|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
2-383 |
0e+00 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 822.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 2 KMKLPPFIEIYRALIATPSISATDSALDQSNATLINLLAGWFGSLGFQVEVQPVPGTRNKFNMLASTGSGAGGLLLAGHT 81
Cdd:PRK05111 1 KMKLPSFIEMYRALIATPSISATDPALDQSNRAVIDLLAGWFEDLGFNVEIQPVPGTRGKFNLLASLGSGEGGLLLAGHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 82 DTVPFDDGRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPLYILATADEETSMAGARYFAETTALR 161
Cdd:PRK05111 81 DTVPFDEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKPLYILATADEETSMAGARAFAEATAIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 162 PDCAIIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDSLKERYHYDAFTVPYPTLNL 241
Cdd:PRK05111 161 PDCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDELQERYHNPAFTVPYPTLNL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 242 GHIHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEPVSLRWPGRLTVFDLHPPIPGYECPPDHKLVQVVEKLL 321
Cdd:PRK05111 241 GHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVSERWPGRITVAPLHPPIPGYECPADHQLVRVVEKLL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565652439 322 GAQTDVVNYCTEAPFIQTI-CPTLVLGPGSINQAHQPDEYLETRFIKPTRELISQVVHHFCWH 383
Cdd:PRK05111 321 GHKAEVVNYCTEAPFIQQLgCPTLVLGPGSIEQAHQPDEYLELSFIKPTRELLRQLIHHFCLH 383
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
10-377 |
0e+00 |
|
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine deacetylases from proteobacteria. This enzyme is the final step of the "acetylated" ornithine biosynthesis pathway. The enzyme is closely related to dapE, succinyl-diaminopimelate desuccinylase, and outside of this clade annotation is very inaccurate as to which function should be ascribed to genes. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130947 [Multi-domain] Cd Length: 364 Bit Score: 587.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 10 EIYRALIATPSISATdsaldqSNATLINLLAGWFGSLGFQVEVQPVPGTRNKFNMLASTG-SGAGGLLLAGHTDTVPFDD 88
Cdd:TIGR01892 1 EILTKLVAFDSTSFR------PNVDLIDWAQAYLEALGFSVEVQPFPDGAEKSNLVAVIGpSGAGGLALSGHTDVVPYDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 89 GRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPLYILATADEETSMAGARYFAETTALRPDCAIIG 168
Cdd:TIGR01892 75 AAWTRDPFRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKMIEAGAGRPRHAIIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 169 EPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDSLKERYHYDAFTVPYPTLNLGHIHGGD 248
Cdd:TIGR01892 155 EPTRLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLREDLDEGFTPPYTTLNIGVIQGGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 249 ASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEPVSLRWPGRLTVFDLHPPIPGYECPPDHKLVQVVEKLLGAQTDVV 328
Cdd:TIGR01892 235 AVNIIPGACEFVFEWRPIPGMDPEELLQLLETIAQALVRDEPGFEVQIEVVSTDPGVNTEPDAELVAFLEELSGNAPEVV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 565652439 329 NYCTEAPFIQTI-CPTLVLGPGSINQAHQPDEYLETRFIKPTRELISQVV 377
Cdd:TIGR01892 315 SYGTEAPQFQELgAEAVVCGPGDIRQAHQPDEYVEIEDLVRCRAVLARLV 364
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
10-378 |
1.14e-169 |
|
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: 478.24 E-value: 1.14e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 10 EIYRALIATPSISAtdsaldQSNATLINLLAGWFGSLGFQVEVQPVPgTRNKFNMLASTG-SGAGGLLLAGHTDTVPFDD 88
Cdd:cd03894 1 ELLARLVAFDTVSR------NSNLALIEYVADYLAALGVKSRRVPVP-EGGKANLLATLGpGGEGGLLLSGHTDVVPVDG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 89 GRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPLYILATADEETSMAGARYFAETTA---LRPDCA 165
Cdd:cd03894 74 QKWSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLIAALAargGRPDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 166 IIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDSLKERYHYDAFTVPYPTLNLGHIH 245
Cdd:cd03894 154 IVGEPTSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGLRDPPFDPPYPTLNVGLIH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 246 GGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEPVSLRWPGRLTVFDLHPPiPGYECPPDHKLVQVVEKLLG-AQ 324
Cdd:cd03894 234 GGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPEAGIEVEPLFEV-PGLETDEDAPLVRLAAALAGdNK 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 565652439 325 TDVVNYCTEAPFIQ-TICPTLVLGPGSINQAHQPDEYLETRFIKPTRELISQVVH 378
Cdd:cd03894 313 VRTVAYGTEAGLFQrAGIPTVVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
1-381 |
2.54e-109 |
|
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: 325.69 E-value: 2.54e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 1 MKMKLPPFIEIYRALIATPSISatdsaldQSNATLINLLAGWFGSLGFQVEVQPVPGtrNKFNMLAS-TGSGAG-GLLLA 78
Cdd:COG0624 7 IDAHLDEALELLRELVRIPSVS-------GEEAAAAELLAELLEALGFEVERLEVPP--GRPNLVARrPGDGGGpTLLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 79 GHTDTVPFDDG-RWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVT--QLKKPLYILATADEETSMAGARYFA 155
Cdd:COG0624 78 GHLDVVPPGDLeLWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAglRLPGNVTLLFTGDEEVGSPGARALV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 156 ETTA--LRPDCAIIGEPTS-LQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDSLKERYHYDaf 232
Cdd:COG0624 158 EELAegLKADAAIVGEPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDGRADPLFG-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 233 tvpYPTLNLGHIHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEpvSLRWPGRLTVFDLHPPIPGYECPPDHK 312
Cdd:COG0624 236 ---RTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLA--AAAPGVEVEVEVLGDGRPPFETPPDSP 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 565652439 313 LVQVVEKLLGAQTDV------VNYCTEAPFIQTI--CPTLVLGPGSINQAHQPDEYLETRFIKPTRELISQVVHHFC 381
Cdd:COG0624 311 LVAAARAAIREVTGKepvlsgVGGGTDARFFAEAlgIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
9-362 |
5.54e-96 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 291.32 E-value: 5.54e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 9 IEIYRALIATPSISATdsaldqSNATLINLLAGWFGSLGFQVEVQPVPgTRNKFNMLASTG-SGAGGLLLAGHTDTVPFD 87
Cdd:PRK07522 7 LDILERLVAFDTVSRD------SNLALIEWVRDYLAAHGVESELIPDP-EGDKANLFATIGpADRGGIVLSGHTDVVPVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 88 DGRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPLYILATADEETSMAGARYF-AETTAL--RPDC 164
Cdd:PRK07522 80 GQAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGCLGVPSMiARLPERgvKPAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 165 AIIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDSLKERYHYDA-FTVPYPTLNLGH 243
Cdd:PRK07522 160 CIVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLADRLAAPGPFDAlFDPPYSTLQTGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 244 IHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEPVSLRW-----PGRLTVFDLHPPIPGYECPPDHKLVQVVE 318
Cdd:PRK07522 240 IQGGTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAELLPEmravhPEAAIEFEPLSAYPGLDTAEDAAAARLVR 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 565652439 319 KLLGAQ-TDVVNYCTEAPFIQTI-CPTLVLGPGSINQAHQPDEYLE 362
Cdd:PRK07522 320 ALTGDNdLRKVAYGTEAGLFQRAgIPTVVCGPGSIEQAHKPDEFVE 365
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
10-362 |
1.34e-81 |
|
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like; Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline.
Pssm-ID: 349944 [Multi-domain] Cd Length: 361 Bit Score: 253.76 E-value: 1.34e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 10 EIYRALIATPSISATDSALDQsnatlinLLAGWFGSLGFQVEVQPVPGTRNkfnMLASTGSGAG-GLLLAGHTDTVPFDD 88
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAE-------YLAELLAKRGYGIESTIVEGRGN---LVATVGGGDGpVLLLNGHIDTVPPGD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 89 G-RWTRDPFTLTEHDNKLFGLGTADMKG-----FFAFIldALRDvDVTQLKKPLYILATADEETSMAGARYFAET-TALR 161
Cdd:cd08659 71 GdKWSFPPFSGRIRDGRLYGRGACDMKGglaamVAALI--ELKE-AGALLGGRVALLATVDEEVGSDGARALLEAgYADR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 162 PDCAIIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDSLKERYhydafTVPYPTLNL 241
Cdd:cd08659 148 LDALIVGEPTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPAHP-----LLGPPTLNV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 242 GHIHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEpvslRWPGRLTVFDLHPPIPGYECPPDHKLVQVVEKLL 321
Cdd:cd08659 223 GVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILE----EHEAKLTVEVSLDGDPPFFTDPDHPLVQALQAAA 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 565652439 322 GAQTD-----VVNYCTEAPFI--QTICPTLVLGPGSINQAHQPDEYLE 362
Cdd:cd08659 299 RALGGdpvvrPFTGTTDASYFakDLGFPVVVYGPGDLALAHQPDEYVS 346
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
9-377 |
3.60e-67 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 217.55 E-value: 3.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 9 IEIYRALIATPSISATDSALDQsnatLINLLAGWFGSLGFQVEVQPVPGT------RNKFNMLASTGSGAGGLLLAGHTD 82
Cdd:PRK08651 9 VEFLKDLIKIPTVNPPGENYEE----IAEFLRDTLEELGFSTEIIEVPNEyvkkhdGPRPNLIARRGSGNPHLHFNGHYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 83 TVPFDDGRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPlyILA-TADEETSMAGARYFAETTALR 161
Cdd:PRK08651 85 VVPPGEGWSVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDPAGDGNI--ELAiVPDEETGGTGTGYLVEEGKVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 162 PDCAIIGEPTSLQPI-RAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDSLKERYHYDAFTVPYPTLN 240
Cdd:PRK08651 163 PDYVIVGEPSGLDNIcIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYEYDDERGAKPTVT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 241 LG--HIHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEPVSLRWPGRLTVFDLhPPIPGYECPPDHKLVQVVE 318
Cdd:PRK08651 243 LGgpTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVEFEIT-PFSEAFVTDPDSELVKALR 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565652439 319 KLLGAQTDV---VNYCTEA----PFIQTICPTLVLGPGSINQAHQPDEYLETRFIKPTRELISQVV 377
Cdd:PRK08651 322 EAIREVLGVepkKTISLGGtdarFFGAKGIPTVVYGPGELELAHAPDEYVEVKDVEKAAKVYEEVL 387
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
76-379 |
3.99e-60 |
|
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 196.80 E-value: 3.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 76 LLAGHTDTVPFDDGrwTRDPFTLTEhDNKLFGLGTADMKGFFAFILDALRDVDVTQLKK-PLYILATADEETSMAGARYF 154
Cdd:pfam01546 1 LLRGHMDVVPDEET--WGWPFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLKKgTVKLLFQPDEEGGMGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 155 AETTALR---PDCAI---IGEPTSLQ------PIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDS 222
Cdd:pfam01546 78 IEDGLLErekVDAVFglhIGEPTLLEggiaigVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 223 LKERYHYDAFTVpyptLNLGHIHGGdaSNRICACCELHMDIRPLPGMTLDDLSGLLNEALEPVSLRWPGRLTVfDLHPPI 302
Cdd:pfam01546 158 NVDPLDPAVVTV----GNITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEV-EYVEGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 303 PGYECpPDHKLVQVVEKLLGAQTDV--------VNYCTEAPFI-QTICPTLV-LGPGSiNQAHQPDEYLETRFIKPTREL 372
Cdd:pfam01546 231 APPLV-NDSPLVAALREAAKELFGLkvelivsgSMGGTDAAFFlLGVPPTVVfFGPGS-GLAHSPNEYVDLDDLEKGAKV 308
|
....*..
