALADIYEQILEQLL 375
Cdd:COG0624 326 EPVLSGVGGGTDARFFAEAlGIPTVVFGPgDGAGAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
7-371 |
4.40e-109 |
|
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: 323.87 E-value: 4.40e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 7 ALAQALIQRESVTPEDAGCQSMMNERLKALGFNIESLFFTDTLNTWARKGNQS-PHFCFAGHTDVVPTGPAQNWQHPPFS 85
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIVEGRGNLVATVGGGDgPVLLLNGHIDTVPPGDGDKWSFPPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 86 GLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGpFINGTTKVIDTLeaRGEKIDMCLVGEPS 165
Cdd:cd08659 81 GRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEV-GSDGARALLEAG--YADRLDALIVGEPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 166 srdvlGDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWD-NGNEFFPATSFQVSNINGGTGAg 244
Cdd:cd08659 158 -----GLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEElPAHPLLGPPTLNVGVINGGTQV- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 245 NVIPGELEVQFNFRFSTEVTHQQLQERVNAILQTHDLNYELSWIVNGLP--FITEHGPLVDATVNAIKSVTGlTTNLETT 322
Cdd:cd08659 232 NSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGDPpfFTDPDHPLVQALQAAARALGG-DPVVRPF 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 940685535 323 GGTSDGRFIAQT-GAKVIELGP-NNATIHKVDECVSTDDLIALADIYEQIL 371
Cdd:cd08659 311 TGTTDASYFAKDlGFPVVVYGPgDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
63-373 |
1.39e-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: 267.29 E-value: 1.39e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 63 CFAGHTDVVPTGPAQNWqhpPFSgLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDhKGSISFLITSDEEGPFiNGT 142
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFK-STEDGKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGGM-GGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 143 TKVIDTLEARGEKIDMCL---VGEPSS-RDVLGDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQT 218
Cdd:pfam01546 75 RALIEDGLLEREKVDAVFglhIGEPTLlEGGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 219 VWDNGNEFFPATsFQVSNINGGTGAGNVIPGELEVQFNFRFSTEVTHQQLQERVNAILQT----HDLNYELSWIVNGLPF 294
Cdd:pfam01546 155 VSRNVDPLDPAV-VTVGNITGIPGGVNVIPGEAELKGDIRLLPGEDLEELEERIREILEAiaaaYGVKVEVEYVEGGAPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 295 ITEHGPLVDATVNAIKSVTGLTTNLETTG--GTSDGRFIAQ-TGAKVIELGPNNATIHKVDECVSTDDLIALADIYEQIL 371
Cdd:pfam01546 234 LVNDSPLVAALREAAKELFGLKVELIVSGsmGGTDAAFFLLgVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLARLL 313
|
..
gi 940685535 372 EQ 373
Cdd:pfam01546 314 LK 315
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
1-374 |
1.53e-55 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 187.12 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 1 MTHEVIALAQALIQRESVTPEDAGCQSMMN---ERLKALGFNIESLFFTDTL---------NTWARKGNQSPHFCFAGHT 68
Cdd:PRK08651 4 MMFDIVEFLKDLIKIPTVNPPGENYEEIAEflrDTLEELGFSTEIIEVPNEYvkkhdgprpNLIARRGSGNPHLHFNGHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 69 DVVPTGPaqNWQ-HPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFvakNPDHKGSISFLITSDEE--GpfiNGTTKV 145
Cdd:PRK08651 84 DVVPPGE--GWSvNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERL---DPAGDGNIELAIVPDEEtgG---TGTGYL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 146 IDTLEARGekiDMCLVGEPSSrdvLGDVVkNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWD---N 222
Cdd:PRK08651 156 VEEGKVTP---DYVIVGEPSG---LDNIC-IGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTiksK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 223 GNEFFPATSFQVSNING----GTGAGNVIPGELEVQFNFRFSTEVTHQQLQERVNAILQT------HDLNYELSWIVNgl 292
Cdd:PRK08651 229 YEYDDERGAKPTVTLGGptveGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEvapelgIEVEFEITPFSE-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 293 PFITEHG-PLVDATVNAIKSVTGLTTNLETTGGTSDGRFIAQTGAKVIELGPNN-ATIHKVDECVSTDDLIALADIYEQI 370
Cdd:PRK08651 307 AFVTDPDsELVKALREAIREVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPGElELAHAPDEYVEVKDVEKAAKVYEEV 386
|
....
gi 940685535 371 LEQL 374
Cdd:PRK08651 387 LKRL 390
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
31-372 |
3.45e-54 |
|
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: 182.79 E-value: 3.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 31 ERLKALGFNIESLFFTDT--LNTWARKG-NQSPHFCFAGHTDVVPTgPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAA 107
Cdd:cd03894 26 DYLAALGVKSRRVPVPEGgkANLLATLGpGGEGGLLLSGHTDVVPV-DGQKWSSDPFTLTERDGRLYGRGTCDMKGFLAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 108 MLVATERFVAKNPdhKGSISFLITSDEEGPFInGTTKVIDTLEARGEKIDMCLVGEPSSRDVLgdVVKNGRRGSLTgflK 187
Cdd:cd03894 105 VLAAVPRLLAAKL--RKPLHLAFSYDEEVGCL-GVRHLIAALAARGGRPDAAIVGEPTSLQPV--VAHKGIASYRI---R 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 188 VKGVQGHVAYPHLAQNPIHLAAPAITELSQTV--WDNG--NEFF--PATSFQVSNINGGTGAgNVIPGELEVQFNFRF-- 259
Cdd:cd03894 177 VRGRAAHSSLPPLGVNAIEAAARLIGKLRELAdrLAPGlrDPPFdpPYPTLNVGLIHGGNAV-NIVPAECEFEFEFRPlp 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 260 --STEVTHQQLQERVNAILQTHDLNYELSWIVNGLPFITEHGplvDATVNAIKSVTGLTTNLETTGGTsDGRFIAQTGAK 337
Cdd:cd03894 256 geDPEAIDARLRDYAEALLEFPEAGIEVEPLFEVPGLETDED---APLVRLAAALAGDNKVRTVAYGT-EAGLFQRAGIP 331
|
330 340 350
....*....|....*....|....*....|....*.
gi 940685535 338 VIELGPNN-ATIHKVDECVSTDDLIALADIYEQILE 372
Cdd:cd03894 332 TVVCGPGSiAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
6-366 |
6.60e-54 |
|
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 182.21 E-value: 6.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 6 IALAQALIQRESVTP---EDAGCQSMMNERLKALGFNIESLFFTDTLNTWARK--------GNQsPHFCFAGHTDVVPTG 74
Cdd:TIGR01910 1 VELLKDLISIPSVNPpggNEETIANYIKDLLREFGFSTDVIEITDDRLKVLGKvvvkepgnGNE-KSLIFNGHYDVVPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 75 PAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEgpfiNGTTKVIDTLEARGE 154
Cdd:TIGR01910 80 DLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEE----SGEAGTLYLLQRGYF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 155 K-IDMCLVGEPSSrdvlGDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTV--WDNGNE--FFP- 228
Cdd:TIGR01910 156 KdADGVLIPEPSG----GDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEehIYARNSygFIPg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 229 ATSFQVSNINGGTGAgNVIPGELEVQFNFRFSTEVTHQQLQERVNAIL----QTHDLNYELSWIVN--GLPFITEHGPLV 302
Cdd:TIGR01910 232 PITFNPGVIKGGDWV-NSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVkalsKSDGWLYENEPVVKwsGPNETPPDSRLV 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940685535 303 DATVNAIKSVTGLTTNLETTGGTSDGRFIAQTGAKVIELGP-NNATIHKVDECVSTDDLIALADI 366
Cdd:TIGR01910 311 KALEAIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPgDLETAHQVNEYISIKNLVESTKV 375
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-368 |
1.01e-50 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349933 [Multi-domain] Cd Length: 355 Bit Score: 173.34 E-value: 1.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 6 IALAQALIQRESVTPEDAGCQSMMN---ERLKALGFNIESLFFTDTLNTW---ARKGNQSPHFCFAGHTDVVPTGPAQNW 79
Cdd:cd08011 1 VKLLQELVQIPSPNPPGDNTSAIAAyikLLLEDLGYPVELHEPPEEIYGVvsnIVGGRKGKRLLFNGHYDVVPAGDGEGW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 80 QHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFV-AKNPDHkGSISFLITSDEEGPFINGTTKVIDTLEARGekiDM 158
Cdd:cd08011 81 TVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLAdAKAPWD-LPVVLTFVPDEETGGRAGTKYLLEKVRIKP---ND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 159 CLVGEPSSrdvlGDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVwdngneffpaTSFQVSNIN 238
Cdd:cd08011 157 VLIGEPSG----SDNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELE----------KTVNPGVIK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 239 GGTGAgNVIPGELEVQFNFRFSTEVTHQQLQERVNAILqthDLNYELSWIVNGLPFITEHGP---LVDATVNAIKSVTGL 315
Cdd:cd08011 223 GGVKV-NLVPDYCEFSVDIRLPPGISTDEVLSRIIDHL---DSIEEVSFEIKSFYSPTVSNPdseIVKKTEEAITEVLGI 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 940685535 316 TTNLETTGGTSDGRFIAQTGAKVIELGPNN-ATIHKVDECVSTDDLIALADIYE 368
Cdd:cd08011 299 RPKEVISVGASDARFYRNAGIPAIVYGPGRlGQMHAPNEYVEIDELIKVIKVHA 352
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
56-375 |
5.46e-40 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 145.41 E-value: 5.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 56 GNQSPHFCFAGHTDVVPTGPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEE 135
Cdd:PRK08588 56 GSGSPVLALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 136 gpfingttkvIDTLEARG--EK-----IDMCLVGEPSsrdvlGDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLA 208
Cdd:PRK08588 136 ----------VGELGAKQltEKgyaddLDALIIGEPS-----GHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 209 APAITELSQTVWD--NGNEFFPATSFQVSNINGGTGAgNVIPGELEVQFNFRFSTEVTHQQLQERVNAIL----QTHDLN 282
Cdd:PRK08588 201 LEFYNEQKEYFDSikKHNPYLGGLTHVVTIINGGEQV-NSVPDEAELEFNIRTIPEYDNDQVISLLQEIInevnQNGAAQ 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 283 YELSWIVNGLPFITE-HGPLVDATVNAIKSVTGLTTNLETTGGTSDGRFIAQTGAK--VIELGP-NNATIHKVDECVSTD 358
Cdd:PRK08588 280 LSLDIYSNHRPVASDkDSKLVQLAKDVAKSYVGQDIPLSAIPGATDASSFLKKKPDfpVIIFGPgNNLTAHQVDEYVEKD 359
|
330
....*....|....*..
gi 940685535 359 DLIALADIYEQILEQLL 375
Cdd:PRK08588 360 MYLKFIDIYKEIIIQYL 376
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
66-276 |
2.98e-38 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 141.09 E-value: 2.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 66 GHTDVVPTGpAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVA---KNPDHkgsisFLITSDEEGpfinGT 142
Cdd:PRK07522 71 GHTDVVPVD-GQAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAaplRRPLH-----LAFSYDEEV----GC 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 143 TKV---IDTLEARGEKIDMCLVGEPSS-RDVLGDVVKNGRRgsltgfLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQ- 217
Cdd:PRK07522 141 LGVpsmIARLPERGVKPAGCIVGEPTSmRPVVGHKGKAAYR------CTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDl 214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940685535 218 ----TVWDNGNEFF--PATSFQVSNINGGTgAGNVIPGELEVQFNFR----FSTEVTHQQLQERVNAIL 276
Cdd:PRK07522 215 adrlAAPGPFDALFdpPYSTLQTGTIQGGT-ALNIVPAECEFDFEFRnlpgDDPEAILARIRAYAEAEL 282
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
5-353 |
6.98e-36 |
|
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.