gi 565652439 373 ISQVVHH 379
Cdd:pfam01546 309 LARLLLK 315
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
9-362 |
2.31e-51 |
|
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: 175.67 E-value: 2.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 9 IEIYRALIATPSISATDSALDqsnaTLINLLAGWFGSLGFQVEVQPVPGTR---NKFNMLASTGSGAGGLL-LAGHTDTV 84
Cdd:TIGR01910 1 VELLKDLISIPSVNPPGGNEE----TIANYIKDLLREFGFSTDVIEITDDRlkvLGKVVVKEPGNGNEKSLiFNGHYDVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 85 PF-DDGRWTRDPFTLTEHDNKLFGLGTADMKGFFA---FILDALRDVDVTqLKKPLYILATADEETSMAGARYFAETTAL 160
Cdd:TIGR01910 77 PAgDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVallYALKAIREAGIK-PNGNIILQSVVDEESGEAGTLYLLQRGYF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 161 R-PDCAIIGEPTSLQPI-RAHKGHISSAIRVQGQSGHSSDPERGVNAIE-LMHDaigrIMQLRDSLKERYH-YDAFTVPY 236
Cdd:TIGR01910 156 KdADGVLIPEPSGGDNIvIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMkLAKL----ITELNELEEHIYArNSYGFIPG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 237 P-TLNLGHIHGGDASNRICACCELHMDIRPLPGMTLDD----LSGLLNEAlepvslrwpGRLTVFDLHPPIP-----GYE 306
Cdd:TIGR01910 232 PiTFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEvkqiIEDVVKAL---------SKSDGWLYENEPVvkwsgPNE 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565652439 307 CPPDHKLVQVVE----KLLG--AQTDVVNYCTEAPF-IQTICPTLVLGPGSINQAHQPDEYLE 362
Cdd:TIGR01910 303 TPPDSRLVKALEaiikKVRGiePEVLVSTGGTDARFlRKAGIPSIVYGPGDLETAHQVNEYIS 365
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
47-375 |
1.81e-50 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 173.53 E-value: 1.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 47 GFQVEVQPVPGTRNkfNMLASTGSGAGGLLLAGHTDTV-PFDDGRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALr 125
Cdd:PRK08588 36 GIESKIVKVNDGRA--NLVAEIGSGSPVLALSGHMDVVaAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAM- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 126 dVDVTQLKKPLY----ILATADEETSMAGARYFAE------TTALrpdcaIIGEPTSLQPIRAHKGHISSAIRVQGQSGH 195
Cdd:PRK08588 113 -IELKEQGQLLNgtirLLATAGEEVGELGAKQLTEkgyaddLDAL-----IIGEPSGHGIVYAHKGSMDYKVTSTGKAAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 196 SSDPERGVNAIELMHDAIGRIMQLRDSLKERYHYDAFTVPYPTLnlghIHGGDASNRICACCELHMDIRPLPGMTLDDLS 275
Cdd:PRK08588 187 SSMPELGVNAIDPLLEFYNEQKEYFDSIKKHNPYLGGLTHVVTI----INGGEQVNSVPDEAELEFNIRTIPEYDNDQVI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 276 GLLNEALEPVSLRWPGRLTvFDL---HPPIpgyECPPDHKLVQ----VVEKLLGAQTDV--VNYCTEAP-FIQTI--CPT 343
Cdd:PRK08588 263 SLLQEIINEVNQNGAAQLS-LDIysnHRPV---ASDKDSKLVQlakdVAKSYVGQDIPLsaIPGATDASsFLKKKpdFPV 338
|
330 340 350
....*....|....*....|....*....|....*.
gi 565652439 344 LVLGPGSINQAHQPDEYLET----RFIKPTRELISQ 375
Cdd:PRK08588 339 IIFGPGNNLTAHQVDEYVEKdmylKFIDIYKEIIIQ 374
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
37-362 |
1.64e-49 |
|
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: 170.26 E-value: 1.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 37 NLLAGWFGSLGFQVEV-QPVPGTRNKFNMLaSTGSGAGGLLLAGHTDTVPFDDGR-WTRDPFTLTEHDNKLFGLGTADMK 114
Cdd:cd08011 25 AYIKLLLEDLGYPVELhEPPEEIYGVVSNI-VGGRKGKRLLFNGHYDVVPAGDGEgWTVDPYSGKIKDGKLYGRGSSDMK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 115 GFFAFILDALRDVDVTQLKKPLYILATA--DEET-SMAGARYFAETTALRPDCAIIGEPTSLQPIR-AHKGHISSAIRVQ 190
Cdd:cd08011 104 GGIAASIIAVARLADAKAPWDLPVVLTFvpDEETgGRAGTKYLLEKVRIKPNDVLIGEPSGSDNIRiGEKGLVWVIIEIT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 191 GQSGHSSDPERGVNAIELMHDAIGRIMQLRdslkeryhydaftvpyPTLNLGHIHGGDASNRICACCELHMDIRPLPGMT 270
Cdd:cd08011 184 GKPAHGSLPHRGESAVKAAMKLIERLYELE----------------KTVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGIS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 271 LDDLSGLLNEALEPVSLRWPGRLTVFDlhppipGYECPPDHKLVQVVE----KLLG--AQTDVVNYCTEAPF-IQTICPT 343
Cdd:cd08011 248 TDEVLSRIIDHLDSIEEVSFEIKSFYS------PTVSNPDSEIVKKTEeaitEVLGirPKEVISVGASDARFyRNAGIPA 321
|
330
....*....|....*....
gi 565652439 344 LVLGPGSINQAHQPDEYLE 362
Cdd:cd08011 322 IVYGPGRLGQMHAPNEYVE 340
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
18-381 |
1.43e-46 |
|
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: 163.42 E-value: 1.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 18 TPSISATDSAldqSNATLINLLAGWFGSLGFQVEV-QPVPGTRNKFNMLASTGSGAGgLLLAGHTDTVPFDDgrWTRDPF 96
Cdd:cd08013 17 NPSLSATGGA---GEAEIATYVAAWLAHRGIEAHRiEGTPGRPSVVGVVRGTGGGKS-LMLNGHIDTVTLDG--YDGDPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 97 TLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPLYILATADEETSMAGARYFAETTaLRPDCAIIGEPTSLQPI 176
Cdd:cd08013 91 SGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGLRGDVILAAVADEEDASLGTQEVLAAG-WRADAAIVTEPTNLQII 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 177 RAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDSLKERyHYDAFTVPyPTLNLGHIHGGDASNRICAC 256
Cdd:cd08013 170 HAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALEEYQQELPER-PVDPLLGR-ASVHASLIKGGEEPSSYPAR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 257 CELHMDIRPLPGMTLDDLSGLLNEALEPVSLRWPG---RLTVFDLHPpiPGYECPPDHKLVQVV----EKLLG--AQTDV 327
Cdd:cd08013 248 CTLTIERRTIPGETDESVLAELTAILGELAQTVPNfsyREPRITLSR--PPFEVPKEHPFVQLVaahaAKVLGeaPQIRS 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 565652439 328 VNYCTEAPFI-QTICPTLVLGPgSINQAHQPDEYLETRFIKPTRELISQVVHHFC 381
Cdd:cd08013 326 ETFWTDAALLaEAGIPSVVFGP-SGAGLHAKEEWVDVESIRQLREVLSAVVREFC 379
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
8-361 |
1.16e-44 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 157.05 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 8 FIEIYRALIATPSISATDSALDqsnatliNLLAGWFGSLGFQVEVQPVPGTrNKFNMLASTGSGAG-GLLLAGHTDTVP- 85
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVG-------DFLAEYLESLGFTVEKQPVENK-DRFNVYAYPGSSRQpRVLLTSHIDTVPp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 86 -FddgrwtrdPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKP--LYILATADEETSMAGARYFAETTALRP 162
Cdd:cd05652 73 fI--------PYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEgdLGLLFVVGEETGGDGMKAFNDLGLNTW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 163 DCAIIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDSLKERYHYDaftvpypTLNLG 242
Cdd:cd05652 145 DAVIFGEPTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPSSELLGPT-------TLNIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 243 HIHGGDASNRICACCELHMDIRPL--PGMTLDDLSGLLNEAL---EPVSLRWPGRLTVFDLhppipgyECPPDhklvqvv 317
Cdd:cd05652 218 RISGGVAANVVPAAAEASVAIRLAagPPEVKDIVKEAVAGILtdtEDIEVTFTSGYGPVDL-------DCDVD------- 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 565652439 318 ekllGAQTDVVNYCTEAPFIQTICPTLVLGPGSINQAHQPDEYL 361
Cdd:cd05652 284 ----GFETDVVAYGTDIPYLKGDHKRYLYGPGSILVAHGPDEAI 323
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
15-362 |
1.83e-39 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 144.76 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 15 LIATPSisatdsaLDQSNATLINLLAGWFGSLGFQVEVQ---------------PVPGTRNKFNMLAS-TGSGAGG--LL 76
Cdd:cd03895 6 LVRFPS-------LRGEEAAAQDLVAAALRSRGYTVDRWeidveklkhhpgfspVAVDYAGAPNVVGThRPRGETGrsLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 77 LAGHTDTVPFDDGR-WTRDPFTLTEHDNKLFGLGTADMKGFFA---FILDALRDVDVtQLKKPLYILATADEETSMAGAr 152
Cdd:cd03895 79 LNGHIDVVPEGPVElWTRPPFEATIVDGWMYGRGAGDMKAGLAanlFALDALRAAGL-QPAADVHFQSVVEEECTGNGA- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 153 yfaeTTAL----RPDCAIIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDSLKERYH 228
Cdd:cd03895 157 ----LAALmrgyRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQELEREWNARKK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 229 YD-AF-TVPYP-TLNLGHIHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALE------------PVSLRWPGRL 293
Cdd:cd03895 233 SHpHFsDHPHPiNFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEECVAdaaatdpwlsnhPPEVEWNGFQ 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 565652439 294 TvfdlhppiPGYECPPDHKLVQVV----EKLLG--AQTDVVNYCTEAPFIQTI--CPTLVLGPGSINqAHQPDEYLE 362
Cdd:cd03895 313 A--------EGYVLEPGSDAEQVLaaahQAVFGtpPVQSAMTATTDGRFFVLYgdIPALCYGPGSRD-AHGFDESVD 380
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
9-362 |
2.84e-39 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 144.31 E-value: 2.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 9 IEIYRALIATPSISATDSALdqsnatlINLLAGWFGSLGF-QVEVQPVpGtrnkfNMLASTGSGAGGLLLAGHTDTVPF- 86
Cdd:PRK13004 18 TRFLRDLIRIPSESGDEKRV-------VKRIKEEMEKVGFdKVEIDPM-G-----NVLGYIGHGKKLIAFDAHIDTVGIg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 87 DDGRWTRDPFTLTEHDNKLFGLGTADMKGFFA-------FILDALRDVDVTqlkkpLYILATADEET--SMAgARYFAET 157
Cdd:PRK13004 85 DIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMAsmvyaakIIKDLGLDDEYT-----LYVTGTVQEEDcdGLC-WRYIIEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 158 TALRPDCAIIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDSLKEryhyDAFTVPyP 237
Cdd:PRK13004 159 DKIKPDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELNPNLKE----DPFLGK-G 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 238 TLNLGHIHGgdASNRICAC---CELHMDIRPLPGMT----LDDLSGLLN--EALEPVSLRWPGRLTVFDLHPPI----PG 304
Cdd:PRK13004 234 TLTVSDIFS--TSPSRCAVpdsCAISIDRRLTVGETwesvLAEIRALPAvkKANAKVSMYNYDRPSYTGLVYPTecyfPT 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 565652439 305 YECPPDHKLVQVVEK----LLG--AQTDVVNYCTEAPFIQ---TIcPTLVLGPGSINQAHQPDEYLE 362
Cdd:PRK13004 312 WLYPEDHEFVKAAVEaykgLFGkaPEVDKWTFSTNGVSIAgraGI-PTIGFGPGKEPLAHAPNEYTW 377
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
9-362 |
3.99e-38 |
|
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: 139.75 E-value: 3.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 9 IEIYRALIATPSISAtdsalDQSNATliNLLAGWFGSLGFQVEvqpvpgtRNKFNMLASTGSGAGG---LLLAGHTDTVP 85
Cdd:cd05651 3 IELLKSLIATPSFSR-----EEHKTA--DLIENYLEQKGIPFK-------RKGNNVWAENGHFDEGkptLLLNSHHDTVK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 86 FDDGrWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDV-DVTQLKKPLYILATADEETS-MAGARyfaettALRP- 162
Cdd:cd05651 69 PNAG-WTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLySEGPLNYNLIYAASAEEEISgKNGIE------SLLPh 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 163 ----DCAIIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPErGVNAIELMHDAIGRIMQLR-DSLKEryhydafTVPYP 237
Cdd:cd05651 142 lpplDLAIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAARNE-GDNAIYKALDDIQWLRDFRfDKVSP-------LLGPV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 238 TLNLGHIHGGDASNRICACCELHMDIRPLPGMT----LDDLSGLLNEALEPVSLRwpgrltvfdLHPPipgyECPPDHKL 313
Cdd:cd05651 214 KMTVTQINAGTQHNVVPDSCTFVVDIRTTEAYTneeiFEIIRGNLKSEIKPRSFR---------LNSS----AIPPDHPI 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 565652439 314 VQVVEKlLGAQTDVVNYCTEAPFIQtiCPTLVLGPGSINQAHQPDEYLE 362
Cdd:cd05651 281 VQAAIA-AGRTPFGSPTLSDQALMP--FPSVKIGPGDSSRSHTADEFIE 326
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
9-362 |
2.83e-37 |
|
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: 138.71 E-value: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 9 IEIYRALIATPSISATDSALdqsnatlINLLAGWFGSLGF-QVEVQPVPgtrnkfNMLASTGSGAGGLLLAGHTDTVPF- 86
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGV-------VERIEEEMEKLGFdEVEIDPMG------NVIGYIGGGKKKILFDGHIDTVGIg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 87 DDGRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALR---DVDVTQLKKPLYILATADEET--SMAgARYFAETTALR 161
Cdd:cd05649 68 NIDNWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKimkDLGLRDFAYTILVAGTVQEEDcdGVC-WQYISKADKIK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 162 PDCAIIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQlrdsLKERYHYDAFtVPYPTLNL 241
Cdd:cd05649 147 PDFVVSGEPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQ----LNPNFPEAPF-LGRGTLTV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 242 GHIHggDASNRICAC---CELHMDIRPLPGMT----LDDLSGLLNE----ALEPVSLR------WPGrlTVFDLHPPIPG 304
Cdd:cd05649 222 TDIF--STSPSRCAVpdsCRISIDRRLTVGETwegcLEEIRALPAVkkygDDVAVSMYnydrpsYTG--EVYESERYFPT 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565652439 305 YECPPDHKLVQVVEK----LLGAQ--TDVVNYCTEAPFIQ--TICPTLVLGPGSINQAHQPDEYLE 362
Cdd:cd05649 298 WLLPEDHELVKALLEaykaLFGARplIDKWTFSTNGVSIMgrAGIPCIGFGPGAENQAHAPNEYTW 363
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
47-361 |
6.25e-35 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 131.86 E-value: 6.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 47 GFQVEVqpVPGTRNKFNMLASTGSGAggLLLAGHTDTVPFDDGrWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDAlrd 126
Cdd:PRK08737 42 GFQVEV--IDHGAGAVSLYAVRGTPK--YLFNVHLDTVPDSPH-WSADPHVMRRTDDRVIGLGVCDIKGAAAALLAA--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 127 vdVTQLKKPLYILATADEE--TSMAGARYFAetTALRPDCAIIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPER-GV 203
Cdd:PRK08737 114 --ANAGDGDAAFLFSSDEEanDPRCVAAFLA--RGIPYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKQDpSA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 204 NAIelmHDAIGRIMQLRDSLKERYHYDAFTVPYPTLNLGHIHGGDASNRICACCELHMDIRPLPGMTLDDL----SGLLN 279
Cdd:PRK08737 190 SAL---HQAMRWGGQALDHVESLAHARFGGLTGLRFNIGRVEGGIKANMIAPAAELRFGFRPLPSMDVDGLlatfAGFAE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 280 EALEPVSLRWPGrltvfdlhPPIPGYECPPDHK----LVQVVEKLLGAQTDVVNYCTEAP-FIQTICPTLVLGPGSINQA 354
Cdd:PRK08737 267 PAAATFEETFRG--------PSLPSGDIARAEErrlaARDVADALDLPIGNAVDFWTEASlFSAAGYTALVYGPGDIAQA 338
|
....*..