Pssm-ID: 349881 [Multi-domain] Cd Length: 362 Bit Score: 134.26 E-value: 6.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 5 VIALAQALIQRESVTPEDAG---CQSMMNERLKALGFNIESLFFTDTLNT--WARKGNQSPHFCFAGHTDVV-PTGPAQN 78
Cdd:cd03885 1 MLDLLERLVNIESGTYDKEGvdrVAELLAEELEALGFTVERRPLGEFGDHliATFKGTGGKRVLLIGHMDTVfPEGTLAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 79 WqhpPFSglIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEE-GPFINGttkviDTLEARGEKID 157
Cdd:cd03885 81 R---PFT--VDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEiGSPGSR-----ELIEEEAKGAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 158 MCLVGEPSSRDvlGDVVKnGRRGSLTGFLKVKGVQGHVayphlAQNPIhLAAPAITELSQTVWD--NGNEFFPATSFQVS 235
Cdd:cd03885 151 YVLVFEPARAD--GNLVT-ARKGIGRFRLTVKGRAAHA-----GNAPE-KGRSAIYELAHQVLAlhALTDPEKGTTVNVG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 236 NINGGTGAgNVIPGELEVQFNFRFSTEVTHQQLQERVNAILQTHDL---NYELSWIVNGLPF-ITEHGPLVDATVNAIKS 311
Cdd:cd03885 222 VISGGTRV-NVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTLVpgtSVELTGGLNRPPMeETPASRRLLARAQEIAA 300
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 940685535 312 VTGLTTNLETTGGTSDGRFIAQTGAKVIE-LGPNNATIHKVDE 353
Cdd:cd03885 301 ELGLTLDWEATGGGSDANFTAALGVPTLDgLGPVGGGAHTEDE 343
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
4-376 |
1.16e-31 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 124.10 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 4 EVIALAQALIQRESVTP---EDAGCQSMMNERLKALGFNIESLFF------TDTLNTW---ARKGNQSPHFC--FAGHTD 69
Cdd:PRK13013 15 DLVALTQDLIRIPTLNPpgrAYREICEFLAARLAPRGFEVELIRAegapgdSETYPRWnlvARRQGARDGDCvhFNSHHD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 70 VVPTGpaQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGPFINGTTKVIDTL 149
Cdd:PRK13013 95 VVEVG--HGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGGFGGVAYLAEQG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 150 EARGEKIDMCLVGEPSSRdvlgDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPI-HLAApAITELSQtvwdngnEFFP 228
Cdd:PRK13013 173 RFSPDRVQHVIIPEPLNK----DRICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIrHMGA-VLAEIEE-------RLFP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 229 A-----TSFQVS---------NINGGTGAGNV------------IPGELEVQFNFRFSTEVTHQQLQERVNAILQT---- 278
Cdd:PRK13013 241 LlatrrTAMPVVpegarqstlNINSIHGGEPEqdpdytglpapcVADRCRIVIDRRFLIEEDLDEVKAEITALLERlkra 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 279 -HDLNYELSWIVNGLPFITEHG-PLVDATVNAIKSVTGLTTNLETTGGTSDGRFIAQTGA--KVIELGPNNATI-HKVDE 353
Cdd:PRK13013 321 rPGFAYEIRDLFEVLPTMTDRDaPVVRSVAAAIERVLGRQADYVVSPGTYDQKHIDRIGKlkNCIAYGPGILDLaHQPDE 400
|
410 420
....*....|....*....|...
gi 940685535 354 CVSTDDLIALADIYEQILEQLLT 376
Cdd:PRK13013 401 WVGIADMVDSAKVMALVLADLLA 423
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
4-375 |
1.92e-31 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 122.74 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 4 EVIALAQALIQRESVTPEDAGCQSMMNERLKALGFNiesLFFTDTL-NTWARKGNQSPHFCFAGHTDVVPTGPAQNWQHP 82
Cdd:PRK13004 16 DMTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFD---KVEIDPMgNVLGYIGHGKKLIAFDAHIDTVGIGDIKNWDFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 83 PFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEgpfingttkVIDTL------EARGEKI 156
Cdd:PRK13004 93 PFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEE---------DCDGLcwryiiEEDKIKP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 157 DMCLVGEPSSRDvlgdvVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDNGN-EFFPATSFQVS 235
Cdd:PRK13004 164 DFVVITEPTDLN-----IYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELNPNLKEdPFLGKGTLTVS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 236 NINGGTGAGNVIPGELEVQFNFRFSTEVTHQQLQERVNAILQTHDLNYELSWIV------NGLPFITEH----------G 299
Cdd:PRK13004 239 DIFSTSPSRCAVPDSCAISIDRRLTVGETWESVLAEIRALPAVKKANAKVSMYNydrpsyTGLVYPTECyfptwlypedH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 300 PLVDATVNAIKSVTGLTT-----NLETTGGTSDGRFiaqtGAKVIELGPNNATI-HKVDECVSTDDLIALADIYEQILEQ 373
Cdd:PRK13004 319 EFVKAAVEAYKGLFGKAPevdkwTFSTNGVSIAGRA----GIPTIGFGPGKEPLaHAPNEYTWKEQLVKAAAMYAAIPKS 394
|
..
gi 940685535 374 LL 375
Cdd:PRK13004 395 LL 396
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
3-374 |
5.74e-30 |
|
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349904 [Multi-domain] Cd Length: 343 Bit Score: 117.84 E-value: 5.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 3 HEVIALAQALIQRESVTPEDAGCQSMMNERLKALGFNiesLFFTDTLNTWARKGNQSPHFCFAGHTDVVPtGPAqnwqhP 82
Cdd:cd05653 1 QDAVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLE---AWVDEAGNAVGGAGSGPPDVLLLGHIDTVP-GEI-----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 83 PfsgLIEDGLLHGRGAADMKGSLAAMLVATerfVAKNPDHKGSISFLITSDEEgpfinGTTKVIDTLEARGEKIDMCLVG 162
Cdd:cd05653 72 V---RVEGGVLYGRGAVDAKGPLAAMILAA---SALNEELGARVVVAGLVDEE-----GSSKGARELVRRGPRPDYIIIG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 163 EPSSRDvlGDVVknGRRGSLTGFLKVKGVQGHVAYPhlAQNPIHLAAPAITELSQTVWDNGNEFFPATSFQVSNINGGTg 242
Cdd:cd05653 141 EPSGWD--GITL--GYRGSLLVKIRCEGRSGHSSSP--ERNAAEDLIKKWLEVKKWAEGYNVGGRDFDSVVPTLIKGGE- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 243 AGNVIPGELEVQFNFRFStevtHQQLQERVNAILQTHDLNYELSWIVNGLPFITE-HGPLVDATVNAIKSvTGLTTNLET 321
Cdd:cd05653 214 SSNGLPQRAEATIDLRLP----PRLSPEEAIALATALLPTCELEFIDDTEPVKVSkNNPLARAFRRAIRK-QGGKPRLKR 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 940685535 322 TGGTSDGRFIAQTGAKVI-ELGPNNATI-HKVDECVSTDDLIALADIYEQILEQL 374
Cdd:cd05653 289 KTGTSDMNVLAPLWTVPIvAYGPGDSTLdHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
176-284 |
1.56e-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: 109.74 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 176 NGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDNGNeFFPATSFQVSNINGGTgAGNVIPGELEVQF 255
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGF-DFPRTTLNITGIEGGT-ATNVIPAEAEAKF 78
|
90 100
....*....|....*....|....*....
gi 940685535 256 NFRFSTEVTHQQLQERVNAILQTHDLNYE 284
Cdd:pfam07687 79 DIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
49-374 |
2.60e-29 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 118.12 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 49 LNTWARKGNQSPHFCFAGHTDVVPTGPA--QNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSI 126
Cdd:PRK08262 101 LYTWKGSDPSLKPIVLMAHQDVVPVAPGteGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 127 SFLITSDEE--GPfinGTTKVIDTLEARGEKIDMCL-VGEPSSRDVLGDVVKN------GRRGSLTGFLKVKGVQGHVAY 197
Cdd:PRK08262 181 YLAFGHDEEvgGL---GARAIAELLKERGVRLAFVLdEGGAITEGVLPGVKKPvaligvAEKGYATLELTARATGGHSSM 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 198 P--------------HLAQNP------------IHLAAPAITELSQTVWDNGNEFFPA----------------TSFQVS 235
Cdd:PRK08262 258 PprqtaigrlaraltRLEDNPlpmrlrgpvaemFDTLAPEMSFAQRVVLANLWLFEPLllrvlakspetaamlrTTTAPT 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 236 NINGGTGAgNVIPGELEVQFNFRFSTEVTHQQLQERV-NAIlqtHDLNYELSWivngLPFITEHGP----------LVDA 304
Cdd:PRK08262 338 MLKGSPKD-NVLPQRATATVNFRILPGDSVESVLAHVrRAV---ADDRVEIEV----LGGNSEPSPvsstdsaaykLLAA 409
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940685535 305 TVNAIKSVTGLTTNLeTTGGTsDGRFIAQTGAKV-----IELGPNN-ATIHKVDECVSTDDLIALADIYEQILEQL 374
Cdd:PRK08262 410 TIREVFPDVVVAPYL-VVGAT-DSRHYSGISDNVyrfspLRLSPEDlARFHGTNERISVANYARMIRFYYRLIENA 483
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-298 |
5.17e-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: 115.06 E-value: 5.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 5 VIALAQALIQRESVTPEDAGCQSMMNERLKALGFNIESLF--FTDTLNTWARKGNQ-SPHFCFAGHTDVVPtgPaqnwqH 81
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEKQPveNKDRFNVYAYPGSSrQPRVLLTSHIDTVP--P-----F 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 82 PPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEgpfiNGTTKVIDTLEARGEKIDMCLV 161
Cdd:cd05652 74 IPYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEE----TGGDGMKAFNDLGLNTWDAVIF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 162 GEPSSRDvLGdvvkNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDnGNEFFPATSFQVSNINGGT 241
Cdd:cd05652 150 GEPTELK-LA----SGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLP-SSELLGPTTLNIGRISGGV 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 940685535 242 gAGNVIPGELEVQFNFRFSTEV--THQQLQERVNAILQTHDlNYELSWIVNGLPFITEH 298
Cdd:cd05652 224 -AANVVPAAAEASVAIRLAAGPpeVKDIVKEAVAGILTDTE-DIEVTFTSGYGPVDLDC 280
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-361 |
1.37e-27 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 112.02 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 7 ALAQALIQRESVTPEDAGCQSMMNERLKALGF-------NIESL-----------FFTDTLNTWARKGNQSP---HFCFA 65
Cdd:cd03895 1 AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYtvdrweiDVEKLkhhpgfspvavDYAGAPNVVGTHRPRGEtgrSLILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 66 GHTDVVPTGPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEE--GpfiNGTt 143
Cdd:cd03895 81 GHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEEctG---NGA- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 144 kvIDTLEaRGEKIDMCLVGEPSsrdvlGDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQ--TVWD 221
Cdd:cd03895 157 --LAALM-RGYRADAALIPEPT-----ELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQEleREWN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 222 NGNEFFPATS-------FQVSNINGGTGAGNViPGELEVQFNFRF----STEVTHQQLQERVNAILQTH----DLNYELS 286
Cdd:cd03895 229 ARKKSHPHFSdhphpinFNIGKIEGGDWPSSV-PAWCVLDCRIGIypgeSPEEARREIEECVADAAATDpwlsNHPPEVE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 287 WivNGLPF----ITEHGPLVDATVNAIKSVTGLTTNLETTGGTSDGRFIAQTGA-KVIELGPNNATIHKVDECVSTDDLI 361
Cdd:cd03895 308 W--NGFQAegyvLEPGSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYGDiPALCYGPGSRDAHGFDESVDLESLR 385
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
6-360 |
4.97e-27 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 110.86 E-value: 4.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 6 IALAQALIQRESVTPEDAGCQSMMNERLKALGFNIE------------------SLFFTDTLN---TWARKGNQSPHFCF 64
Cdd:PRK06837 23 VAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDrwsidpddlkshpgagpvEIDYSGAPNvvgTYRPAGKTGRSLIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 65 AGHTDVVPTGPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEE--GpfiNGT 142
Cdd:PRK06837 103 QGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSVIEEEstG---NGA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 143 tkvIDTLeARGEKIDMCLVGEPssrdvLGDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQ--TVW 220
Cdd:PRK06837 180 ---LSTL-QRGYRADACLIPEP-----TGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALREleAEW 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 221 DN---GNEFFPA----TSFQVSNINGGTGAGNViPGELEVQFNFRFSTEVTHQ----QLQERVNAILQTHdlnyelSWIV 289
Cdd:PRK06837 251 NArkaSDPHFEDvphpINFNVGIIKGGDWASSV-PAWCDLDCRIAIYPGVTAAdaqaEIEACLAAAARDD------RFLS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 290 NGLPFITEHG------------PLVDATVNAIKSVTGLTTNLETTGGTSDGRFIAQT-GAKVIELGPNNATIHKVDECVS 356
Cdd:PRK06837 324 NNPPEVVWSGflaegyvlepgsEAEAALARAHAAVFGGPLRSFVTTAYTDTRFYGLYyGIPALCYGPSGEGIHGFDERVD 403
|
....