gi 565652439 355 HQPDEYL 361
Cdd:PRK08737 339 HTADEFV 345
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
9-373 |
1.63e-33 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 127.57 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 9 IEIYRALIATPSISATDSALdqsnatlINLLAGWFGSLGFQVEVQPVPGTRNKFNmlastgSGAGGLLLAGHTDTVPFdd 88
Cdd:PRK08652 5 KELLKQLVKIPSPSGQEDEI-------ALHIMEFLESLGYDVHIESDGEVINIVV------NSKAELFVEVHYDTVPV-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 89 grwTRDPFtltEHDNKLFGLGTADMKGFFAFILDALRdvdvtQLKKP-----LYILATADEETSMAGARYFAETtaLRPD 163
Cdd:PRK08652 70 ---RAEFF---VDGVYVYGTGACDAKGGVAAILLALE-----ELGKEfedlnVGIAFVSDEEEGGRGSALFAER--YRPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 164 CAIIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDSLKERYHydaftvpyPTLNLGH 243
Cdd:PRK08652 137 MAIVLEPTDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFD--------PHIGIQE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 244 IHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEPVSLRwpgrltvFDLHPPIPGYECPPDHKLVQVVEKLLGA 323
Cdd:PRK08652 209 IIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVK-------YEYTEIWDGFELDEDEEIVQLLEKAMKE 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565652439 324 Q------------TDVVNycteapFIQTICPTLVLGPGSINQAHQPDEYLETRFIKPTRELI 373
Cdd:PRK08652 282 VglepeftvmrswTDAIN------FRYNGTKTVVWGPGELDLCHTKFERIDVREVEKAKEFL 337
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
9-360 |
6.40e-33 |
|
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE; aspartyl dipeptidase; succinyl-diaminopimelate desuccinylase) subfamily. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349886 [Multi-domain] Cd Length: 366 Bit Score: 126.47 E-value: 6.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 9 IEIYRALIATPSISATDsaldqsnATLINLLAGWFGSLGFQVEVQPVPGTRNkfnMLASTGSGAGGLLLAGHTDTVPF-D 87
Cdd:cd03891 1 LELAKELIRRPSVTPDD-------AGAQDLIAERLKALGFTCERLEFGGVKN---LWARRGTGGPHLCFAGHTDVVPPgD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 88 DGRWTRDPFTLTEHDNKLFGLGTADMKGFFA-FILDALRDVDVT-QLKKPLYILATADEETSmA--GARYFAETTA---L 160
Cdd:cd03891 71 LEGWSSDPFSPTIKDGMLYGRGAADMKGGIAaFVAAAERFVAKHpNHKGSISFLITSDEEGP-AidGTKKVLEWLKargE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 161 RPDCAIIGEPTSLQPI-------RahKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQlrdslkerYHYDAFT 233
Cdd:cd03891 150 KIDYCIVGEPTSEKKLgdtikigR--RGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTA--------TVLDEGN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 234 VPYP--TLNLGHIHGG-DASNRICACCELHMDIRPLPGMTLDDLSGLLNEALE----PVSLRW----------PGRLTvf 296
Cdd:cd03891 220 EFFPpsSLQITNIDVGnGATNVIPGELKAKFNIRFNDEHTGESLKARIEAILDkhglDYDLEWklsgepfltkPGKLV-- 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565652439 297 DLhppipgyecppdhkLVQVVEKLLGAQTDVVNY--CTEAPFI-QTICPTLVLGPgsINQ-AHQPDEY 360
Cdd:cd03891 298 DA--------------VSAAIKEVTGITPELSTSggTSDARFIaSYGCPVVEFGL--VNAtIHKVNER 349
|
|
| selenium_YgeY |
TIGR03526 |
putative selenium metabolism hydrolase; SelD, selenophosphate synthase, is the selenium donor ... |
6-360 |
7.03e-32 |
|
putative selenium metabolism hydrolase; SelD, selenophosphate synthase, is the selenium donor protein for both selenocysteine and selenouridine biosynthesis systems, but it occurs also in a few prokaryotes that have neither of those pathways. The method of partial phylogenetic profiling, starting from such orphan-selD genomes, identifies this protein as one of those most strongly correlated to SelD occurrence. Its distribution is also well correlated with that of family TIGR03309, a putative accessory protein of labile selenium (non-selenocysteine) enzyme maturation. This family includes the uncharacterized YgeY of Escherichia coli, and belongs to a larger family of metalloenzymes in which some are known peptidases, others enzymes of different types.
Pssm-ID: 132565 [Multi-domain] Cd Length: 395 Bit Score: 124.14 E-value: 7.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 6 PPFIEIYRALIATPSISATDSALdqsnatlINLLAGWFGSLGF-QVEVQPVPgtrnkfNMLASTGSGAGGLLLAGHTDTV 84
Cdd:TIGR03526 13 GDMIRFLRDLVAIPSESGDEGRV-------ALRIKQEMEKLGFdKVEIDPMG------NVLGYIGHGPKLIAMDAHIDTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 85 PF-DDGRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDA---LRDVDVTQlKKPLYILATADEETSMAGA-RYFAETTA 159
Cdd:TIGR03526 80 GIgDMDQWQFDPYEGYEDEEIIYGRGASDQEGGIASMVYAgkiIKDLGLLD-DYTLLVTGTVQEEDCDGLCwQYIIEEDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 160 LRPDCAIIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDSLKEryhyDAFtVPYPTL 239
Cdd:TIGR03526 159 IKPEFVVITEPTDMNIYRGQRGRMEIKVTVKGVSCHGSAPERGDNAIYKMAPILKELSQLNANLVE----DPF-LGKGTL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 240 NLGHIHGGDASnrICAC---CELHMDIRPLPG----MTLDDLSGL--LNEALEPVSLRWPGRLTVFDLHPPI----PGYE 306
Cdd:TIGR03526 234 TVSEIFFSSPS--RCAVadgCTISIDRRLTWGetweYALEQIRNLpaVQGAEAEVEMYEYDRPSYTGLVYPTecyfPTWV 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565652439 307 CPPDHKLVQVVEKL---LGAQTDVVN---YCTEAPFI--QTICPTLVLGPGSINQAHQPDEY 360
Cdd:TIGR03526 312 LPEDHLITKAALETykrLFGKEPGVDkwtFSTNGVSImgRHGIPVIGFGPGDEDQAHAPNEK 373
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
177-290 |
1.29e-30 |
|
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: 112.82 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 177 RAHKGHISSAIRVQGQSGHSSDPERGVNAIELMhdaigriMQLRDSLKERYHYDAFTVPYPTLNLGHIHGGDASNRICAC 256
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLL-------ARLLAELPAEYGDIGFDFPRTTLNITGIEGGTATNVIPAE 73
|
90 100 110
....*....|....*....|....*....|....