gi 940685535 357 TDDL 360
Cdd:PRK06837 404 LESV 407
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
5-371 |
6.41e-27 |
|
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349899 [Multi-domain] Cd Length: 347 Bit Score: 109.45 E-value: 6.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 5 VIALAQALIQRESVTPEDAgcqSMMNERLKALGFN--IESLFFTDTLntWARKG-NQSPHFCFAGHTDVVPTgpAQNWQh 81
Cdd:cd05647 1 PIELTAALVDIPSVSGNEK---PIADEIEAALRTLphLEVIRDGNTV--VARTErGLASRVILAGHLDTVPV--AGNLP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 82 ppfSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHkgSISFLITSDEEGPF-INGTTKVIdtlEARGE--KIDM 158
Cdd:cd05647 73 ---SRVEEDGVLYGCGATDMKAGDAVQLKLAATLAAATLKH--DLTLIFYDCEEVAAeLNGLGRLA---EEHPEwlAADF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 159 CLVGEPSSRDVLGdvvknGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSqtvwdngnEFFPATsfqvSNIN 238
Cdd:cd05647 145 AVLGEPTDGTIEG-----GCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLA--------AYEPRT----VNID 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 239 G-------------GTGAGNVIPGELEVQFNFRFSTEVTHQQLQERVNAILQTHDLNYELSWIVNG-LPFITEhgPLVDA 304
Cdd:cd05647 208 GltyreglnavfisGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLGYEIEVTDLSPGaLPGLDH--PVARD 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940685535 305 TVNAIKSvtgltTNLETTGGTSDGRFiAQTGAKVIELGPNNATI-HKVDECVSTDDLIALADIYEQIL 371
Cdd:cd05647 286 LIEAVGG-----KVRAKYGWTDVARF-SALGIPAVNFGPGDPLLaHKRDEQVPVEQITACAAILRRWL 347
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
4-371 |
8.54e-27 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349902 [Multi-domain] Cd Length: 341 Bit Score: 108.94 E-value: 8.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 4 EVIALAQALIQRESVTPEDAGCQSMMNERLKALGFNIESLFFtdtlNTWARKGN---QSPHFCFAGHTDVVPtgPAQNWQ 80
Cdd:cd05651 1 EAIELLKSLIATPSFSREEHKTADLIENYLEQKGIPFKRKGN----NVWAENGHfdeGKPTLLLNSHHDTVK--PNAGWT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 81 HPPFSGLIEDGLLHGRGAADMKGSLAAMLvATERFVAKNPDHKGSISFLITSDEEgpfINGTTKVIDTLEARGeKIDMCL 160
Cdd:cd05651 75 KDPFEPVEKGGKLYGLGSNDAGASVVSLL-ATFLHLYSEGPLNYNLIYAASAEEE---ISGKNGIESLLPHLP-PLDLAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 161 VGEPSSRDvlgdvVKNGRRGSLTGFLKVKGVQGHVAYPHlAQNPIHLAAPAITELSQTVWDNGNEFFPATSFQVSNINGG 240
Cdd:cd05651 150 VGEPTEMQ-----PAIAEKGLLVLDCTARGKAGHAARNE-GDNAIYKALDDIQWLRDFRFDKVSPLLGPVKMTVTQINAG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 241 TgAGNVIPGE----LEVQFNFRFSTEVTHQQLQERVNAILQTHDLNYELSwivnglpFITEHGPLVDATVNAIKSVTGLT 316
Cdd:cd05651 224 T-QHNVVPDSctfvVDIRTTEAYTNEEIFEIIRGNLKSEIKPRSFRLNSS-------AIPPDHPIVQAAIAAGRTPFGSP 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 940685535 317 TnlettggTSDGRFIAQTGAKvieLGPNNAT-IHKVDECVSTDDLIALADIYEQIL 371
Cdd:cd05651 296 T-------LSDQALMPFPSVK---IGPGDSSrSHTADEFIELSEIEEGIDIYIELL 341
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
20-374 |
5.67e-23 |
|
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: 99.10 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 20 PEDAGCQSMMNERLKALGFNIESLFFTD----TLNTWARKGNQSPHFCFAGHTDVVPTGPaQNWQHPPFSGLI-EDGLLH 94
Cdd:TIGR01880 28 PDYAACVDFLIKQADELGLARKTIEFVPgkpvVVLTWPGSNPELPSILLNSHTDVVPVFR-EHWTHPPFSAFKdEDGNIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 95 GRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGPFINGTTKVIDTLEARGEKIDMCL-VGEPSSRDVLgdV 173
Cdd:TIGR01880 107 ARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGMEKFAKTDEFKALNLGFALdEGLASPDDVY--R 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 174 VKNGRRGSLTGFLKVKGVQGHVA--YPHLAQNPIHLAAPAITELSQTVWD---NGNEFF--PATSFQVSNINGGTgAGNV 246
Cdd:TIGR01880 185 VFYAERVPWWVVVTAPGNPGHGSklMENTAMEKLEKSVESIRRFRESQFQllqSNPDLAigDVTSVNLTKLKGGV-QSNV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 247 IPGELEVQFNFRFST----EVTHQQLQERVNAILQTHDLNYELSWivnGLPFITEH---GPLVDATVNAIKSVtGLTTNL 319
Cdd:TIGR01880 264 IPSEAEAGFDIRLAPsvdfEEMENRLDEWCADAGEGVTYEFSQHS---GKPLVTPHddsNPWWVAFKDAVKEM-GCTFKP 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 940685535 320 ETTGGTSDGRFIAQTGAKVIELGPNNAT---IHKVDECVSTDDLIALADIYEQILEQL 374
Cdd:TIGR01880 340 EILPGSTDSRYIRAAGVPALGFSPMNNTpvlLHDHNEFLNEAVFLRGIEIYQTLISAL 397
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
8-371 |
1.18e-22 |
|
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: 98.59 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 8 LAQALIQRESVTPEDAGCQS-----MMNERLKALGFNIESLFFTDT---LNTWARKGNQSPH---FCFAGHTDVVPTGPA 76
Cdd:cd05675 3 LLQELIRIDTTNSGDGTGSEtraaeVLAARLAEAGIQTEIFVVESHpgrANLVARIGGTDPSagpLLLLGHIDVVPADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 77 qNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGPFINGTTKVIDTLEARGEKI 156
Cdd:cd05675 83 -DWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWLVDNHPELFDGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 157 DMCL-------VGEPSSRDVLgdVVKNGRRGSLTGFLKVKGVQGHVAYPHlAQNPIHLAAPAITELSQTVWDngNEFFPA 229
Cdd:cd05675 162 TFALneggggsLPVGKGRRLY--PIQVAEKGIAWMKLTVRGRAGHGSRPT-DDNAITRLAEALRRLGAHNFP--VRLTDE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 230 TSF--QVSNINGGTG------------------------------------------AGNVIPGELEVQFNFRFSTEVTH 265
Cdd:cd05675 237 TAYfaQMAELAGGEGgalmltavpvldpalaklgpsapllnamlrntasptmldagyATNVLPGRATAEVDCRILPGQSE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 266 QQLQERVNAILQTHDLNYELSWIVNGLPfitehGPLVDATVNAIKSVT------GLTTNLETTGGTsDGRFIAQTGAK-- 337
Cdd:cd05675 317 EEVLDTLDKLLGDPDVSVEAVHLEPATE-----SPLDSPLVDAMEAAVqavdpgAPVVPYMSPGGT-DAKYFRRLGIPgy 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 940685535 338 ---VIELGPNNAT---IHKVDECVSTDDLIALADIYEQIL 371
Cdd:cd05675 391 gfaPLFLPPELDYtglFHGVDERVPVESLYFGVRFLDRLV 430
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
1-375 |
1.89e-22 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 97.80 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 1 MTHEVIALAQALIQRESVTP---EDAGCQSMMNERLKALGFNI--ESLFFTDTLNTWARKGNQSPHF---CFAGHTDVVP 72
Cdd:PRK08596 11 RKDELLELLKTLVRFETPAPparNTNEAQEFIAEFLRKLGFSVdkWDVYPNDPNVVGVKKGTESDAYkslIINGHMDVAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 73 TGPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFL-ITSDEEGPfiNGTTKVIDtlea 151
Cdd:PRK08596 91 VSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQsVIGEEVGE--AGTLQCCE---- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 152 RGEKIDMCLVGEPSSRDVLgdvvknGRRGSLTGFLKVKGVQGHvaypH--LAQNPIH-----LAAPAITELSQTV----- 219
Cdd:PRK08596 165 RGYDADFAVVVDTSDLHMQ------GQGGVITGWITVKSPQTF----HdgTRRQMIHaggglFGASAIEKMMKIIqslqe 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 220 ----WD--NGNEFFP--ATSFQVSNINGGTGAGnVIPGELEVQFNFRFSTEVTHQQ----LQERVNAI------LQTHDL 281
Cdd:PRK08596 235 lerhWAvmKSYPGFPpgTNTINPAVIEGGRHAA-FIADECRLWITVHFYPNETYEQvikeIEEYIGKVaaadpwLRENPP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 282 NYElsW-----------IVNGLPFITEHgPLVDATVNAIKSVTGLTTNLETTGGTSDGRFIAQTGAKVIELGPNNAT-IH 349
Cdd:PRK08596 314 QFK--WggesmiedrgeIFPSLEIDSEH-PAVKTLSSAHESVLSKNAILDMSTTVTDGGWFAEFGIPAVIYGPGTLEeAH 390
|
410 420
....*....|....*....|....*.