gi 565652439 257 CELHMDIRPLPGMTLDDLSGLLNEALEPVSLRWP 290
Cdd:pfam07687 74 AEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
11-323 |
6.35e-30 |
|
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: 119.39 E-value: 6.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 11 IYRALIAtpsISATDSALDQSNAT-LINLLAGWFGSLGFQVE---VQPVPGTRNKFNMLASTGSGAGGLLLAGHTDTVPF 86
Cdd:cd05675 3 LLQELIR---IDTTNSGDGTGSETrAAEVLAARLAEAGIQTEifvVESHPGRANLVARIGGTDPSAGPLLLLGHIDVVPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 87 DDGRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDV--DVTQLKKPLYILATADEET-SMAGARYFAETtalRPD 163
Cdd:cd05675 80 DASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYkrEGFKPKRDLVFAFVADEEAgGENGAKWLVDN---HPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 164 C------AI---------IGEPTSLQPIR-AHKGHISSAIRVQGQSGHSSDPERGvNAIELMHDAIGRI------MQLRD 221
Cdd:cd05675 157 LfdgatfALneggggslpVGKGRRLYPIQvAEKGIAWMKLTVRGRAGHGSRPTDD-NAITRLAEALRRLgahnfpVRLTD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 222 SLKERYHYDAFTVPY-------------PTLN-LGH-----------------IHGGDASNRICACCELHMDIRPLPGMT 270
Cdd:cd05675 236 ETAYFAQMAELAGGEggalmltavpvldPALAkLGPsapllnamlrntasptmLDAGYATNVLPGRATAEVDCRILPGQS 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 565652439 271 LDDLSGLLNEALEP--VSLRWPGRltvfdlhppIPGYECPPDHKLVQVVEKLLGA 323
Cdd:cd05675 316 EEEVLDTLDKLLGDpdVSVEAVHL---------EPATESPLDSPLVDAMEAAVQA 361
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
9-362 |
2.06e-29 |
|
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: 116.30 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 9 IEIYRALIATPSISAtdsaldqSNATLINLLAGWFGSLGFQVEVQPVPgtrnkfNMLASTGSGAGGLLLAGHTDTVPfdd 88
Cdd:cd05653 4 VELLLDLLSIYSPSG-------EEARAAKFLEEIMKELGLEAWVDEAG------NAVGGAGSGPPDVLLLGHIDTVP--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 89 grwtrDPFTLTEHDNKLFGLGTADMKG-FFAFILDALRDVDVTQLKkpLYILATADEETSMAGARYFAEtTALRPDCAII 167
Cdd:cd05653 68 -----GEIPVRVEGGVLYGRGAVDAKGpLAAMILAASALNEELGAR--VVVAGLVDEEGSSKGARELVR-RGPRPDYIII 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 168 GEPTSLQPIR-AHKGHISSAIRVQGQSGHSSDPERgvNAIELMHDAIGRIMQlRDSLKERYHYDAFTVpYPTLnlghIHG 246
Cdd:cd05653 140 GEPSGWDGITlGYRGSLLVKIRCEGRSGHSSSPER--NAAEDLIKKWLEVKK-WAEGYNVGGRDFDSV-VPTL----IKG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 247 GDASNRICACCELHMDIR-PLPGMTLDDLSgllnEALEPVSlrwPGRLTVFDLHPPipgYECPPDHKLVQVVEKLLGAQ- 324
Cdd:cd05653 212 GESSNGLPQRAEATIDLRlPPRLSPEEAIA----LATALLP---TCELEFIDDTEP---VKVSKNNPLARAFRRAIRKQg 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 565652439 325 ----------TDVVNycTEAPFIQtiCPTLVLGPGSINQAHQPDEYLE 362
Cdd:cd05653 282 gkprlkrktgTSDMN--VLAPLWT--VPIVAYGPGDSTLDHTPNEHIE 325
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
68-360 |
2.21e-29 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 117.80 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 68 TGSGAGG--LLLAGHTDTVPFDD-GRWTRDPFTLTEHDNKLFGLGTADMKGFFA---FILDALRDVDVtQLKKPLYILAT 141
Cdd:PRK06837 91 RPAGKTGrsLILQGHIDVVPEGPlDLWSRPPFDPVIVDGWMYGRGAADMKAGLAamlFALDALRAAGL-APAARVHFQSV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 142 ADEETSMAGARyfaeTTALR---PDCAIIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQ 218
Cdd:PRK06837 170 IEEESTGNGAL----STLQRgyrADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALRE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 219 LRDSLKERYHYDAF--TVPYP-TLNLGHIHGGDASNRICACCELHMDIRPLPGMTLDD----LSGLLNEAL--------E 283
Cdd:PRK06837 246 LEAEWNARKASDPHfeDVPHPiNFNVGIIKGGDWASSVPAWCDLDCRIAIYPGVTAADaqaeIEACLAAAArddrflsnN 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 284 PVSLRWPGRLTvfdlhppiPGYECPPD----------HKLV---QVVEKLLGAQTDVVNYCTEAPFiqticPTLVLGPGS 350
Cdd:PRK06837 326 PPEVVWSGFLA--------EGYVLEPGseaeaalaraHAAVfggPLRSFVTTAYTDTRFYGLYYGI-----PALCYGPSG 392
|
330
....*....|
gi 565652439 351 INqAHQPDEY 360
Cdd:PRK06837 393 EG-IHGFDER 401
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
9-360 |
1.36e-28 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 114.80 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 9 IEIYRALIATPSISATDS-ALDqsnaTLINLLAGwfgsLGFQVEVQPVPGTRNkfnMLASTGSGAGGLLLAGHTDTVPF- 86
Cdd:PRK13009 5 LELAQDLIRRPSVTPDDAgCQD----LLAERLEA----LGFTCERMDFGDVKN---LWARRGTEGPHLCFAGHTDVVPPg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 87 DDGRWTRDPFTLTEHDNKLFGLGTADMKGFFA-FILDALRDVDVT-QLKKPLYILATADEETSmA--GARYFAETTA--- 159
Cdd:PRK13009 74 DLEAWTSPPFEPTIRDGMLYGRGAADMKGSLAaFVVAAERFVAAHpDHKGSIAFLITSDEEGP-AinGTVKVLEWLKarg 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 160 LRPDCAIIGEPTSLQPI-------RahKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQlrdslkerYHYDAF 232
Cdd:PRK13009 153 EKIDYCIVGEPTSTERLgdvikngR--RGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAA--------TEWDEG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 233 TVPYP--TLNLGHIHGG-DASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEPVSLRWpgrltvfDLHPPIPGYecP- 308
Cdd:PRK13009 223 NEFFPptSLQITNIDAGtGATNVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGLDY-------TLEWTLSGE--Pf 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565652439 309 --PDHKLVQVVEKllgAQTDVVNYCTE---------APFIQTICPTLV-LGPgsINQ-AHQPDEY 360
Cdd:PRK13009 294 ltPPGKLVDAVVA---AIEAVTGITPElstsggtsdARFIADYGAQVVeFGP--VNAtIHKVNEC 353
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
37-264 |
1.43e-28 |
|
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: 114.22 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 37 NLLAGWFGSLGFQVEVQPVPGTRNkfNMLA-STGSGAGGLLLAGHTDTVpFDDGRWTRDPFTltEHDNKLFGLGTADMKG 115
Cdd:cd03885 26 ELLAEELEALGFTVERRPLGEFGD--HLIAtFKGTGGKRVLLIGHMDTV-FPEGTLAFRPFT--VDGDRAYGPGVADMKG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 116 FFAFILDALRDVDVTQLKK--PLYILATADEETSMAGARYFAETTALRPDCAIIGEPTSL--QPIRAHKGHISSAIRVQG 191
Cdd:cd03885 101 GLVVILHALKALKAAGGRDylPITVLLNSDEEIGSPGSRELIEEEAKGADYVLVFEPARAdgNLVTARKGIGRFRLTVKG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565652439 192 QSGHSS-DPERGVNAIELMHDAIGRIMQLRDslkeryhYDAFTvpypTLNLGHIHGGDASNRICACCELHMDIR 264
Cdd:cd03885 181 RAAHAGnAPEKGRSAIYELAHQVLALHALTD-------PEKGT----TVNVGVISGGTRVNVVPDHAEAQVDVR 243
|
|
| PRK06915 |
PRK06915 |
peptidase; |
68-381 |
2.35e-27 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 112.09 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 68 TGSGAG-GLLLAGHTDTVPFDD-GRWTRDPFTLTEHDNKLFGLGTADMKG-----FFAfiLDALRDVDVtQLKKPLYILA 140
Cdd:PRK06915 88 KGSGGGkSMILNGHIDVVPEGDvNQWDHHPYSGEVIGGRIYGRGTTDMKGgnvalLLA--MEALIESGI-ELKGDVIFQS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 141 TADEETSMAGARyfaeTTALR---PDCAIIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIE-LMH--DAIG 214
Cdd:PRK06915 165 VIEEESGGAGTL----AAILRgykADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEkSMFviDHLR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 215 RIMQLR-----DSLkeryhYDAFTVPYPtLNLGHIHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALE------ 283
Cdd:PRK06915 241 KLEEKRndritDPL-----YKGIPIPIP-INIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWIAelndvd 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 284 ------PVSLRWPGRLTVfdlhppiPGyECPPDHKLVQVV----EKLLGAQ--TDVVNYCTEAPFIQTI--CPTLVLGPG 349
Cdd:PRK06915 315 ewfvehPVEVEWFGARWV-------PG-ELEENHPLMTTLehnfVEIEGNKpiIEASPWGTDGGLLTQIagVPTIVFGPG 386
|
330 340 350
....*....|....*....|....*....|..
gi 565652439 350 SINQAHQPDEYLETRFIKPTRELISQVVHHFC 381
Cdd:PRK06915 387 ETKVAHYPNEYIEVDKMIAAAKIIALTLLDWC 418
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
21-362 |
4.49e-26 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 107.44 E-value: 4.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 21 ISATDSaldQSN--ATLINLLAGWFGSLGFQVEVqpvpgtRNKFNML----ASTGSGAGGLLLAGHTDTVP--------- 85
Cdd:COG2195 12 YVKIPT---PSDheEALADYLVEELKELGLEVEE------DEAGNVIatlpATPGYNVPTIGLQAHMDTVPqfpgdgikp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 86 -FDDGRWTRDPFTLtehdnklfgLGtADMKGFFAFILDALRDVDVTQLK-KPLYILATADEETSMAGARYFaETTALRPD 163
Cdd:COG2195 83 qIDGGLITADGTTT---------LG-ADDKAGVAAILAALEYLKEPEIPhGPIEVLFTPDEEIGLRGAKAL-DVSKLGAD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 164 CAII---GEPTSLQpirahkghISSA------IRVQGQSGHSSD-PERGVNAIELMHDAIGRIMQLRDslkeryhyDAFT 233
Cdd:COG2195 152 FAYTldgGEEGELE--------YECAgaadakITIKGKGGHSGDaKEKMINAIKLAARFLAALPLGRI--------PEET 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 234 vpypTLNLGHIHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEPVSLRWP-GRLTVfDLHPPIPGYECPPDHK 312
Cdd:COG2195 216 ----EGNEGFIHGGSATNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGvGVVEV-EIEDQYPNWKPEPDSP 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565652439 313 LVQVVEKL---LGAQtdvvnycteaPFIQTI-----C--------PTLVLGPGsINQAHQPDEYLE 362
Cdd:COG2195 291 IVDLAKEAyeeLGIE----------PKIKPIrggldGgilsfkglPTPNLGPG-GHNFHSPDERVS 345
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
38-364 |
9.57e-26 |
|
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: 106.41 E-value: 9.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 38 LLAGWFGSLGFQ-VEVQPVpgtrnkFNMLAS-TGSGAG-GLLLAGHTDTVPFDDgrwtrDPFTLTEHDNKLFGLGTADMK 114
Cdd:cd03896 23 LVAEWMADLGLGdVERDGR------GNVVGRlRGTGGGpALLFSAHLDTVFPGD-----TPATVRHEGGRIYGPGIGDNK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 115 GFFAFIL---DALRDVDVTqLKKPLYILATADEETS--MAGARYFAETTALRPDCAIIGEPTSLQPIRAHKGHISSAIRV 189
Cdd:cd03896 92 GSLACLLamaRAMKEAGAA-LKGDVVFAANVGEEGLgdLRGARYLLSAHGARLDYFVVAEGTDGVPHTGAVGSKRFRITT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 190 QGQSGHSSDPERGVNAIELMhdaigriMQLRDSLKErYHYDAftVPYPTLNLGHIHGGDASNRICACCELHMDIRPLPGM 269
Cdd:cd03896 171 VGPGGHSYGAFGSPSAIVAM-------AKLVEALYE-WAAPY--VPKTTFAAIRGGGGTSVNRIANLCSMYLDIRSNPDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 270 TLDDLSGLLNEALEPVSLRWPG---RLTVFDLHppiPGYECPPDHKLVQ---VVEKLLGAQTDVVNYCTEA-PFIQTICP 342
Cdd:cd03896 241 ELADVQREVEAVVSKLAAKHLRvkaRVKPVGDR---PGGEAQGTEPLVNaavAAHREVGGDPRPGSSSTDAnPANSLGIP 317
|
330 340
....*....|....*....|..