gi 940685535 350 KVDECVSTDDLIAladiYEQILEQLL 375
Cdd:PRK08596 391 SVNEKVEIEQLIE----YTKVITAFI 412
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-372 |
4.27e-22 |
|
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: 96.34 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 6 IALAQALIQRESVTPEDAGCQSMMNERLKALGFNIESLfftDTL-NTWARKGNQSPHFCFAGHTDVVPTGPAQNWQHPPF 84
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGFDEVEI---DPMgNVIGYIGGGKKKILFDGHIDTVGIGNIDNWKFDPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 85 SGLIEDGLLHGRGAADMKGSLAAMlVATERFVAK--NPDHKGSISFLITSDEEgpfingttkVIDTLEAR------GEKI 156
Cdd:cd05649 78 EGYETDGKIYGRGTSDQKGGLASM-VYAAKIMKDlgLRDFAYTILVAGTVQEE---------DCDGVCWQyiskadKIKP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 157 DMCLVGEPSSrdvLGdvVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDNG-NEFFPATSFQVS 235
Cdd:cd05649 148 DFVVSGEPTD---GN--IYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFPeAPFLGRGTLTVT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 236 NINGGTGAGNVIPGELEVQFNFRFST-EVTHQQLQERVNAILQTHD--------LNY-ELSWIVNGLP--------FITE 297
Cdd:cd05649 223 DIFSTSPSRCAVPDSCRISIDRRLTVgETWEGCLEEIRALPAVKKYgddvavsmYNYdRPSYTGEVYEseryfptwLLPE 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940685535 298 HGPLVDATVNAIKSVTGLTTNLETTGGTSDGRFIA-QTGAKVIELGPN-NATIHKVDECVSTDDLIALADIYEQILE 372
Cdd:cd05649 303 DHELVKALLEAYKALFGARPLIDKWTFSTNGVSIMgRAGIPCIGFGPGaENQAHAPNEYTWKEDLVRCAAGYAAIPT 379
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
64-373 |
4.65e-22 |
|
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: 96.39 E-value: 4.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 64 FAGHTDVVPTgpaQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERfvAKNPDHKGSISFLITSDEEGPFInGTT 143
Cdd:cd08013 73 LNGHIDTVTL---DGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALAD--AKEAGLRGDVILAAVADEEDASL-GTQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 144 KVIdtleARGEKIDMCLVGEPSSRdvlgdVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITEL----SQTV 219
Cdd:cd08013 147 EVL----AAGWRADAAIVTEPTNL-----QIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALeeyqQELP 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 220 WDNGNEFFPATSFQVSNINGGTGAgNVIPGELEVQFNFRFSTEVTHQQLQERVNAIL----QTH-DLNYELSWIV-NGLP 293
Cdd:cd08013 218 ERPVDPLLGRASVHASLIKGGEEP-SSYPARCTLTIERRTIPGETDESVLAELTAILgelaQTVpNFSYREPRITlSRPP 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 294 FI--TEHgPLVDATVNAIKSVTGLTTNLETTGGTSDGRFIAQTGAKVIELGPNNATIHKVDECVSTDDLIALADIYEQIL 371
Cdd:cd08013 297 FEvpKEH-PFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAGIPSVVFGPSGAGLHAKEEWVDVESIRQLREVLSAVV 375
|
..
gi 940685535 372 EQ 373
Cdd:cd08013 376 RE 377
|
|
| PRK06915 |
PRK06915 |
peptidase; |
4-194 |
5.74e-22 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 96.30 E-value: 5.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 4 EVIALAQALIQRESVTPEDAGCQSMMNERLKALGFNIE------------SLF------FTDTLNTWARK----GNQSph 61
Cdd:PRK06915 18 EAVKLLKRLIQEKSVSGDESGAQAIVIEKLRELGLDLDiwepsfkklkdhPYFvsprtsFSDSPNIVATLkgsgGGKS-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 62 FCFAGHTDVVPTGPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEgpfiNG 141
Cdd:PRK06915 96 MILNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEE----SG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 940685535 142 TTKVIDTLEaRGEKIDMCLVGEPSSRDVLgdvVKngRRGSLTGFLKVKGVQGH 194
Cdd:PRK06915 172 GAGTLAAIL-RGYKADGAIIPEPTNMKFF---PK--QQGSMWFRLHVKGKAAH 218
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
66-371 |
1.38e-21 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 94.83 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 66 GHTDVVPTGPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEgpfINGTTKV 145
Cdd:cd05650 76 SHLDTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEE---DGSEYGI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 146 IDTLEARG--EKIDMCLVgePSSRDVLGDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTV---W 220
Cdd:cd05650 153 QYLLNKFDlfKKDDLIIV--PDFGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNFALELDELLhekF 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 221 DNGNEFF--PATSFQVSNINGGTGAGNVIPGELEVQFNFR----FSTEVTHQQLQERVNAILQTHDLNYELSWIV--NGL 292
Cdd:cd05650 231 DEKDDLFnpPYSTFEPTKKEANVPNVNTIPGYDVFYFDCRvlptYKLDEVLKFVNKIISDFENSYGAGITYEIVQkeQAP 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940685535 293 PFITEHGPLVDATVNAIKSVTGLTTNLETTGGTSDGRFIAQTGAKVIELGPNNATIHKVDECVSTDDLIALADIYEQIL 371
Cdd:cd05650 311 PATPEDSEIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYIRISHIVKDAKVFAEML 389
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
66-367 |
3.59e-21 |
|
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: 94.23 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 66 GHTDVVPTGPaqNWQHPPFSGLIEDGLLHGRGAADMKG-SLAAML----------------------------VATERFV 116
Cdd:cd03888 78 GHLDVVPAGE--GWTTDPFKPVIKDGKLYGRGTIDDKGpTIAALYalkilkdlglplkkkirlifgtdeetgwKCIEHYF 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 117 AKN--------PD--------HKGSISFLITSdeegPFINGTTKVI-------------DTLEARGEKIDMCLVGEPSSR 167
Cdd:cd03888 156 EHEeypdfgftPDaefpvingEKGIVTVDLTF----KIDDDKGYRLisikggeatnmvpDKAEAVIPGKDKEELALSAAT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 168 DVLGDVVKNGRRGSLTgflkVKGVQGHVAYPHLAQNPI------------HLAAPAITELSQTVW---DNGNEFFPATSF 232
Cdd:cd03888 232 DLKGNIEIDDGGVELT----VTGKSAHASAPEKGVNAItllakflaelnkDGNDKDFIKFLAKNLhedYNGKKLGINFED 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 233 QVS-----NInggtGAGNVIPGELEVQFNFRFSTEVTHQQLQERVNAILQTHDLNYELSWIVNGLpFITEHGPLVDATVN 307
Cdd:cd03888 308 EVMgeltlNP----GIITLDDGKLELGLNVRYPVGTSAEDIIKQIEEALEKYGVEVEGHKHQKPL-YVPKDSPLVKTLLK 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940685535 308 AIKSVTGLTTNLETTGGTSDGRFIAqtgaKVIELGP----NNATIHKVDECVSTDDLIALADIY 367
Cdd:cd03888 383 VYEEQTGKEGEPVAIGGGTYARELP----NGVAFGPefpgQKDTMHQANEFIPIDDLIKALAIY 442
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
4-371 |
6.01e-21 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 93.37 E-value: 6.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 4 EVIALAQALIQRESVTPEDAG------CQSMMnERLKALGFN-IESLFFTDTLNTW-------AR--KGNQSPHFCFAGH 67
Cdd:PRK13983 6 EMIELLSELIAIPAVNPDFGGegekekAEYLE-SLLKEYGFDeVERYDAPDPRVIEgvrpnivAKipGGDGKRTLWIISH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 68 TDVVPTGPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEgpfiNGTTKVID 147
Cdd:PRK13983 85 MDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEE----TGSKYGIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 148 TL-EARGE---KIDMCLVGEPSSRDvlGDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTV---W 220
Cdd:PRK13983 161 YLlKKHPElfkKDDLILVPDAGNPD--GSFIEIAEKSILWLKFTVKGKQCHASTPENGINAHRAAADFALELDEALhekF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 221 DNGNEFF--PATSFQ-------VSNInggtgagNVIPGELEVQFNFR----FSTEVTHQQLQERVNAILQTHDLNYELSw 287
Cdd:PRK13983 239 NAKDPLFdpPYSTFEptkkeanVDNI-------NTIPGRDVFYFDCRvlpdYDLDEVLKDIKEIADEFEEEYGVKIEVE- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 288 IVNGL---PFITEHGPLVDATVNAIKSVTGLTTNLETTGGTSDGRFIAQTG--AKVIELGPNNAtiHKVDECVSTDDLIA 362
Cdd:PRK13983 311 IVQREqapPPTPPDSEIVKKLKRAIKEVRGIEPKVGGIGGGTVAAFLRKKGypAVVWSTLDETA--HQPNEYAKISNLIE 388
|
....*....
gi 940685535 363 LADIYEQIL 371
Cdd:PRK13983 389 DAKVFALLL 397
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
2-375 |
7.95e-21 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 92.13 E-value: 7.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 2 THEVIALAQALIQRESVTPEDAGCQSMMNERLKALGFNIESLFFTDTLNTWArkgNQSPHFCFAGHTDVVPTgpaqnwQH 81
Cdd:PRK08652 1 TERAKELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHIESDGEVINIVV---NSKAELFVEVHYDTVPV------RA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 82 PPFsglIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLitSDEEgpfingttkvidtLEARGEKI----- 156
Cdd:PRK08652 72 EFF---VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFV--SDEE-------------EGGRGSALfaery 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 157 --DMCLVGEPSSRDvlgdvVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDNGNEFFPATSFQV 234
Cdd:PRK08652 134 rpKMAIVLEPTDLK-----VAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFDPHIGIQE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 235 snINGGTGAgNVIPGELEVQFNFRFSTEVTHQQLQERVNAILQTHDLNYELSWIVNG--LPFITEHGPLVDATVNAiksv 312
Cdd:PRK08652 209 --IIGGSPE-YSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEYTEIWDGfeLDEDEEIVQLLEKAMKE---- 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940685535 313 TGLttNLETTGGTS--DGRFIAQTGAKVIELGPNNATI-HKVDECVSTDDLIALADIYEQILEQLL 375
Cdd:PRK08652 282 VGL--EPEFTVMRSwtDAINFRYNGTKTVVWGPGELDLcHTKFERIDVREVEKAKEFLKALNEILL 345
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
10-376 |
9.19e-21 |
|
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: 93.16 E-value: 9.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 10 QALIQRESVTPEDA---GCQSMMN---ERLKALGFNIESLfftDTLNT----WA-RKGN-QSPHFCFAGHTDVVPTGPAQ 77
Cdd:cd03893 5 AELVAIPSVSAQPDrreELRRAAEwlaDLLRRLGFTVEIV---DTSNGapvvFAeFPGApGAPTVLLYGHYDVQPAGDED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 78 NWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEgpfiNGTTKVIDTLEARGE--K 155
Cdd:cd03893 82 GWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEE----SGSPSLDQLVEAHRDllA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 156 IDMCLVGEPSSRDVLGDVVKNGRRGSLTGFLKVKGVQGHV---AYPHLAQNPIHLAAPAIT------------------- 213
Cdd:cd03893 158 ADAIVISDSTWVGQEQPTLTYGLRGNANFDVEVKGLDHDLhsgLYGGVVPDPMTALAQLLAslrdetgrilvpglydavr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 214 ------------------ELSQTVWDNGNEFFPATSFQVSNING---GTGAGNVIPGELEVQFNFRFSTEVTHQQLQERV 272
Cdd:cd03893 238 elpeeefrldagvleeveIIGGTTGSVAERLWTRPALTVLGIDGgfpGEGSKTVIPPRARAKISIRLVPGQDPEEASRLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 273 NAILQTH---DLNYELSWIVNGLPFITE-HGPLVDATVNAIKSVTGLTTNLETTGGT--SDGRFIAQTGAKVIELGPNNA 346
Cdd:cd03893 318 EAHLEKHapsGAKVTVSYVEGGMPWRSDpSDPAYQAAKDALRTAYGVEPPLTREGGSipFISVLQEFPQAPVLLIGVGDP 397
|
410 420 430
....*....|....*....|....*....|..
gi 940685535 347 T--IHKVDECVSTDDLIALAdiyeQILEQLLT 376
Cdd:cd03893 398 DdnAHSPNESLRLGNYKEGT----QAEAALLY 425
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
53-177 |
1.63e-20 |
|
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: 88.26 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 53 ARKGNQSPHFCFAGHTDVVPTGPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITS 132
Cdd:cd18669 6 YGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTP 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 940685535 133 DEEGPFINGTTKVIDTLEARGEKIDMCLVGEPSSRDVLGDVVKNG 177
Cdd:cd18669 86 DEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTP 130
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
64-297 |
6.70e-20 |
|
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: 90.78 E-value: 6.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 64 FAGHTDVVPT--GPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGPFING 141
Cdd:cd05674 74 LMAHQDVVPVnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRTIILAFGHDEEVGGERG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 142 TTKVIDTLEARGEKIDMCLV---GEPSSRDVLGDV----VKNGRRGSLTGFLKVKGVQGHVAYPH--------------L 200
Cdd:cd05674 154 AGAIAELLLERYGVDGLAAIldeGGAVLEGVFLGVpfalPGVAEKGYMDVEITVHTPGGHSSVPPkhtgigilseavaaL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 201 AQNP--------------------------------IHLAAPAITELSQTVWDNGNEFFPA---TSFQVSNINGGTGAgN 245
Cdd:cd05674 234 EANPfppkltpgnpyygmlqclaehsplpprslksnLWLASPLLKALLASELLSTSPLTRAllrTTQAVDIINGGVKI-N 312
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 940685535 246 VIPGELEVQFNFRFSTEVTHQQLQERVNAILQTHDLNYELSWIVNGLPFITE 297
Cdd:cd05674 313 ALPETATATVNHRIAPGSSVEEVLEHVKNLIADIAVKYGLGLSAFGGDVIYS 364
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
64-374 |
3.46e-19 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 88.10 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 64 FAGHTDVV--PTGPAQNWQHppfsglIEDGLLHGRGAADMKGSLAAMLVATERFvaKNPDHKGSISF--LITSDEE-GPF 138
Cdd:PRK07338 97 LTGHMDTVfpADHPFQTLSW------LDDGTLNGPGVADMKGGIVVMLAALLAF--ERSPLADKLGYdvLINPDEEiGSP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 139 inGTTKVIDTLEARGekiDMCLVGEPSSRDvlGDVVKNgRRGSLTGFLKVKGVQGHVAY-PHLAQNPIHLAAPAITELSQ 217
Cdd:PRK07338 169 --ASAPLLAELARGK---HAALTYEPALPD--GTLAGA-RKGSGNFTIVVTGRAAHAGRaFDEGRNAIVAAAELALALHA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 218 TvwdngNEFFPATSFQVSNINGGtGAGNVIPGELEVQFNFRFSTEVTHQQLQERVNAILQTHDLNYELSWIVNG------ 291
Cdd:PRK07338 241 L-----NGQRDGVTVNVAKIDGG-GPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQRHGVSLHLHGgfgrpp 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 292 LPFITEHGPLVDAtVNAIKSVTGLTTNLETTGGTSDGRFIAQTGAKVIE-LGPNNATIHKVDECVSTDDLIALADIYEQI 370
Cdd:PRK07338 315 KPIDAAQQRLFEA-VQACGAALGLTIDWKDSGGVCDGNNLAAAGLPVVDtLGVRGGNIHSEDEFVILDSLVERAQLSALI 393
|
....
gi 940685535 371 LEQL 374
Cdd:PRK07338 394 LMRL 397
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
65-374 |
1.74e-18 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 85.61 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 65 AGHTDVVPtgpaqNWQHPPfsglIEDGLLHGRGAADMKGSLAAMLVATERFvaknpDHKG-SISFLITSDEEgpfinGTT 143
Cdd:PRK00466 66 ASHVDTVP-----GYIEPK----IEGEVIYGRGAVDAKGPLISMIIAAWLL-----NEKGiKVMVSGLADEE-----STS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 144 KVIDTLEARGEKIDMCLVGEPSSrdvlGDVVKNGRRGSLTGFLKVKGVQGHVAYPhlAQNPIHLAAPAITELSQTvwdng 223
Cdd:PRK00466 127 IGAKELVSKGFNFKHIIVGEPSN----GTDIVVEYRGSIQLDIMCEGTPEHSSSA--KSNLIVDISKKIIEVYKQ----- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 224 NEFFPATSFQVSNINGGTGAgNVIPGELEVQFNFRFSTEVTHQQLQERVNAILQTHDLNyelswIVNGLPFITehgplVD 303
Cdd:PRK00466 196 PENYDKPSIVPTIIRAGESY-NVTPAKLYLHFDVRYAINNKRDDLISEIKDKFQECGLK-----IVDETPPVK-----VS 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940685535 304 ATVNAIKSVT------GLTTNLETTGGTSDGRFIAQTGAKVIELGPNNATI-HKVDECVSTDDLIALADIYEQILEQL 374
Cdd:PRK00466 265 INNPVVKALMrallkqNIKPRLVRKAGTSDMNILQKITTSIATYGPGNSMLeHTNQEKITLDEIYIAVKTYMLAIEEL 342
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
63-174 |
6.28e-18 |
|
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: 81.32 E-value: 6.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 63 CFAGHTDVVPTGPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGPFINGT 142
Cdd:cd03873 16 ALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEEVGSGGGK 95
|
90 100 110
....*....|....*....|....*....|..
gi 940685535 143 TKVIDTLEARGEKIDMCLVGEPSSRDVLGDVV 174
Cdd:cd03873 96 GLLSKFLLAEDLKVDAAFVIDATAGPILQKGV 127
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
1-374 |
2.22e-17 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 82.31 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 1 MTHEVIALAQALIQRESVTPEDAGCQSMMNERLKALGFNIeslFFTDTLNTWARKGNQSPHFCFAGHTDVVPtG--PAQn 78
Cdd:PRK04443 4 SALEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREA---WVDEAGNARGPAGDGPPLVLLLGHIDTVP-GdiPVR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 79 wqhppfsglIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPdhkGSISFLITSDEEGPFINGTTKVIDTleargEKIDM 158
Cdd:PRK04443 79 ---------VEDGVLWGRGSVDAKGPLAAFAAAAARLEALVR---ARVSFVGAVEEEAPSSGGARLVADR-----ERPDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 159 CLVGEPSSRDvlGdvVKNGRRGSLTGFLKVKGVQGHVAYPHlaqnpiHLAAPAITELSQTVwdngneffpATSFQVSniN 238
Cdd:PRK04443 142 VIIGEPSGWD--G--ITLGYKGRLLVTYVATSESFHSAGPE------PNAAEDAIEWWLAV---------EAWFEAN--D 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 239 GGTGAGNVIPGELeVQFN-----FRFSTEVTHQ-----QLQ-ERVNAILQTHDLNYELSWIVNGLPFITE-HGPLVDATV 306
Cdd:PRK04443 201 GRERVFDQVTPKL-VDFDsssdgLTVEAEMTVGlrlppGLSpEEAREILDALLPTGTVTFTGAVPAYMVSkRTPLARAFR 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 307 NAIKSVTGLTTNLETTgGTSDGRFIAQT-GAKVIELGPNNATI-HKVDECVSTDDLIALADIYEQILEQL 374
Cdd:PRK04443 280 VAIREAGGTPRLKRKT-GTSDMNVVAPAwGCPMVAYGPGDSDLdHTPDEHLPLAEYLRAIAVLTDVLERL 348
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
19-374 |
3.72e-16 |
|
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: 79.24 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 19 TPEDAGCQSMMNERLKALGFNIESLFFTD----TLNTWARKGNQSPHFCFAGHTDVVPTGPaQNWQHPPFSGLI-EDGLL 93
Cdd:cd05646 20 NPDYDACVEFLKRQADELGLPVRVIEVVPgkpvVVLTWEGSNPELPSILLNSHTDVVPVFE-EKWTHDPFSAHKdEDGNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 94 HGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGPFINGTTKVIDTLEARGEKIDMCL-VGEPSSRDVLgd 172
Cdd:cd05646 99 YARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIGGHDGMEKFVKTEEFKKLNVGFALdEGLASPTEEY-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 173 VVKNGRRGSLTGFLKVKGVQGHVA--YPHLAQNPIHLAAPAITELSQTVWD---NGNEFFPA--TSFQVSNINGGTgAGN 245
Cdd:cd05646 177 RVFYGERSPWWVVITAPGTPGHGSklLENTAGEKLRKVIESIMEFRESQKQrlkSNPNLTLGdvTTVNLTMLKGGV-QMN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 246 VIPGELEVQFNFRFSTEVTHQQLQERVNAILQTHDLNYELSWIvnglpfitEHGPLVDATVN--------AIKSVT---G 314
Cdd:cd05646 256 VVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGRGVTYEFE--------QKSPEKDPTSLddsnpwwaAFKKAVkemG 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940685535 315 LTTNLETTGGTSDGRFIAQTGAKVIELGPNNAT---IHKVDECVSTDDLIALADIYEQILEQL 374
Cdd:cd05646 328 LKLKPEIFPAATDSRYIRALGIPALGFSPMNNTpilLHDHNEFLNEDVFLRGIEIYEKIIPAL 390
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
37-258 |
1.09e-15 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 77.55 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 37 GFNIESLFFTD-TLNTWARKGnqSPHFCFAGHTDVVPTGPAqnWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATErf 115
Cdd:PRK08737 42 GFQVEVIDHGAgAVSLYAVRG--TPKYLFNVHLDTVPDSPH--WSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAAN-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 116 vaknpDHKGSISFLITSDEEGpfinGTTKVIDTLEARGEKIDMCLVGEPS-SRDVLgdvvknGRRGSLTGFLKVKGVQGH 194
Cdd:PRK08737 116 -----AGDGDAAFLFSSDEEA----NDPRCVAAFLARGIPYEAVLVAEPTmSEAVL------AHRGISSVLMRFAGRAGH 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940685535 195 VAYPH-LAQNPIHLAAPAITELSQTVWDNGNEFFPATS---FQVSNINGGTGAgNVIPGELEVQFNFR 258
Cdd:PRK08737 181 ASGKQdPSASALHQAMRWGGQALDHVESLAHARFGGLTglrFNIGRVEGGIKA-NMIAPAAELRFGFR 247
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
56-375 |
1.19e-14 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 74.81 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 56 GNQSPHFCFAGHTDVVPTGPAQnWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFvaKNPDHKGSISFLITSDEE 135
Cdd:PRK08554 60 GEGKPKLLFMAHFDVVPVNPEE-WNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKEL--SKEPLNGKVIFAFTGDEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 136 gpfINGTT--KVIDTLEARGEKIDMCLVGEPSS-------RDVLGDVVK--------NGRRGSLTGFLKVKGVQG-HVAY 197
Cdd:PRK08554 137 ---IGGAMamHIAEKLREEGKLPKYMINADGIGmkpiirrRKGFGVTIRvpsekvkvKGKLREQTFEIRTPVVETrHAAY 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 198 --PHLAQNPIhLAAPAitelsqtvwdngneFFPATSFQVSNINGGTGAGNVIPGELEVQF-------------------- 255
Cdd:PRK08554 214 flPGVDTHPL-IAASH--------------FLRESNVLAVSLEGKFLKGNVVPGEVTLTYlepgegeevevdlgltrllk 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 256 ------------------------N-FRFSTE----------VTH--QQLQERVNAILQTHDLNYELSWIVN---GLPFI 295
Cdd:PRK08554 279 aivplvrapikaekysdygvsitpNvYSFAEGkhvlkldiraMSYskEDIERTLKEVLEFNLPEAEVEIRTNekaGYLFT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 296 TEHGPLVDATVNAIKSVtGLTTNLETTGGTSDGRFIAQTGAKVIELGPNNATIHKVDECVSTDDLIALADIYEQILEQLL 375
Cdd:PRK08554 359 PPDEEIVKVALRVLKEL-GEDAEPVEGPGASDSRYFTPYGVKAIDFGPKGGNIHGPNEYVEIDSLKKMPEVYKRIALRLL 437
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
66-309 |
2.10e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 74.12 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 66 GHTDVVPTGPAQnWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGPFINGTTKV 145
Cdd:PRK07906 72 GHLDVVPAEAAD-WSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVADEEAGGTYGAHWL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 146 IDT--------LEARGEkidmclVGEpSSRDVLGD----VVKNGRRGSLTGFLKVKGVQGHVAYPH-------LA----- 201
Cdd:PRK07906 151 VDNhpelfegvTEAISE------VGG-FSLTVPGRdrlyLIETAEKGLAWMRLTARGRAGHGSMVNddnavtrLAeavar 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 202 ----QNPIHLAAP------AITELSQTVWDNGNeffPATSF----QVSNINGGT----------GAG---NVIPGELEVQ 254