gi 565652439 343 TLVLGPGSINQAHQPDEYLETR 364
Cdd:cd03896 318 AVTYGLGRGGNAHRGDEYVLKD 339
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
9-362 |
1.65e-25 |
|
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: 105.60 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 9 IEIYRALIATPSISATDSAL-DQSNATLINLlagwfgslgfqvevQPVPGTRNKFNMLASTGSG-AGGLLLAGHTDTVPF 86
Cdd:cd05647 2 IELTAALVDIPSVSGNEKPIaDEIEAALRTL--------------PHLEVIRDGNTVVARTERGlASRVILAGHLDTVPV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 87 DD---GRWtrdpftltEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPLYILATADEETSMA--GARYFAETTA-- 159
Cdd:cd05647 68 AGnlpSRV--------EEDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHDLTLIFYDCEEVAAElnGLGRLAEEHPew 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 160 LRPDCAIIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRdslKERYHYDAFTVpYPTL 239
Cdd:cd05647 140 LAADFAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLAAYE---PRTVNIDGLTY-REGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 240 NLGHIHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEPVSLRWpgrlTVFDLHP-PIPGYECPPDHKLVQVV- 317
Cdd:cd05647 216 NAVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLGYEI----EVTDLSPgALPGLDHPVARDLIEAVg 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 565652439 318 EKLLGAQ--TDVvnycteAPFIQTICPTLVLGPGSINQAHQPDEYLE 362
Cdd:cd05647 292 GKVRAKYgwTDV------ARFSALGIPAVNFGPGDPLLAHKRDEQVP 332
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
1-362 |
1.25e-23 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 100.42 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 1 MKMKLPPfIEIYRALIATPSISATDSALDQsnatlinLLAGWFGSLGFQVEVQPVpGtrnkfNMLASTGSGAGGLLLAGH 80
Cdd:PRK04443 2 TISALEA-RELLKGLVEIPSPSGEEAAAAE-------FLVEFMESHGREAWVDEA-G-----NARGPAGDGPPLVLLLGH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 81 TDTVPFD------DGrwtrdpftltehdnKLFGLGTADMKG-FFAFILDALRdvdVTQLKKPLYILATA-DEETSMAGAR 152
Cdd:PRK04443 68 IDTVPGDipvrveDG--------------VLWGRGSVDAKGpLAAFAAAAAR---LEALVRARVSFVGAvEEEAPSSGGA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 153 YFAETTaLRPDCAIIGEPTSLQPIR-AHKGHISSAIRVQGQSGHSSDPErgVNAIELMHDAIGRIMQLRDSLKERYH-YD 230
Cdd:PRK04443 131 RLVADR-ERPDAVIIGEPSGWDGITlGYKGRLLVTYVATSESFHSAGPE--PNAAEDAIEWWLAVEAWFEANDGRERvFD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 231 AFTvpyPTLNLGHIHGGDASNRicacCELHMDIRPLPGMTLDDLSGLLNEALEPVSLRWPGrltvfdlhpPIPGYECPPD 310
Cdd:PRK04443 208 QVT---PKLVDFDSSSDGLTVE----AEMTVGLRLPPGLSPEEAREILDALLPTGTVTFTG---------AVPAYMVSKR 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565652439 311 HKLVQ--------------VVEKLLGAQTDVVnycteAPFIQtiCPTLVLGPGSINQAHQPDEYLE 362
Cdd:PRK04443 272 TPLARafrvaireaggtprLKRKTGTSDMNVV-----APAWG--CPMVAYGPGDSDLDHTPDEHLP 330
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
6-368 |
2.63e-22 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 97.39 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 6 PPFIEIYRALIATPSISATDSALDQsnatLINLLAGWFGSLGFQVEVQPVPGTRNKfNMLAS-TGSGAGGLLLAGHTDTV 84
Cdd:PRK06133 37 PAYLDTLKELVSIESGSGDAEGLKQ----VAALLAERLKALGAKVERAPTPPSAGD-MVVATfKGTGKRRIMLIAHMDTV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 85 pFDDGRWTRDPFTltEHDNKLFGLGTADMKGFFAFILDA---LRDVDVTQLKKpLYILATADEETSMAGARYFAETTALR 161
Cdd:PRK06133 112 -YLPGMLAKQPFR--IDGDRAYGPGIADDKGGVAVILHAlkiLQQLGFKDYGT-LTVLFNPDEETGSPGSRELIAELAAQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 162 PDCAIIGEPT----SLqpIRAHKGHISSAIRVQGQSGHS-SDPERGVNA-IELMHdaigRIMQLRDSLKEryhydaftVP 235
Cdd:PRK06133 188 HDVVFSCEPGrakdAL--TLATSGIATALLEVKGKASHAgAAPELGRNAlYELAH----QLLQLRDLGDP--------AK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 236 YPTLNLGHIHGGDASNRICACCELHMDIRPL-PGMT---LDDLSGLLNEALEP---VSLRWPGRLtvfdlhPPIPgyECP 308
Cdd:PRK06133 254 GTTLNWTVAKAGTNRNVIPASASAQADVRYLdPAEFdrlEADLQEKVKNKLVPdteVTLRFERGR------PPLE--ANA 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565652439 309 PDHKLVQ--------------VVEKLLGAQTD--VVNYCTEAPFIQTICptlVLGPGsinqAHQPDEYLETRFIKP 368
Cdd:PRK06133 326 ASRALAEhaqgiygelgrrlePIDMGTGGGTDaaFAAGSGKAAVLEGFG---LVGFG----AHSNDEYIELNSIVP 394
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
12-361 |
1.55e-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: 95.47 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 12 YRALIATPSISATDSALDQSNaTLINLLAGWFGSLGFQVE-VQPVPGTRNKFNMLASTGsGAGGLLLAGHTDTVPFDD-G 89
Cdd:cd03893 4 LAELVAIPSVSAQPDRREELR-RAAEWLADLLRRLGFTVEiVDTSNGAPVVFAEFPGAP-GAPTVLLYGHYDVQPAGDeD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 90 RWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPLYI--LATADEETSMAGARYFAETTA--LRPDCA 165
Cdd:cd03893 82 GWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVkfIIEGEEESGSPSLDQLVEAHRdlLAADAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 166 IIGEPTSLQPIR-----AHKGHISSAIRVQGQSG--HSS-------DP-ERGVNAIELMHDAIGRIM--QLRDSLK---- 224
Cdd:cd03893 162 VISDSTWVGQEQptltyGLRGNANFDVEVKGLDHdlHSGlyggvvpDPmTALAQLLASLRDETGRILvpGLYDAVRelpe 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 225 ERYHYDAfTVP-------------------YPTLNL----GHIHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEA 281
Cdd:cd03893 242 EEFRLDA-GVLeeveiiggttgsvaerlwtRPALTVlgidGGFPGEGSKTVIPPRARAKISIRLVPGQDPEEASRLLEAH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 282 LEPVSlRWPGRLTVFDLHPPIPgYECPPDHKLVQVVEKLL----GAQTDVVNYCTEAPFIQTI-----CPTLVLGPGSIN 352
Cdd:cd03893 321 LEKHA-PSGAKVTVSYVEGGMP-WRSDPSDPAYQAAKDALrtayGVEPPLTREGGSIPFISVLqefpqAPVLLIGVGDPD 398
|
410
....*....|
gi 565652439 353 -QAHQPDEYL 361
Cdd:cd03893 399 dNAHSPNESL 408
|
|
| dapE-gram_pos |
TIGR01900 |
succinyl-diaminopimelate desuccinylase; This model represents a clade of ... |
9-363 |
2.12e-21 |
|
succinyl-diaminopimelate desuccinylase; This model represents a clade of succinyl-diaminopimelate desuccinylases from actinobacteria (high-GC gram positives), delta-proteobacteria and aquificales and is based on the characterization of the enzyme from Corynebacterium glutamicum. This enzyme is involved in the biosynthesis of lysine, and is related to the enzyme acetylornithine deacetylase and other amidases and peptidases found within pfam01546. Other sequences included in the seed of this model were assessed to confirm that 1) the related genes DapC (succinyl-diaminopimelate transaminase) and DapD (2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase) are also found in the genome, 2) each is found only once in those genomes, 3) the lysine biosynthesis pathway is complete and 4) the direct (TIGR03540 or TIGR03542) or acetylated (GenProp0787) aminotransferase pathways are absent in thes genomes. Additionally, a number of the seed members are observed adjacent to either DapC or DapD (often as a divergon with a putative promoter site between them. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273864 [Multi-domain] Cd Length: 351 Bit Score: 93.89 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 9 IEIYRALIATPSISATDSAL-DQSNATLiNLLAGWfgslgfqvEVqpvpgTRNKFNMLASTGSG-AGGLLLAGHTDTVPF 86
Cdd:TIGR01900 6 AELTAALVDIPSVSGDERALaDAVESAL-RALPHL--------EV-----IRHGNSVVARTNLGrPSRVILAGHLDTVPI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 87 DDGrwtrdpFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPLYILATADEETSmagaryfAETTALRP---- 162
Cdd:TIGR01900 72 ADN------LPSRVEGGRLYGRGAVDMKGGLAVMLALAATLDRTEPRHDLTLVFYEREEGP-------AEENGLGRllre 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 163 -------DCAIIGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIelmHDAIGRIMQLRDSLKERYHYDAFTVp 235
Cdd:TIGR01900 139 hpewlagDLAVLLEPTDGKIEAGCQGTLRATVTFHGRRAHSARSWMGENAI---HKAAPILARLAAYEPREVTVDGLTY- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 236 YPTLNLGHIHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEpvslRWPGRLTVFDLHPP-IPGYECPPDHKLV 314
Cdd:TIGR01900 215 REGLNAVRIEGGVAGNVIPDECEVNVNYRFAPDRSLEQARAHVRELFE----GDGAEVEVTDLSPGaRPGLDNPLAAELV 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 565652439 315 -----QVVEKLlgAQTDVvnycteAPFIQTICPTLVLGPGSINQAHQPDEYLET 363
Cdd:TIGR01900 291 aavggEVRAKY--GWTDV------ARFSALGIPAVNFGPGDPALAHQDDEHVPV 336
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
37-360 |
3.53e-21 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 94.44 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 37 NLLAGWFGSLGFQVEV---QPVPGTRNKF---NMLASTGSGAGGLL--LAGHTDTVPFDDGrWTRDPFTLTEHDNKLFGL 108
Cdd:PRK13013 41 EFLAARLAPRGFEVELiraEGAPGDSETYprwNLVARRQGARDGDCvhFNSHHDVVEVGHG-WTRDPFGGEVKDGRIYGR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 109 GTADMKGFFA---FILDALRDVDVtQLKKPLYILATADEET-SMAGARYFAET---TALRPDCAIIGEPTSLQPI-RAHK 180
Cdd:PRK13013 120 GACDMKGGLAasiIAAEAFLAVYP-DFAGSIEISGTADEESgGFGGVAYLAEQgrfSPDRVQHVIIPEPLNKDRIcLGHR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 181 GHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDSLKERYHYDAFTVP----YPTLNLGHIHGG------DAS 250
Cdd:PRK13013 199 GVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAEIEERLFPLLATRRTAMPVVPegarQSTLNINSIHGGepeqdpDYT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 251 NRICAC----CELHMDIRPLPGMTLDDLSGLLNEALEPVSLRWPGRL----TVFDLHPPIPGYECPPDHKLVQVVEKLLG 322
Cdd:PRK13013 279 GLPAPCvadrCRIVIDRRFLIEEDLDEVKAEITALLERLKRARPGFAyeirDLFEVLPTMTDRDAPVVRSVAAAIERVLG 358
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 565652439 323 AQTD-VVNYCT----EAPFIQTICPTLVLGPGSINQAHQPDEY 360
Cdd:PRK13013 359 RQADyVVSPGTydqkHIDRIGKLKNCIAYGPGILDLAHQPDEW 401
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
9-367 |
9.79e-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: 92.52 E-value: 9.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 9 IEIYRALIATPSI---SATDSALDQSNAtlinlLAGWFGSLGF-QVEVQPVPGTRNKF--NMLASTGSGAGGLL-LAGHT 81
Cdd:cd05650 4 IELERDLIRIPAVnpeSGGEGEKEKADY-----LEKKLREYGFyTLERYDAPDERGIIrpNIVAKIPGGNDKTLwIISHL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 82 DTVPFDD-GRWTRDPFTLTEHDNKLFGLGTAD-MKGFFA--FILDALRDVDVTQlKKPLYILATADEET-SMAGARYFAE 156
Cdd:cd05650 79 DTVPPGDlSLWETDPWEPVVKDGKIYGRGVEDnQQGIVSslLALKAIIKNGITP-KYNFGLLFVADEEDgSEYGIQYLLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 157 TTAL-RPDCAII----GEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNA-------IELMHDAIGRIMQLRDSLk 224
Cdd:cd05650 158 KFDLfKKDDLIIvpdfGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAfvaasnfALELDELLHEKFDEKDDL- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 225 eryhydaFTVPYPTL----------NLGHIHGGDasnricaccELHMDIRPLPGMTLDDLSGLLNEALEPVSLRWPGRLT 294
Cdd:cd05650 237 -------FNPPYSTFeptkkeanvpNVNTIPGYD---------VFYFDCRVLPTYKLDEVLKFVNKIISDFENSYGAGIT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 295 VFDLHPPIPGYECPPD----HKLVQVVEKLLGAQTDV--VNYCTEAPFIQTI-CPTLVLGPGsINQAHQPDEYletRFIK 367
Cdd:cd05650 301 YEIVQKEQAPPATPEDseivVRLSKAIKKVRGREAKLigIGGGTVAAFLRKKgYPAVVWSTL-DETAHQPNEY---IRIS 376
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
8-362 |
1.51e-20 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 92.41 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 8 FIEIYRALIA--TPSISATDSALDQsnatliNLLAGWFGSLGFQVEVQPV-PGTRNKFNMLASTGSGA-GGLLLAGHTDT 83
Cdd:PRK08596 15 LLELLKTLVRfeTPAPPARNTNEAQ------EFIAEFLRKLGFSVDKWDVyPNDPNVVGVKKGTESDAyKSLIINGHMDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 84 VPFDDGR-WTRDPFTLTEHDNKLFGLGTADMKGFFA---FILDALRDVDVtQLKKPLYILATADEETSMAGARYFAEtTA 159
Cdd:PRK08596 89 AEVSADEaWETNPFEPTIKDGWLYGRGAADMKGGLAgalFAIQLLHEAGI-ELPGDLIFQSVIGEEVGEAGTLQCCE-RG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 160 LRPDCAIIGEPTSLQpIRAHKGHISSAIRVQG----------QSGHSSDPERGVNAIELMHDAIGRIMQLrdslkERyHY 229
Cdd:PRK08596 167 YDADFAVVVDTSDLH-MQGQGGVITGWITVKSpqtfhdgtrrQMIHAGGGLFGASAIEKMMKIIQSLQEL-----ER-HW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 230 dAFTVPYP-------TLNLGHIHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEAL------------EPVSLRWP 290
Cdd:PRK08596 240 -AVMKSYPgfppgtnTINPAVIEGGRHAAFIADECRLWITVHFYPNETYEQVIKEIEEYIgkvaaadpwlreNPPQFKWG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 291 GRLTVFDLHPPIPGYECPPDHKLVQVvekLLGAQTDVVNYCTEAPFIQTIC----------PTLVLGPGSINQAHQPDEY 360
Cdd:PRK08596 319 GESMIEDRGEIFPSLEIDSEHPAVKT---LSSAHESVLSKNAILDMSTTVTdggwfaefgiPAVIYGPGTLEEAHSVNEK 395
|
..