Cdd:PRK07906 224 igrhRWPLVLTPTvrafldGVAELTGLEFDPDD---PDALLaklgPAARMVGATlrntanptmlKAGykvNVIPGTAEAV 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 940685535 255 FNFRF--STEvthQQLQERVNAILQTHdlnYELSWIVNGLPFITEH-GPLVDATVNAI 309
Cdd:PRK07906 301 VDGRFlpGRE---EEFLATVDELLGPD---VEREWVHRDPALETPFdGPLVDAMNAAL 352
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
6-314 |
2.47e-14 |
|
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: 73.28 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 6 IALAQALIQRESVTPEDAGCQSMMNERLKALGFniESLFFTDTLNTWAR-KGNQS-PHFCFAGHTDVVPtgPAQNwqhpP 83
Cdd:cd03896 1 VDTAIELGEIPAPTFREGARADLVAEWMADLGL--GDVERDGRGNVVGRlRGTGGgPALLFSAHLDTVF--PGDT----P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 84 FSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGpfINGTTKVIDTLEARGEKIDMCLVGE 163
Cdd:cd03896 73 ATVRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVGEEG--LGDLRGARYLLSAHGARLDYFVVAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 164 PSsrdvlGDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDngneFFPATSFQVSNINGGTGA 243
Cdd:cd03896 151 GT-----DGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAAP----YVPKTTFAAIRGGGGTSV 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940685535 244 gNVIPGELEVQFNFRFSTEVTHQQLQERVNAILQ-----THDLNYELSWIVNGLPFITEH-GPLVDATVNAIKSVTG 314
Cdd:cd03896 222 -NRIANLCSMYLDIRSNPDAELADVQREVEAVVSklaakHLRVKARVKPVGDRPGGEAQGtEPLVNAAVAAHREVGG 297
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
11-204 |
3.39e-14 |
|
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: 73.53 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 11 ALIQRESVTPEDAG---CQSMMNERLKALGFNIEsLFFTDTlN--TWARKGNQSPH-FCFAGHTDVVPTGPAQNWQHPPF 84
Cdd:cd05681 7 DLLKIPSVSAQGRGipeTADFLKEFLRRLGAEVE-IFETDG-NpiVYAEFNSGDAKtLLFYNHYDVQPAEPLELWTSDPF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 85 SGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEgpfiNGTTKVIDTLEARGEKI--DMCLVg 162
Cdd:cd05681 85 ELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEE----VGSPNLEKFVAEHADLLkaDGCIW- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 940685535 163 EPSSRDVLGD-VVKNGRRGSLTGFLKVKG--VQGHVAYPHLAQNP 204
Cdd:cd05681 160 EGGGKNPKGRpQISLGVKGIVYVELRVKTadFDLHSSYGAIVENP 204
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
12-372 |
9.04e-14 |
|
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349932 [Multi-domain] Cd Length: 368 Bit Score: 71.71 E-value: 9.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 12 LIQRESVTPEDAGCQSMMNERLKALGFNIESLFFTDTLN--------TWARKGNQSPHFCFAGHTDVVPtgPAQNWQHPp 83
Cdd:cd05683 12 LVQIDSETLHEKEISKVLKKKFENLGLSVIEDDAGKTTGggagnlicTLKADKEEVPKILFTSHMDTVT--PGINVKPP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 84 fsgLIEDGLLHGRG----AADMKGSLAAMLVATERFVAKNPDHkGSISFLITSDEEGPFI---NGTTKVIDT-----LEA 151
Cdd:cd05683 89 ---QIADGYIYSDGttilGADDKAGIAAILEAIRVIKEKNIPH-GQIQFVITVGEESGLVgakALDPELIDAdygyaLDS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 152 RGEkidmclVGEPSSRDVLGDVVKngrrgsltgfLKVKGVQGHVA-YPHLAQNPIHLAAPAITELSqtvWDNGNEFfpaT 230
Cdd:cd05683 165 EGD------VGTIIVGAPTQDKIN----------AKIYGKTAHAGtSPEKGISAINIAAKAISNMK---LGRIDEE---T 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 231 SFQVSNINGGTgAGNVIPGELEVQFNFR------FSTEVTHqqLQERVNAILQTHDLNYELSWIVNGLPF-ITEHGPLVD 303
Cdd:cd05683 223 TANIGKFQGGT-ATNIVTDEVNIEAEARsldeekLDAQVKH--MKETFETTAKEKGAHAEVEVETSYPGFkINEDEEVVK 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940685535 304 ATVNAIKSVtGLTTNLETTGGTSDGRFIAQTGAKVIELGPNNATIHKVDECVSTDDLIALADIYEQILE 372
Cdd:cd05683 300 LAKRAANNL-GLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLYDTAVLVVEIIK 367
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
90-330 |
1.25e-13 |
|
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: 71.22 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 90 DGLLHGRGaadmKGSLAAMLVATERFVAKNPDH-KGSISFLITSDEEGpfINGTTKVIdtlEARGEK-IDMCLVGEPSSR 167
Cdd:TIGR01891 83 PGVMHACG----HDLHTAILLGTAKLLKKLADLlEGTVRLIFQPAEEG--GGGATKMI---EDGVLDdVDAILGLHPDPS 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 168 DVLGDVVKngRRGSLTG-----FLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDNGNEFFPATsFQVSNINGGtG 242
Cdd:TIGR01891 154 IPAGTVGL--RPGTIMAaadkfEVTIHGKGAHAARPHLGRDALDAAAQLVVALQQIVSRNVDPSRPAV-VSVGIIEAG-G 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 243 AGNVIPGELEVQFNFRFSTEVTHQQLQERVNAIL----QTHDLNYELSWiVNGLPFITEHGPLVDATVNAIKSVTG---- 314
Cdd:TIGR01891 230 APNVIPDKASMSGTVRSLDPEVRDQIIDRIERIVegaaAMYGAKVELNY-DRGLPAVTNDPALTQILKEVARHVVGpenv 308
|
250
....*....|....*.
gi 940685535 315 LTTNLETTGGTSDGRF 330
Cdd:TIGR01891 309 AEDPEVTMGSEDFAYY 324
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
4-353 |
6.06e-13 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 69.66 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 4 EVIALAQALIQRESVTPEDAGCQSMMN---ERLKALGFNIESlffTDT--------LNTWarKGNQSPHFCFAGHTDVV- 71
Cdd:PRK06133 38 AYLDTLKELVSIESGSGDAEGLKQVAAllaERLKALGAKVER---APTppsagdmvVATF--KGTGKRRIMLIAHMDTVy 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 72 PTGPAQNwqhPPFSglIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGPFInGTTKVIDTLea 151
Cdd:PRK06133 113 LPGMLAK---QPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGSP-GSRELIAEL-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 152 rGEKIDMCLVGEPSSRDvlgDVVKNGRRGSLTGFLKVKGVQGHV-AYPHLAQNpihlaapAITELSQTVWDNGNEFFPAT 230
Cdd:PRK06133 185 -AAQHDVVFSCEPGRAK---DALTLATSGIATALLEVKGKASHAgAAPELGRN-------ALYELAHQLLQLRDLGDPAK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 231 SFQVS--NINGGTgAGNVIPGELEVQFNFRFS----TEVTHQQLQERVNAILqTHDLNYELSWIVNGLPFI-TEHGPLVD 303
Cdd:PRK06133 254 GTTLNwtVAKAGT-NRNVIPASASAQADVRYLdpaeFDRLEADLQEKVKNKL-VPDTEVTLRFERGRPPLEaNAASRALA 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 940685535 304 ATVNAIKSVTGLTTNL--ETTGGTSDGRFIAQTG-AKVIE-LGPNNATIHKVDE 353
Cdd:PRK06133 332 EHAQGIYGELGRRLEPidMGTGGGTDAAFAAGSGkAAVLEgFGLVGFGAHSNDE 385
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
52-135 |
1.04e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 68.95 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 52 WARKGNQSPHFCFAGHTDVVPTGPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLIT 131
Cdd:PRK07205 68 YAEIGQGEELLAILCHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFG 147
|
....
gi 940685535 132 SDEE 135
Cdd:PRK07205 148 TDEE 151
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
66-369 |
2.62e-12 |
|
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.
Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 67.79 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 66 GHTDVVPTGpaQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEG--------- 136
Cdd:TIGR01887 74 GHLDVVPAG--DGWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEESgwkcidyyf 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 137 ----------------PFING---------TTK-------VIDTLEArGEKIDM------CLVGEPSSRDVLGDVVKNGR 178
Cdd:TIGR01887 152 eheempdigftpdaefPIIYGekgittleiKFKddtegdvVLESFKA-GEAYNMvpdhatAVISGKKLTEVEQLKFVFFI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 179 RGSLTGFLK---------VKGVQGHVAYP--------HLAQ-----NPIHLAAPAITELSQTVW--DNGNEFFPATSFQV 234
Cdd:TIGR01887 231 AKELEGDFEvndgtltitLEGKSAHGSAPekginaatYLALflaqlNLAGGAKAFLQFLAEYLHedHYGEKLGIKFHDDV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 235 S---NINGGTGAGNViPGELEVQFNFRFSteVTHQQLQERVNAILQTHDLNYElswIVNGL--P-FITEHGPLVDATVNA 308
Cdd:TIGR01887 311 SgdlTMNVGVIDYEN-AEAGLIGLNVRYP--VGNDPDTMLKNELAKESGVVEV---TLNGYlkPlYVPKDDPLVQTLMKV 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940685535 309 IKSVTGLTTNLETTGGTSDGRFiAQTGAKVIELGPNNA-TIHKVDECVSTDDLIALADIYEQ 369
Cdd:TIGR01887 385 YEKQTGDEGEPVAIGGGTYARL-MPNGVAFGALFPGEEdTMHQANEYIMIDDLLLATAIYAE 445
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
29-217 |
9.52e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 66.18 E-value: 9.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 29 MNERLKALGFNIESLFFT----DTLNTWARKGNQSPH--FCFAGHTDVVpTGPAQNWQHPPFSGLIEDGLLHGRGAADMK 102
Cdd:PRK09133 65 MAARLKAAGFADADIEVTgpypRKGNLVARLRGTDPKkpILLLAHMDVV-EAKREDWTRDPFKLVEENGYFYGRGTSDDK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 103 gSLAAMLVAT------ERFVAKNPdhkgsISFLITSDEEGPFINGTTkviDTLEARGEKIDMCLV---GEPSSRDVLGDV 173
Cdd:PRK09133 144 -ADAAIWVATlirlkrEGFKPKRD-----IILALTGDEEGTPMNGVA---WLAENHRDLIDAEFAlneGGGGTLDEDGKP 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 940685535 174 VKNGRRGS----LTGFLKVKGVQGHVAYPhLAQNPIHLAAPAITELSQ 217
Cdd:PRK09133 215 VLLTVQAGektyADFRLEVTNPGGHSSRP-TKDNAIYRLAAALSRLAA 261
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
4-375 |
2.02e-11 |
|
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: 64.88 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 4 EVIALAQALIQRESVTP--EDAGCQSMMNERLKALGFNIE----------SLFFTDTLNTWARK--GNQSPHFCFAGHTD 69
Cdd:cd02697 4 EEVRFLQKLVRVPTDTPpgNNAPHAERTAALLQGFGFEAErhpvpeaevrAYGMESITNLIVRRryGDGGRTVALNAHGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 70 VVPtgPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEE-----GP---FING 141
Cdd:cd02697 84 VVP--PGDGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEfggelGPgwlLRQG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 142 TTKViDTLEARGEKIDmclvgepssrdvlgdvVKNGRRGSLTGFLKVKGVQGHVAYPHLAqnpiHLAAPAITELSQTVWD 221
Cdd:cd02697 162 LTKP-DLLIAAGFSYE----------------VVTAHNGCLQMEVTVHGKQAHAAIPDTG----VDALQGAVAILNALYA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 222 NGNEFFPATS---------FQVSNINGGTGAgNVIPGELEVQFNFRFSTEVTHQQLQERVNAILQTH-----DLNYELSW 287
Cdd:cd02697 221 LNAQYRQVSSqvegithpyLNVGRIEGGTNT-NVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAaasmpGISVDIRR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 288 IVNGLPF--ITEHGPLVDATVNAIKSVTGLTTNLETTGGTSDGRFIAQTGAKVIELGPNNATI-----HKVDECVSTDDL 360
Cdd:cd02697 300 LLLANSMrpLPGNAPLVEAIQTHGEAVFGEPVPAMGTPLYTDVRLYAEAGIPGVIYGAGPRTVleshaKRADERLQLEDL 379
|
410
....*....|....*
gi 940685535 361 IALADIYEQILEQLL 375
Cdd:cd02697 380 RRATKVIARSLRDLL 394
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
64-161 |
3.16e-11 |
|
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: 64.29 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 64 FAGHTDVVPTGPAQNWQHPPFSGLIEDGLLHGRGAADMKG-SLAAMLVATERFVAKNPDHkgSISFLITSDEEgpfiNGT 142
Cdd:cd05677 76 FYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGpLLAAIYAVAELFQEGELDN--DVVFLIEGEEE----SGS 149
|
90 100
....*....|....*....|..
gi 940685535 143 T---KVIDTLEARGEKIDMCLV 161
Cdd:cd05677 150 PgfkEVLRKNKELIGDIDWILL 171
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
187-314 |
3.39e-11 |
|
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: 63.98 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 187 KVKGVQGHVAYPHLAQNPIHLAAPAITELsQTVWdnGNEFFPATSFQVS--NINGGTgAGNVIPGELEVQFNFRFSTEVT 264
Cdd:COG1473 189 TIKGKGGHAAAPHLGIDPIVAAAQIVTAL-QTIV--SRNVDPLDPAVVTvgIIHGGT-APNVIPDEAELEGTVRTFDPEV 264
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 940685535 265 HQQLQERVNAIL----QTHDLNYELSWIvNGLPFITEHGPLVDATVNAIKSVTG 314
Cdd:COG1473 265 RELLEERIERIAegiaAAYGATAEVEYL-RGYPPTVNDPELTELAREAAREVLG 317
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
58-360 |
3.52e-11 |
|
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: 64.25 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 58 QSPHFCFAGHTDVVPTGPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEgp 137
Cdd:cd05680 62 GAPTVLVYGHYDVQPPDPLELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEE-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 138 fiNGTTKVIDTLEARGEKI--DMCLVGEPSSRDVLGDVVKNGRRGSLTGFLKVKGVQ-----GHvaYPHLAQNPIHLAAP 210
Cdd:cd05680 140 --IGSPSLPAFLEENAERLaaDVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPNrdlhsGS--YGGAVPNPANALAR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 211 AITELS---------------QTVWDNGNEFFPAT--------------------------------SFQVSNINGG-TG 242
Cdd:cd05680 216 LLASLHdedgrvaipgfyddvRPLTDAEREAWAALpfdeaafkaslgvpalggeagyttlerlwarpTLDVNGIWGGyQG 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 243 AG--NVIPGELEVQFNFRFsteVTHQQLQeRVNAILQTH-------DLNYELSWIVNGLPFITEHG-PLVDATVNAIKSV 312
Cdd:cd05680 296 EGskTVIPSKAHAKISMRL---VPGQDPD-AIADLLEAHlrahappGVTLSVKPLHGGRPYLVPTDhPALQAAERALEEA 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 940685535 313 TGLTTNLETTGGTSD--GRFIAQTGAKVIELG---PNNAtIHKVDECVSTDDL 360
Cdd:cd05680 372 FGKPPVFVREGGSIPivALFEKVLGIPTVLMGfglPDDA-IHAPNEKFRLECF 423
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
28-155 |
8.80e-11 |
|
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: 63.00 E-value: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 28 MMNERLKALGFNIESLFF-TDTLNTW----------ARKGN--QSPHFCFAGHTDVVPTGPAQNWQHPPFSGLIEDGLLH 94
Cdd:cd05676 41 WAAERLEKLGFKVELVDIgTQTLPDGeelplppvllGRLGSdpSKKTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLY 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940685535 95 GRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEgpfiNGTTKVIDTLEARGEK 155
Cdd:cd05676 121 GRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEGMEE----SGSEGLDELIEARKDT 177
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
106-290 |
1.23e-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: 62.23 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 106 AAMLVATERFVAKNPDH-KGSISFLITSDEEGPfiNGTTKVIDTLEARGEKIDMCLvGEPSSRDV-LGDVVknGRRGSLT 183
Cdd:cd03886 94 TAMLLGAAKLLAERRDPlKGTVRFIFQPAEEGP--GGAKAMIEEGVLENPGVDAAF-GLHVWPGLpVGTVG--VRSGALM 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 184 G-----FLKVKGVQGHVAYPHLAQNPIHLAAPAITELsQTVwdNGNEFFPATSFQVS--NINGGTGAgNVIPGELEVQFN 256
Cdd:cd03886 169 AsadefEITVKGKGGHGASPHLGVDPIVAAAQIVLAL-QTV--VSRELDPLEPAVVTvgKFHAGTAF-NVIPDTAVLEGT 244
|
170 180 190
....*....|....*....|....*....|....*...
gi 940685535 257 FR-FSTEV---THQQLQERVNAILQTHDLNYELSWIVN 290
Cdd:cd03886 245 IRtFDPEVreaLEARIKRLAEGIAAAYGATVELEYGYG 282
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
67-135 |
5.57e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 60.54 E-value: 5.57e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940685535 67 HTDVVPTGPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKgSISFLITSDEE 135
Cdd:PRK06446 70 HYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKHKLNV-NVKFLYEGEEE 137
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
64-272 |
7.14e-10 |
|
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: 60.17 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 64 FAG-HTDVVPTGPAQnWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGPFINGT 142
Cdd:cd08012 82 FVGsHMDVVTANPET-WEFDPFSLSIDGDKLYGRGTTDCLGHVALVTELFRQLATEKPALKRTVVAVFIANEENSEIPGV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 143 TkvIDTLEARGeKIDMCLVGEPSSRDVLGDVVKNGRRGSLTGFLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDN 222
Cdd:cd08012 161 G--VDALVKSG-LLDNLKSGPLYWVDSADSQPCIGTGGMVTWKLTATGKLFHSGLPHKAINALELVMEALAEIQKRFYID 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940685535 223 gnefFP----------ATS-----FQVSNINGGTgagNVIPGELEVQFNFRFSTEVTHQQLQERV 272
Cdd:cd08012 238 ----FPphpkeevygfATPstmkpTQWSYPGGSI---NQIPGECTICGDCRLTPFYDVKEVREKL 295
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
106-277 |
6.10e-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: 57.35 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 106 AAMLVATERFVAKNPDHKGSISFLITSDEEGpfINGTTKVIDT-LEARGEKIDMCL----VGEPSsrdvlGDVV-KNGRR 179
Cdd:cd05664 105 AALLGAARLLVEAKDAWSGTLIAVFQPAEET--GGGAQAMVDDgLYDKIPKPDVVLaqhvMPGPA-----GTVGtRPGRF 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 180 GSLTGFLKV--KGVQGHVAYPHLAQNPIHLAAPAITELsQTVWDNGNEFFPATSFQVSNINGGTgAGNVIPGELEVQFNF 257
Cdd:cd05664 178 LSAADSLDItiFGRGGHGSMPHLTIDPVVMAASIVTRL-QTIVSREVDPQEFAVVTVGSIQAGS-AENIIPDEAELKLNV 255
|
170 180
....*....|....*....|
gi 940685535 258 RFSTEVTHQQLQERVNAILQ 277
Cdd:cd05664 256 RTFDPEVREKVLNAIKRIVR 275
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
187-277 |
6.65e-09 |
|
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: 56.96 E-value: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 187 KVKGVQGHVAYPHLAQNPIHLAAPAITELsQTVWDNGNEFFPATSFQVSNINGGTgAGNVIPGELEVQFNFRFSTEVTHQ 266
Cdd:cd08019 174 EVKGKGGHGSMPHQGIDAVLAAASIVMNL-QSIVSREIDPLEPVVVTVGKLNSGT-RFNVIADEAKIEGTLRTFNPETRE 251
|
90
....*....|.
gi 940685535 267 QLQERVNAILQ 277
Cdd:cd08019 252 KTPEIIERIAK 262
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
67-154 |
2.06e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 55.68 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 67 HTDVVPTGPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVAterFVAKNPDHKGSISFLITSDEEGpfinGTTKVI 146
Cdd:PRK07907 91 HHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAA---LRALGGDLPVGVTVFVEGEEEM----GSPSLE 163
|
....*...
gi 940685535 147 DTLEARGE 154
Cdd:PRK07907 164 RLLAEHPD 171
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
56-334 |
6.18e-08 |
|
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: 53.78 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 56 GNQSPHFCFAGHTDVVPTGPAQNWQHPPFSglieDGLLHGRGaadmKGSLAAMLVATERFVAKNPDH-KGSISFLITSDE 134
Cdd:cd08660 53 GEDGPVIAIRADIDALPIQEQTNLPFASKV----DGT*HACG----HDFHTTSIIGTA*LLNQRRAElKGTVVFIFQPAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 135 EGpfINGTTKVIDtlEARGEKIDMCLVGEPSSRDVLGDV-VKNGRRGSLTGFL--KVKGVQGHVAYPHLAQNPIHLAAPA 211
Cdd:cd08660 125 EG--AAGARKVLE--AGVLNGVSAIFGIHNKPDLPVGTIgVKEGPL*ASVDVFeiVIKGKGGHASIPNNSIDPIAAAGQI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 212 ITELSQTVWDNGNEFFPATsFQVSNINGGTgAGNVIPGELEVQFNFRFSTEVTHQQLQE----RVNAILQTHDLNYELSW 287
Cdd:cd08660 201 ISGLQSVVSRNISSLQNAV-VSITRVQGGT-AWNVIPDQAE*EGTVRAFTKEARQAVPEh*rrVAEGIAAGYGCQAEFKW 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 940685535 288 IVNGLPFITEHGPLVDATVNAIKSVTGLTTNLETTGGTSDGRFIAQT 334
Cdd:cd08660 279 FPNGPSEVQNDGTLLNAFSKAAARLGYATVHAEQSPGSEDFALYQEK 325
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
106-320 |
8.74e-08 |
|
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: 53.43 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 106 AAMLVATERFVAKNPDH-KGSISFLITSDEEGPfINGTTKVIDtlEARGEKIDMCLVGEPSSRDVLGDVVKngRRGSLTG 184
Cdd:cd08021 105 TAMLLGAAKVLAENKDEiKGTVRFIFQPAEEVP-PGGAKPMIE--AGVLEGVDAVFGLHLWSTLPTGTIAV--RPGAIMA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 185 -----FLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDNGNEFFPATsFQVSNINGGTgAGNVIPGELEVQFNFRF 259
Cdd:cd08021 180 apdefDITIKGKGGHGSMPHETVDPIVIAAQIVTALQTIVSRRVDPLDPAV-VTIGTFQGGT-SFNVIPDTVELKGTVRT 257
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940685535 260 STEVTHQQLQERVNAIL----QTHDLNYELSWiVNGLPFITEHGPLVDATVNAIKSVTGLTTNLE 320
Cdd:cd08021 258 FDEEVREQVPKRIERIVkgicEAYGASYELEY-QPGYPVVYNDPEVTELVKKAAKEVLIGVENVE 321
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
66-107 |
1.18e-07 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 53.31 E-value: 1.18e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 940685535 66 GHTDVVPTGPAqnWQHPPFSGLIEDGLLHGRGAADMKG-SLAA 107
Cdd:PRK07318 86 GHLDVVPAGDG--WDTDPYEPVIKDGKIYARGTSDDKGpTMAA 126
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
183-324 |
1.46e-07 |
|
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349939 [Multi-domain] Cd Length: 365 Bit Score: 52.67 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 183 TGFLKV--KGVQGHVAYPHLAQNPIHLAAPAITELSQtVWDNGNEffpATSFQVSNINGGTGAGNVIPGELEVQFNFRFS 260
Cdd:cd08018 167 STFLEGtiKGKQAHGARPHLGINAIEAASAIVNAVNA-IHLDPNI---PWSVKMTKLQAGGEATNIIPDKAKFALDLRAQ 242
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940685535 261 TEVTHQQLQERV-NAILQTHDLN---YELSWiVNGLPFITEHGPLVDATVNAIKSVTG---LTTNLETTGG 324
Cdd:cd08018 243 SNEAMEELKEKVeHAIEAAAALYgasIEITE-KGGMPAAEYDEEAVELMEEAITEVLGeekLAGPCVTPGG 312
|
|
| M20_Acy1-like |
cd05667 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
107-333 |
2.05e-07 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins that have been predicted as N-acyl-L-amino acid amidohydrolase (amaA), thermostable carboxypeptidase (cpsA-1, cpsA-2 in Sulfolobus solfataricus) and abgB (aminobenzoyl-glutamate utilization protein B), and generally are involved in the urea cycle and metabolism of amino groups. Aminoacylases 1 (ACY1s) comprise a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and is a highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349917 [Multi-domain] Cd Length: 403 Bit Score: 52.43 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 107 AMLVATERFVAKNPDH-KGSISFLITSDEEGPfingttkviDTLEARGEK--IDMCLVGEPSSRDVLGDVVKNGRRGSLT 183
Cdd:cd05667 114 AILLGAAEVLAANKDKiKGTVMFIFQPAEEGP---------PEGEEGGAKlmLKEGAFKDYKPEAIFGLHVGSGLPSGQL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 184 GF-------------LKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDNGNEFFPATSFQVSNINGGTgAGNVIPGE 250
Cdd:cd05667 185 GYrsgpimasadrfrITVKGKQTHGSRPWDGIDPIMASAQIIQGLQTIISRRIDLTKEPAVISIGKINGGT-RGNIIPED 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 251 LEVQFNFR-FSTEVTHQ---QLQERVNAILQTHDLNYELSwIVNGLPfITEHGP-LVDATVNAIKSVTGLTTN---LETT 322
Cdd:cd05667 264 AEMVGTIRtFDPEMREDifaRLKTIAEHIAKAYGATAEVE-FANGYP-VTYNDPaLTAKMLPTLQKAVGKADLvvlPPTQ 341
|
250
....*....|.