gi 565652439 361 LE 362
Cdd:PRK08596 396 VE 397
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
8-216 |
4.97e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 91.22 E-value: 4.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 8 FIEIYRALIATPSISATDSALDQSNATLINLLAGWFGSLGFQVEVqPVPGTRNkfnmLAST--GSGAGG-LLLAGHTDTV 84
Cdd:PRK09133 39 ARDLYKELIEINTTASTGSTTPAAEAMAARLKAAGFADADIEVTG-PYPRKGN----LVARlrGTDPKKpILLLAHMDVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 85 PFDDGRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALrdvdvTQLK----KP---LYILATADEE-TSMAGARYFAE 156
Cdd:PRK09133 114 EAKREDWTRDPFKLVEENGYFYGRGTSDDKADAAIWVATL-----IRLKregfKPkrdIILALTGDEEgTPMNGVAWLAE 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565652439 157 TT--ALRPDCAI----------IGEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPeRGVNAIELMHDAIGRI 216
Cdd:PRK09133 189 NHrdLIDAEFALneggggtldeDGKPVLLTVQAGEKTYADFRLEVTNPGGHSSRP-TKDNAIYRLAAALSRL 259
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
45-362 |
9.35e-19 |
|
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: 87.30 E-value: 9.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 45 SLGFQvevqpvpgTRNKFNMLASTGSGAGGLLLA--GHTDTVPFDDGrWTRDPFTLTEHDNKLFGLGTADMKG-----FF 117
Cdd:cd03888 50 RLGFK--------TKNIDNYAGYAEYGEGEEVLGilGHLDVVPAGEG-WTTDPFKPVIKDGKLYGRGTIDDKGptiaaLY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 118 AfiLDALRDVDVtQLKKPLYILATADEETSMAG-ARYFAE----TTALRPDC---AIIGEPTSLQ-----PIRAHKGH-- 182
Cdd:cd03888 121 A--LKILKDLGL-PLKKKIRLIFGTDEETGWKCiEHYFEHeeypDFGFTPDAefpVINGEKGIVTvdltfKIDDDKGYrl 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 183 --ISSAIR------------------------------------------VQGQSGHSSDPERGVNAIELM--------- 209
Cdd:cd03888 198 isIKGGEAtnmvpdkaeavipgkdkeelalsaatdlkgnieiddggveltVTGKSAHASAPEKGVNAITLLakflaelnk 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 210 ----HDAIGRimqLRDSLKERYHYDAFTVPYP-------TLNLGHIHGGDASNricaccELHMDIRPLPGMTLDDLSGLL 278
Cdd:cd03888 278 dgndKDFIKF---LAKNLHEDYNGKKLGINFEdevmgelTLNPGIITLDDGKL------ELGLNVRYPVGTSAEDIIKQI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 279 NEALEpvslRWPGRLTVFDLHPPIpgYeCPPDHKLV----QVVEKLLGAQTDVV-----NYCTEAPFIQTICPTLvlgPG 349
Cdd:cd03888 349 EEALE----KYGVEVEGHKHQKPL--Y-VPKDSPLVktllKVYEEQTGKEGEPVaigggTYARELPNGVAFGPEF---PG 418
|
410
....*....|...
gi 565652439 350 SINQAHQPDEYLE 362
Cdd:cd03888 419 QKDTMHQANEFIP 431
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
9-360 |
1.74e-18 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 86.06 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 9 IEIYRALIATPSISAT---DSALDQSNAtLINLLAGWfgslGF-QVEVQPVPGTRNKF----NMLASTGSGAGG--LLLA 78
Cdd:PRK13983 8 IELLSELIAIPAVNPDfggEGEKEKAEY-LESLLKEY----GFdEVERYDAPDPRVIEgvrpNIVAKIPGGDGKrtLWII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 79 GHTDTVPF-DDGRWTRDPFTLTEHDNKLFGLGTAD-MKGFFA--FILDALRDVDVTQlKKPLYILATADEET-SMAGARY 153
Cdd:PRK13983 83 SHMDVVPPgDLSLWETDPFKPVVKDGKIYGRGSEDnGQGIVSslLALKALMDLGIRP-KYNLGLAFVSDEETgSKYGIQY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 154 FAETTA--LRPDCAII----GEPTSLQPIRAHKGHISSAIRVQGQSGHSSDPERGVNAIELmhdAIGRIMQLRDSLKEry 227
Cdd:PRK13983 162 LLKKHPelFKKDDLILvpdaGNPDGSFIEIAEKSILWLKFTVKGKQCHASTPENGINAHRA---AADFALELDEALHE-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 228 HYDA----FTVPY----PTL------NLGHIHGGDasnricaccELHMDIRPLPGMTLDDLSGLLNEALEPVSLRWPGRL 293
Cdd:PRK13983 237 KFNAkdplFDPPYstfePTKkeanvdNINTIPGRD---------VFYFDCRVLPDYDLDEVLKDIKEIADEFEEEYGVKI 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565652439 294 TVFDLHPPIPGYECPPDHKLVQ----VVEKLLGAQTDVV----NYCTeAPFIQTICPTLVLGPGsINQAHQPDEY 360
Cdd:PRK13983 308 EVEIVQREQAPPPTPPDSEIVKklkrAIKEVRGIEPKVGgiggGTVA-AFLRKKGYPAVVWSTL-DETAHQPNEY 380
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
31-304 |
3.17e-18 |
|
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: 85.30 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 31 SNATLINLLAGWFGSLGFQVEVQPVP-------GTRNKFNMLASTGSGAGGLLLA--GHTDTVPFDDGrWTRDPFTLTEH 101
Cdd:cd02697 23 NNAPHAERTAALLQGFGFEAERHPVPeaevrayGMESITNLIVRRRYGDGGRTVAlnAHGDVVPPGDG-WTRDPYGAVVE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 102 DNKLFGLGTADMKGFFA---FILDALRDVDVTqLKKPLYILATADEET-SMAGARYFAETTALRPDCAIIGEpTSLQPIR 177
Cdd:cd02697 102 DGVMYGRAAAVSKSDFAsftFAVRALESLGAP-LRGAVELHFTYDEEFgGELGPGWLLRQGLTKPDLLIAAG-FSYEVVT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 178 AHKGHISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQLRDSLKE-RYHYDAFTVPYptLNLGHIHGGDASNRICAC 256
Cdd:cd02697 180 AHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYALNAQYRQvSSQVEGITHPY--LNVGRIEGGTNTNVVPGK 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 565652439 257 CELHMDIRPLPGMTLDDLSGLLNEALEPVSLRWPG------RLTVFDLHPPIPG 304
Cdd:cd02697 258 VTFKLDRRMIPEENPVEVEAEIRRVIADAAASMPGisvdirRLLLANSMRPLPG 311
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
56-216 |
1.29e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 77.97 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 56 PGTRNKFNMLASTGSGAGGLLLAGHTDTVPFDDGRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKP 135
Cdd:PRK07906 49 PGRANVVARLPGADPSRPALLVHGHLDVVPAEAADWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 136 --LYILATADEETSMA-GARYFAETtalRPD----C--AI---------IGEPTSLQPIR-AHKGHISSAIRVQGQSGHS 196
Cdd:PRK07906 129 rdLVFAFVADEEAGGTyGAHWLVDN---HPElfegVteAIsevggfsltVPGRDRLYLIEtAEKGLAWMRLTARGRAGHG 205
|
170 180
....*....|....*....|
gi 565652439 197 SDPERGvNAIELMHDAIGRI 216
Cdd:PRK07906 206 SMVNDD-NAVTRLAEAVARI 224
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
75-288 |
4.26e-14 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 73.07 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 75 LLLAGHTDTV-----PFDDGRWtRDpftltehDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPL-Y-ILATADEET- 146
Cdd:PRK07338 95 VLLTGHMDTVfpadhPFQTLSW-LD-------DGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLgYdVLINPDEEIg 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 147 SMAGARYFAEtTALRPDCAIIGEPT----SLQPIRAHKGHISsaIRVQGQSGHSS-DPERGVNAIELMHDAIGRIMQLRD 221
Cdd:PRK07338 167 SPASAPLLAE-LARGKHAALTYEPAlpdgTLAGARKGSGNFT--IVVTGRAAHAGrAFDEGRNAIVAAAELALALHALNG 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 565652439 222 SlkeryhYDAFTVpyptlNLGHIHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEPVSLR 288
Cdd:PRK07338 244 Q------RDGVTV-----NVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQR 299
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
8-216 |
2.19e-13 |
|
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: 71.22 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 8 FIEIYRALIATPSISATDSALDQSnatlINLLAGWFGSLGFQVEVQPVPGtrNKFnMLASTGSGAGG-LLLAGHTDTVPF 86
Cdd:cd05681 1 YLEDLRDLLKIPSVSAQGRGIPET----ADFLKEFLRRLGAEVEIFETDG--NPI-VYAEFNSGDAKtLLFYNHYDVQPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 87 D-DGRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPLYI--LATADEETSMAGARYFAETTA--LR 161
Cdd:cd05681 74 EpLELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIkfLVEGEEEVGSPNLEKFVAEHAdlLK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565652439 162 PDCAI-----IGEPTSLQPIRAHKGHISSAIRVQGQSG--HSSD-------PERGVNAIELMHDAIGRI 216
Cdd:cd05681 154 ADGCIwegggKNPKGRPQISLGVKGIVYVELRVKTADFdlHSSYgaivenpAWRLVQALNSLRDEDGRV 222
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
61-300 |
3.51e-13 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 69.81 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 61 KFNMLASTGS---GAGGLLLAGHTDTVPfddGRWtrDPFTLTEhdnKLFGLGTADMKGFFAFILDALRDVDVTQLKkpLY 137
Cdd:PRK00466 46 KLEILPDSNSfilGEGDILLASHVDTVP---GYI--EPKIEGE---VIYGRGAVDAKGPLISMIIAAWLLNEKGIK--VM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 138 ILATADEETSMAGARYFAeTTALRPDCAIIGEPT-SLQPIRAHKGHISSAIRVQGQSGHSSDPERgvNAIELMHDAIGRI 216
Cdd:PRK00466 116 VSGLADEESTSIGAKELV-SKGFNFKHIIVGEPSnGTDIVVEYRGSIQLDIMCEGTPEHSSSAKS--NLIVDISKKIIEV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 217 mqlrdsLKERYHYDAFTVpYPTLnlghIHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEPVSLRwpgrlTVF 296
Cdd:PRK00466 193 ------YKQPENYDKPSI-VPTI----IRAGESYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKFQECGLK-----IVD 256
|
....
gi 565652439 297 DLHP 300
Cdd:PRK00466 257 ETPP 260
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
63-172 |
5.03e-13 |
|
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: 67.07 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 63 NMLASTGSGAGG--LLLAGHTDTVPFDDGRWTRDPF-TLTEHDNKLFGLGTADMKGFFAFILDALRDV--DVTQLKKPLY 137
Cdd:cd18669 1 NVIARYGGGGGGkrVLLGAHIDVVPAGEGDPRDPPFfVDTVEEGRLYGRGALDDKGGVAAALEALKLLkeNGFKLKGTVV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 565652439 138 ILATADEETSMAGARYFAETTALRP----DCAIIGEPTS 172
Cdd:cd18669 81 VAFTPDEEVGSGAGKGLLSKDALEEdlkvDYLFVGDATP 119
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
75-235 |
9.76e-13 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 69.20 E-value: 9.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 75 LLLAGHTDTVPFDDGR---WTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVT--QLKKPLYILATADEETSMA 149
Cdd:PRK08262 114 IVLMAHQDVVPVAPGTegdWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQgfQPRRTIYLAFGHDEEVGGL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 150 GARYFAETTA---LRPDCAI-------------IGEPTSLQPIrAHKGHISSAIRVQGQSGHSSDPERGvNAIELMHDAI 213
Cdd:PRK08262 194 GARAIAELLKergVRLAFVLdeggaitegvlpgVKKPVALIGV-AEKGYATLELTARATGGHSSMPPRQ-TAIGRLARAL 271
|
170 180
....*....|....*....|....*...
gi 565652439 214 GRI------MQLRDSLKERYHYDAFTVP 235
Cdd:PRK08262 272 TRLednplpMRLRGPVAEMFDTLAPEMS 299
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
69-189 |
1.30e-12 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 68.65 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 69 GSGAGGLLLAGHTDTVPFDDGRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPLYILATADEETSM 148
Cdd:PRK08554 60 GEGKPKLLFMAHFDVVPVNPEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLNGKVIFAFTGDEEIGG 139
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 565652439 149 AGARYFAETTA---LRPDCAIIGEPTSLQPI-RAHKGhISSAIRV 189
Cdd:PRK08554 140 AMAMHIAEKLReegKLPKYMINADGIGMKPIiRRRKG-FGVTIRV 183
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
45-285 |
3.66e-12 |
|
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: 67.12 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 45 SLGFQVeVQPVPGtrNKFNMLASTGSGAG--GLLLAGHTDTVPFDDGRWTRDPFT-LTEHDNKLFGLGTADMKGFFAFIL 121
Cdd:TIGR01880 45 GLARKT-IEFVPG--KPVVVLTWPGSNPElpSILLNSHTDVVPVFREHWTHPPFSaFKDEDGNIYARGAQDMKCVGVQYL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 122 DALRDVDVT--QLKKPLYILATADEET-SMAGARYFAETT---ALRPDCAI---IGEPTSLQPI-RAHKGHISSAIRVQG 191
Cdd:TIGR01880 122 EAVRNLKASgfKFKRTIHISFVPDEEIgGHDGMEKFAKTDefkALNLGFALdegLASPDDVYRVfYAERVPWWVVVTAPG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 192 QSGHSSDPERGvNAIELMHDAIGRIMQLRDSLKERYH--YDAFTVPYPTLNLGHIHGGDASNRICACCELHMDIRPLPGM 269
Cdd:TIGR01880 202 NPGHGSKLMEN-TAMEKLEKSVESIRRFRESQFQLLQsnPDLAIGDVTSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSV 280
|
250
....*....|....*.
gi 565652439 270 TLDDLSGLLNEALEPV 285
Cdd:TIGR01880 281 DFEEMENRLDEWCADA 296
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
75-284 |
4.22e-11 |
|
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 63.83 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 75 LLLAGHTDTVPFDDGRWTRDPFT-LTEHDNKLFGLGTADMKGFFAFILDALRDVDVT--QLKKPLYILATADEET-SMAG 150
Cdd:cd05646 67 ILLNSHTDVVPVFEEKWTHDPFSaHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASgfKPKRTIHLSFVPDEEIgGHDG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 151 ARYFAETT---ALRPDCAI---IGEPTSLQPI----RAhKGHIssAIRVQGQSGHSSDPERGvNAIELMHDAIGRIMQLR 220
Cdd:cd05646 147 MEKFVKTEefkKLNVGFALdegLASPTEEYRVfygeRS-PWWV--VITAPGTPGHGSKLLEN-TAGEKLRKVIESIMEFR 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565652439 221 DSLKERYHYDAFTVP--YPTLNLGHIHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEP 284
Cdd:cd05646 223 ESQKQRLKSNPNLTLgdVTTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAE 288
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
8-127 |
5.03e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 63.78 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 8 FIEIYRALIATPSISATDSALDQSNATLINLLAGWFGSLGFQVEVQ--PVPGtRNKFnMLAS--TGSGAGGLLLAGHTDT 83
Cdd:PRK07079 19 FFADLARRVAYRTESQNPDRAPALRAYLTDEIAPALAALGFTCRIVdnPVAG-GGPF-LIAEriEDDALPTVLIYGHGDV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 565652439 84 VPFDDGRWT--RDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDV 127
Cdd:PRK07079 97 VRGYDEQWRegLSPWTLTEEGDRWYGRGTADNKGQHTINLAALEQV 142
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
8-115 |
9.32e-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: 9.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 8 FIEIYRALIATPSISATDSALDQSNaTLINLLAGWFGSLGFQVEVQPVPgtRNKFN----------MLASTGS--GAGGL 75
Cdd:cd05676 12 FIERLREAVAIQSVSADPEKRPELI-RMMEWAAERLEKLGFKVELVDIG--TQTLPdgeelplppvLLGRLGSdpSKKTV 88
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 565652439 76 LLAGHTDTVP--FDDGrWTRDPFTLTEHDNKLFGLGTADMKG 115
Cdd:cd05676 89 LIYGHLDVQPakLEDG-WDTDPFELTEKDGKLYGRGSTDDKG 129
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
75-216 |
1.07e-10 |
|
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: 63.04 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 75 LLLAGHTDTVPFDD---GRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVdVTQLKKP---LYILATADEETS- 147
Cdd:cd05674 72 LLLMAHQDVVPVNPeteDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELL-LKRGFKPrrtIILAFGHDEEVGg 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 148 MAGARYFAET------------------TALRPDcaIIGEPTSLqPIRAHKGHISSAIRVQGQSGHSSDPERGvNAIELM 209
Cdd:cd05674 151 ERGAGAIAELllerygvdglaaildeggAVLEGV--FLGVPFAL-PGVAEKGYMDVEITVHTPGGHSSVPPKH-TGIGIL 226
|
....*..
gi 565652439 210 HDAIGRI 216
Cdd:cd05674 227 SEAVAAL 233
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
63-171 |
2.52e-10 |
|
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: 59.36 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 63 NMLASTGSGAGG--LLLAGHTDTVPFDDGRWTRDPF-TLTEHDNKLFGLGTADMKGFFAFILDALRDV--DVTQLKKPLY 137
Cdd:cd03873 1 NLIARLGGGEGGksVALGAHLDVVPAGEGDNRDPPFaEDTEEEGRLYGRGALDDKGGVAAALEALKRLkeNGFKPKGTIV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 565652439 138 ILATADEETSMAGARYFAETTALR----PDCAIIGEPT 171
Cdd:cd03873 81 VAFTADEEVGSGGGKGLLSKFLLAedlkVDAAFVIDAT 118
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
16-224 |
3.31e-10 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 61.36 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 16 IATPSISATDSALDQSNATLINLLAGWFGSLGFQVEV--QPVPGtRNKFnMLAS--TGSGAGGLLLAGHTDTVPFDDGRW 91
Cdd:cd05679 14 VAVPTESQEPARKPELRAYLDQEMRPRFERLGFTVHIhdNPVAG-RAPF-LIAEriEDPSLPTLLIYGHGDVVPGYEGRW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 92 T--RDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPLY---ILATADEETSMAGARYFAET--TALRPDC 164
Cdd:cd05679 92 RdgRDPWTVTVWGERWYGRGTADNKGQHSINMAALRQVLEARGGKLGFnvkFLIEMGEEMGSPGLRAFCFShrEALKADL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565652439 165 AIIGEPTSLQPIR-----AHKGHISSAIRVQ-GQSGHSSDPERGV---------NAIELMHDAIGRImqLRDSLK 224
Cdd:cd05679 172 FIASDGPRLAADRptmflGSRGGLNFELRVNlREGGHHSGNWGGLlanpgiilaNAIASLVDGKGRI--KLPALK 244
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
43-359 |
5.72e-10 |
|
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349932 [Multi-domain] Cd Length: 368 Bit Score: 60.16 E-value: 5.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 43 FGSLGFQV---EVQPVPG--TRNKFNMLASTGSGAGGLLLAGHTDTVpfDDGRWTRDPftlTEHDNKLFGLGT----ADM 113
Cdd:cd05683 33 FENLGLSViedDAGKTTGggAGNLICTLKADKEEVPKILFTSHMDTV--TPGINVKPP---QIADGYIYSDGTtilgADD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 114 KGFFAFILDALRDVDVTQLK-KPLYILATADEETSMAGARY-----------FAETTALRPDCAIIGEPTSLQpirahkg 181
Cdd:cd05683 108 KAGIAAILEAIRVIKEKNIPhGQIQFVITVGEESGLVGAKAldpelidadygYALDSEGDVGTIIVGAPTQDK------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 182 hISSAIRvqGQSGHSS-DPERGVNAIELMHDAIGRIMQLRdslkeryhYDAFTvpypTLNLGHIHGGDASNRICACCELH 260
Cdd:cd05683 181 -INAKIY--GKTAHAGtSPEKGISAINIAAKAISNMKLGR--------IDEET----TANIGKFQGGTATNIVTDEVNIE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 261 MDIRPLPGMTLDDLSGLLNEALEPVSLRWPGRLTVfDLHPPIPGYECPPDHKLVQVVEKLLG-----AQTDVVNYCTEAP 335
Cdd:cd05683 246 AEARSLDEEKLDAQVKHMKETFETTAKEKGAHAEV-EVETSYPGFKINEDEEVVKLAKRAANnlgleINTTYSGGGSDAN 324
|
330 340
....*....|....*....|....*
gi 565652439 336 FIQTI-CPTLVLGPGSINqAHQPDE 359
Cdd:cd05683 325 IINGLgIPTVNLGIGYEN-IHTTNE 348
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
47-375 |
5.81e-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: 60.55 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 47 GFQVEVQPVPGTRNKFNMLAS-TGSGAGGLL--LAGHTDTVPFDDGRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDA 123
Cdd:cd08012 50 GGPLVIDHVSYVKGRGNIIVEyPGTVDGKTVsfVGSHMDVVTANPETWEFDPFSLSIDGDKLYGRGTTDCLGHVALVTEL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 124 LRDVDVTQ--LKKPLYILATADEETS-------------------MAGARYFAETtalrpdcaiigepTSLQPIRAHKGH 182
Cdd:cd08012 130 FRQLATEKpaLKRTVVAVFIANEENSeipgvgvdalvksglldnlKSGPLYWVDS-------------ADSQPCIGTGGM 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 183 ISSAIRVQGQSGHSSDPERGVNAIELMHDAIGRIMQ--LRD----SLKERYHYDAFTVPYPTLnLGHIHGGdaSNRICAC 256
Cdd:cd08012 197 VTWKLTATGKLFHSGLPHKAINALELVMEALAEIQKrfYIDfpphPKEEVYGFATPSTMKPTQ-WSYPGGS--INQIPGE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 257 CELHMDIRPLPGMTLDDLSGLL-------NEALEPVSLRWP------------GRLTVFDLHPPIPGYECPPDHKLVQVv 317
Cdd:cd08012 274 CTICGDCRLTPFYDVKEVREKLeeyvddiNANIEELPTRGPvskyvlpaeglrGRVSLEFDEAAASGVACNLDSPGFHA- 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565652439 318 ekLLGAQTDVVNYCTeaPFiqTICPTLVL--------------GPGSINQAHQPDEY-LETRF---IKPTRELISQ 375
Cdd:cd08012 353 --LCKATSEVVGYVK--PY--AITGSLPLirelqdegfdvqitGYGLMATYHAKNEYcLLSDFqngFKVLARTIAQ 422
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
8-146 |
4.76e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 57.78 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 8 FIEIYRALIATPSI-----------SATDSALDQSNATLinllagwfGSLGFQVEVQPvpgtrNKFNMLASTGSGAGGLL 76
Cdd:PRK07205 13 CVAAIKTLVSYPSVlnegengtpfgQAIQDVLEATLDLC--------QGLGFKTYLDP-----KGYYGYAEIGQGEELLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565652439 77 LAGHTDTVPF-DDGRWTRDPFTLTEHDNKLFGLGTADMKG-----FFAfiLDALRDVDVTQLKKPLYILATaDEET 146
Cdd:PRK07205 80 ILCHLDVVPEgDLSDWQTPPFEAVEKDGCLFGRGTQDDKGpsmaaLYA--VKALLDAGVQFNKRIRFIFGT-DEET 152
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
15-125 |
1.11e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 56.45 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 15 LIATPSISAtDSALDQSNATLINLLAGWFGSLGFQ-VEVQPVPGTRNKFNMLASTgSGAGGLLLAGHTDTVP-FDDGRWT 92
Cdd:PRK07907 27 LVRIPSVAA-DPFRREEVARSAEWVADLLREAGFDdVRVVSADGAPAVIGTRPAP-PGAPTVLLYAHHDVQPpGDPDAWD 104
|
90 100 110
....*....|....*....|....*....|...