gi 940685535 323 GGTSDGRFIAQ 333
Cdd:cd05667 342 TGAEDFSFYAE 352
|
|
| M20_IAA_Hyd |
cd08017 |
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant ... |
187-307 |
3.85e-07 |
|
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.
Pssm-ID: 349938 [Multi-domain] Cd Length: 376 Bit Score: 51.55 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 187 KVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVwdnGNEFFPATS--FQVSNINGGTgAGNVIPGELEVQFNFR-FSTEV 263
Cdd:cd08017 174 VIRGKGGHAAMPHHTVDPVVAASSAVLALQQLV---SRETDPLDSqvVSVTRFNGGH-AFNVIPDSVTFGGTLRaLTTEG 249
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 940685535 264 ---THQQLQERVNAILQTHDLNYELSWIVNGLPFItehgPlvdATVN 307
Cdd:cd08017 250 fyrLRQRIEEVIEGQAAVHRCNATVDFSEDERPPY----P---PTVN 289
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
60-135 |
6.20e-07 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 50.90 E-value: 6.20e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940685535 60 PHFCFAGHTDVVPTGPAQNWQHPPFSGLIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEE 135
Cdd:PRK08201 80 PTVLIYGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIEGEEE 155
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
65-219 |
8.06e-07 |
|
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: 50.80 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 65 AGHTDVVPT---GPAQNWQHPP------FSGLIED------------GLLHGRGAADMKGSLAAMLVATERFvAKNPDHK 123
Cdd:cd05654 77 ISHFDTVGIedyGELKDIAFDPdeltkaFSEYVEEldeevredllsgEWLFGRGTMDMKSGLAVHLALLEQA-SEDEDFD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 124 GSISFLITSDEEGPFiNGTTKVIDTLEARGEKIDM----CLVGEPSSRDVLGDVVKNGRRGS----LTGFLkVKGVQGHV 195
Cdd:cd05654 156 GNLLLMAVPDEEVNS-RGMRAAVPALLELKKKHDLeyklAINSEPIFPQYDGDQTRYIYTGSigkiLPGFL-CYGKETHV 233
|
170 180
....*....|....*....|....
gi 940685535 196 AYPHLAQNPIHLAAPAITELSQTV 219
Cdd:cd05654 234 GEPFAGINANLMASEITARLELNA 257
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
60-215 |
1.52e-06 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 49.90 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 60 PHFCFAGHTDVVPTGPAQNWQHPPFSGLIEDG-----LLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDE 134
Cdd:PRK09104 83 PHVLFYGHYDVQPVDPLDLWESPPFEPRIKETpdgrkVIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 135 EgpfiNGTTKVIDTLEARGE--KIDMCLVGEPSSRDVLGDVVKNGRRGSLTGFLKVKGV-----QGHvaYPHLAQNPIHL 207
Cdd:PRK09104 163 E----SGSPSLVPFLEANAEelKADVALVCDTGMWDRETPAITTSLRGLVGEEVTITAAdrdlhSGL--FGGAAANPIRV 236
|
....*...
gi 940685535 208 AAPAITEL 215
Cdd:PRK09104 237 LTRILAGL 244
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
187-322 |
2.48e-06 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of uncharacterized 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: 349936 [Multi-domain] Cd Length: 371 Bit Score: 48.81 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 187 KVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDNGNEFFPaTSFQVSNINGGTgAGNVIPGELEVQFNFRFSTEVTHQ 266
Cdd:cd08014 176 RIQGEGGHGARPHLTVDLVWAAAQVVTDLPQAISRRIDPRSP-VVLTWGSIEGGR-APNVIPDSVELSGTVRTLDPDTWA 253
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 267 QL----QERVNAILQTHDLNYELSWIvNGLPFITEHGPLVDATVNAIKSVTGLTTNLETT 322
Cdd:cd08014 254 QLpdlvEEIVAGICAPYGAKYELEYR-RGVPPVINDPASTALLEAAVREILGEDNVVALA 312
|
|
| M20_Acy1_YxeP-like |
cd05669 |
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
186-307 |
5.06e-06 |
|
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: 48.06 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 186 LKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDNGNEFFPATsFQVSNINGGTgAGNVIPGELEVQFNFR-FSTEVt 264
Cdd:cd05669 177 IEIAGKGAHAAKPENGVDPIVAASQIINALQTIVSRNISPLESAV-VSVTRIHAGN-TWNVIPDSAELEGTVRtFDAEV- 253
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 940685535 265 HQQLQER----VNAILQTHDLNYELSWIvnglpfiteHGPlvDATVN 307
Cdd:cd05669 254 RQLVKERfeqiVEGIAAAFGAKIEFKWH---------SGP--PAVIN 289
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
185-277 |
8.75e-06 |
|
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: 47.26 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 185 FLKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDNGNEFFPATsFQVSNINGGTgAGNVIPGELEVQFNFRFSTEVT 264
Cdd:cd05670 176 HIDFIGKSGHAAYPHNANDMVVAAANFVTQLQTIVSRNVDPIDGAV-VTIGKIHAGT-ARNVIAGTAHLEGTIRTLTQEM 253
|
90
....*....|...
gi 940685535 265 HQQLQERVNAILQ 277
Cdd:cd05670 254 MELVKQRVRDIAE 266
|
|
| M20_Acy1-like |
cd05666 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
186-314 |
9.16e-05 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349916 [Multi-domain] Cd Length: 373 Bit Score: 44.05 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 186 LKVKGVQGHVAYPHLAQNPIHLAAPAITELSQTVWDNGNeffPATSFQVS--NINGGTgAGNVIPGELEVQFNFR-FSTE 262
Cdd:cd05666 177 ITIRGKGGHAAMPHLGVDPIVAAAQLVQALQTIVSRNVD---PLDAAVVSvtQIHAGD-AYNVIPDTAELRGTVRaFDPE 252
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 263 VtHQQLQERVNAILQ--------THDLNYElswivNGLPFITEHGPLVDATVNAIKSVTG 314
Cdd:cd05666 253 V-RDLIEERIREIADgiaaaygaTAEVDYR-----RGYPVTVNDAEETAFAAEVAREVVG 306
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
93-209 |
5.36e-04 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 41.76 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 93 LHGRGAADMKGSLAAMLVATERFvAKNPDHKGSISFLITSDEEG---------PFINgttkviDTLEARGEKIDMCLVGE 163
Cdd:COG4187 132 LFGRGTMDMKAGLALHLALLEEA-SENEEFPGNLLLLAVPDEEVnsagmraavPLLA------ELKEKYGLEYKLAINSE 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 940685535 164 PSSRDVLGDvvkNGRR---GS----LTGFLkVKGVQGHVAYPHLAQNPIHLAA 209
Cdd:COG4187 205 PSFPKYPGD---ETRYiytGSigklMPGFY-CYGKETHVGEPFSGLNANLLAS 253
|
|
| PLN02693 |
PLN02693 |
IAA-amino acid hydrolase |
58-293 |
6.61e-04 |
|
IAA-amino acid hydrolase
Pssm-ID: 178296 [Multi-domain] Cd Length: 437 Bit Score: 41.58 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 58 QSPHFCFAGHTDVVPTGPAQNWQHPPFSGliedGLLHGRGaadMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEGp 137
Cdd:PLN02693 101 EPPFVALRADMDALPIQEAVEWEHKSKIP----GKMHACG---HDGHVAMLLGAAKILQEHRHHLQGTVVLIFQPAEEG- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 138 fINGTTKVIDtlEARGEKIDMCLVGEPSSRDVLGDVVKngRRGSL---TGFLK--VKGVQGHVAYPHLAQNPIHLAAPAI 212
Cdd:PLN02693 173 -LSGAKKMRE--EGALKNVEAIFGIHLSPRTPFGKAAS--RAGSFmagAGVFEavITGKGGHAAIPQHTIDPVVAASSIV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 213 TELSQTVwdnGNEFFPATS--FQVSNINGGTgAGNVIPGELEVQFNFRFSTEVThqQLQERVNAILQTHDLNYELSWIVN 290
Cdd:PLN02693 248 LSLQQLV---SRETDPLDSkvVTVSKVNGGN-AFNVIPDSITIGGTLRAFTGFT--QLQQRIKEIITKQAAVHRCNASVN 321
|
...
gi 940685535 291 GLP 293
Cdd:PLN02693 322 LTP 324
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
66-114 |
7.28e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 38.36 E-value: 7.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 940685535 66 GHTDVVPtGPAQNWQHP--PFSGLIEDGLLHGRGAADMKG----SLAAM-LVATER 114
Cdd:PRK07079 92 GHGDVVR-GYDEQWREGlsPWTLTEEGDRWYGRGTADNKGqhtiNLAALeQVLAAR 146
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
60-168 |
8.72e-03 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 37.84 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940685535 60 PHFCFAGHTDVV-PTGPAQNWqhpPFSglIEDGLLHGRGAADMKGSLAAMLVATERFVAKNPDHKGSISFLITSDEEgpf 138
Cdd:PRK07473 76 PGILIAGHMDTVhPVGTLEKL---PWR--REGNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPITVLFTPDEE--- 147
|
90 100 110
....*....|....*....|....*....|
gi 940685535 139 iNGTTKVIDTLEARGEKIDMCLVGEPSSRD 168
Cdd:PRK07473 148 -VGTPSTRDLIEAEAARNKYVLVPEPGRPD 176
|
|
| |