gi 565652439 93 RDPFTLTEHDNKLFGLGTADMKGFFAFILDALR 125
Cdd:PRK07907 105 SPPFELTERDGRLYGRGAADDKGGIAMHLAALR 137
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
71-258 |
1.91e-07 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 52.48 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 71 GAGGLLLAGHTDTV----PFDDGRWTRDpftltehDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPLYI--LATADE 144
Cdd:PRK07473 74 GEPGILIAGHMDTVhpvgTLEKLPWRRE-------GNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPItvLFTPDE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 145 ETSMAGARYFAETTALRPDCAIIGEPTslqpiRAHKGHISS--AI-----RVQGQSGHS-SDPERGVNAIELMHDAIGRI 216
Cdd:PRK07473 147 EVGTPSTRDLIEAEAARNKYVLVPEPG-----RPDNGVVTGryAIarfnlEATGRPSHAgATLSEGRSAIREMARQILAI 221
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 565652439 217 mqlrdslkeryhyDAFTVPYPTLNLGHIHGGDASNRICACCE 258
Cdd:PRK07473 222 -------------DAMTTEDCTFSVGIVHGGQWVNCVATTCT 250
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
3-241 |
4.76e-07 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 51.78 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 3 MKLPPFIEIYRA----LIATPSISATDSALDqsnatLINLLAGWFGSL-GFQ-----VEVQPVPGT----RNKFNMLAST 68
Cdd:COG4187 1 MKKWQTKEQLEEllceLVSIPSVTGTEGEKE-----VAEFIYEKLSELpYFQenpehLGLHPLPDDplgrKNVTALVKGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 69 GSGAGGLLLAGHTDTVPFDD-GRWTR---DPFTLTEH----------------DNKLFGLGTADMKG----FFAFILDAL 124
Cdd:COG4187 76 GESKKTVILISHFDVVDVEDyGSLKPlafDPEELTEAlkeiklpedvrkdlesGEWLFGRGTMDMKAglalHLALLEEAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 125 RDVDvtqLKKPLYILATADEETSMAGARY-------FAETTALRPDCAIIGEPTSLQPIRAHKGHISS--------AIRV 189
Cdd:COG4187 156 ENEE---FPGNLLLLAVPDEEVNSAGMRAavpllaeLKEKYGLEYKLAINSEPSFPKYPGDETRYIYTgsigklmpGFYC 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 565652439 190 QGQSGHSSDPERGVNAIeLMHDAIGRIMQLRDSLKERYhYDAFTVPYPTLNL 241
Cdd:COG4187 233 YGKETHVGEPFSGLNAN-LLASELTRELELNPDFCEEV-GGEVTPPPVSLKQ 282
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
14-362 |
4.95e-06 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 48.07 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 14 ALIATPSISAtDSALDQSNATLINLLAGWFGSLGFQ-VEVQPVPGtrnkFNMLASTGSGAGG---LLLAGHTDTVPFD-- 87
Cdd:cd05680 6 ELLRIPSVSA-DPAHKGDVRRAAEWLADKLTEAGFEhTEVLPTGG----HPLVYAEWLGAPGaptVLVYGHYDVQPPDpl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 88 DGrWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPLYI--LATADEETSMAGARYFAETTALRPDCA 165
Cdd:cd05680 81 EL-WTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVkfLIEGEEEIGSPSLPAFLEENAERLAAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 166 II----------GEPTSLQPIRahkGHISSAIRVQGQSG--HSSDPERGV-NAIEL-------MHDAIGRIM------QL 219
Cdd:cd05680 160 VVlvsdtsmwspDTPTITYGLR---GLAYLEISVTGPNRdlHSGSYGGAVpNPANAlarllasLHDEDGRVAipgfydDV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 220 RD-SLKERYHYDAFtvPY-----------------------------PTLNLGHIHGG--DASNRICACCELHMDI--RP 265
Cdd:cd05680 237 RPlTDAEREAWAAL--PFdeaafkaslgvpalggeagyttlerlwarPTLDVNGIWGGyqGEGSKTVIPSKAHAKIsmRL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 266 LPGMTLDDLSGLLNEALE---PVSLRWpgrlTVFDLHPPIPgYECPPDHKLVQVVEKLLGAQTDVVNYCTEA----PFIQ 338
Cdd:cd05680 315 VPGQDPDAIADLLEAHLRahaPPGVTL----SVKPLHGGRP-YLVPTDHPALQAAERALEEAFGKPPVFVREggsiPIVA 389
|
410 420 430
....*....|....*....|....*....|
gi 565652439 339 TI-----CPTLVLGPG-SINQAHQPDEYLE 362
Cdd:cd05680 390 LFekvlgIPTVLMGFGlPDDAIHAPNEKFR 419
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
56-238 |
1.17e-05 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 47.34 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 56 PGTRNKFNMLASTGSGAGGLLLAGHTDTVPFDD-GRWTR---DPFTLTE------------------HDNKLFGLGTADM 113
Cdd:cd05654 55 LGRRNVTALVKGKKPSKRTIILISHFDTVGIEDyGELKDiafDPDELTKafseyveeldeevredllSGEWLFGRGTMDM 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 114 KGFFAFILDALRD-VDVTQLKKPLYILATADEETSMAGARyfAETTALRPDC---------AIIGEPTS-LQPIRAHK-- 180
Cdd:cd05654 135 KSGLAVHLALLEQaSEDEDFDGNLLLMAVPDEEVNSRGMR--AAVPALLELKkkhdleyklAINSEPIFpQYDGDQTRyi 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565652439 181 -----GHISSAIRVQGQSGHSSDPERGVNAiELMHDAIGRIMQLRDSLKERYHYDAftVPYPT 238
Cdd:cd05654 213 ytgsiGKILPGFLCYGKETHVGEPFAGINA-NLMASEITARLELNADLCEKVEGEI--TPPPV 272
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
80-166 |
2.71e-05 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 46.12 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 80 HTDTVPFDDGRW-----TRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKP----LYILATadEETSMAG 150
Cdd:PRK06156 117 HADVVPANPELWvldgtRLDPFKVTLVGDRLYGRGTEDDKGAIVTALYAMKAIKDSGLPLArrieLLVYTT--EETDGDP 194
|
90
....*....|....*.
gi 565652439 151 ARYFAETTALrPDCAI 166
Cdd:PRK06156 195 LKYYLERYTP-PDYNI 209
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
187-264 |
2.19e-04 |
|
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: 42.97 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 187 IRVQGQSGHSSDPERGVNAIELMHDAIGRIMQL---RDSLKERYHydaftvpyptLNLGHIHGGDASNRICACCELHMDI 263
Cdd:cd03886 176 ITVKGKGGHGASPHLGVDPIVAAAQIVLALQTVvsrELDPLEPAV----------VTVGKFHAGTAFNVIPDTAVLEGTI 245
|
.
gi 565652439 264 R 264
Cdd:cd03886 246 R 246
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
144-295 |
5.70e-04 |
|
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: 41.49 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 144 EETSMAGARYFAETTALRPDCAIIG---EPT-SLQPIRAHKGHISSA-----IRVQGQSGHSSDPERGVNAIEL------ 208
Cdd:cd08014 123 EETMPGGALDMIRAGALDGVSAIFAlhvDPRlPVGRVGVRYGPITAAadsleIRIQGEGGHGARPHLTVDLVWAaaqvvt 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 209 -MHDAIGRIMQLRDSLkeryhydaftvpypTLNLGHIHGGDASNRICACCELHMDIRPLPGMTLDDLSGLLNEALEPVSL 287
Cdd:cd08014 203 dLPQAISRRIDPRSPV--------------VLTWGSIEGGRAPNVIPDSVELSGTVRTLDPDTWAQLPDLVEEIVAGICA 268
|
....*...
gi 565652439 288 RWPGRLTV 295
Cdd:cd08014 269 PYGAKYEL 276
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
5-146 |
1.19e-03 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 40.78 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 5 LPPFIEIyralIATPSIS-------ATDSALDQSnatlINLLAGWFGS---LGFQVEVQPVPGtRNKFNM--LASTGSGA 72
Cdd:cd05682 3 LPALSDY----IRIPNQSplfdpewATNGLLEKA----ANLIADWVKAqniKGAKVEVVELEG-RTPLLFveIPGTEQDD 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565652439 73 GGLLLAGHTDTVPFDDGrWTRD--PFTLTEHDNKLFGLGTADmKGFFAF-ILDALRDVDVTQLKKPLYI-LATADEET 146
Cdd:cd05682 74 DTVLLYGHMDKQPPFTG-WDEGlgPTKPVIRGDKLYGRGGAD-DGYAIFaSLTAIKALQEQGIPHPRCVvLIEACEES 149
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
71-217 |
1.23e-03 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 40.88 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 71 GAGGLLLAGHTDTVPFDD-GRWTRDPFTLTEHDNKLFGLGTADMKGFFAFILDALRDVDVTQLKKPLYI--LATADEETS 147
Cdd:PRK08201 78 GKPTVLIYGHYDVQPVDPlNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVkfCIEGEEEIG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 148 MAGARYFAETTA--LRPDCAIIGEPTSLQP-----IRAHKGHISSAIRVQGQSG--HSSDPERGV-NAI----EL---MH 210
Cdd:PRK08201 158 SPNLDSFVEEEKdkLAADVVLISDTTLLGPgkpaiCYGLRGLAALEIDVRGAKGdlHSGLYGGAVpNALhalvQLlasLH 237
|
....*..
gi 565652439 211 DAIGRIM 217
Cdd:PRK08201 238 DEHGTVA 244
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
75-115 |
1.67e-03 |
|
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: 40.40 E-value: 1.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 565652439 75 LLLAGHTDTVPFDD-GRWTRDPFTLTEHDNKLFGLGTADMKG 115
Cdd:cd05677 74 ILFYGHYDVIPAGEtDGWDTDPFTLTCENGYLYGRGVSDNKG 115
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
19-115 |
4.09e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 38.97 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 19 PSISATDSALDQSNATLINLLAgwfgSLGFQVEVQPVPGtrNKFnMLASTGSGAG-GLLLAGHTDTVPFDD-GRWTRDPF 96
Cdd:PRK06446 15 PSISATGEGIEETANYLKDTME----KLGIKANIERTKG--HPV-VYGEINVGAKkTLLIYNHYDVQPVDPlSEWKRDPF 87
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90
....*....|....*....
gi 565652439 97 TLTEHDNKLFGLGTADMKG 115
Cdd:PRK06446 88 SATIENGRIYARGASDNKG 106
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| Peptidase_M28 |
pfam04389 |
Peptidase family M28; |
69-156 |
5.12e-03 |
|
Peptidase family M28;
Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 37.65 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565652439 69 GSGAGGLLLAGHTDTVPFDDGrwtrdpftltEHDNklfGLGTAdmkgffaFILDALRDV-DVTQLKKPLYILATADEETS 147
Cdd:pfam04389 9 KAPDEVVLLSAHYDSVGTGPG----------ADDN---ASGVA-------ALLELARVLaAGQRPKRSVRFLFFDAEEAG 68
|
....*....
gi 565652439 148 MAGARYFAE 156
Cdd:pfam04389 69 LLGSHHFAK 77
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|
| M20_Acy1_YxeP-like |
cd05669 |
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
144-206 |
8.94e-03 |
|
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349919 [Multi-domain] Cd Length: 371 Bit Score: 38.04 E-value: 8.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565652439 144 EETSmAGARYFAETTALRPDCAIIG---EPT-SLQPIRAHKGHISSA-----IRVQGQSGHSSDPERGVNAI 206
Cdd:cd05669 126 EETG-AGAKKVIEAGALDDVSAIFGfhnKPDlPVGTIGLKSGALMAAvdrfeIEIAGKGAHAAKPENGVDPI 196
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