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Conserved domains on  [gi|493292681|ref|WP_006250364|]
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acetylornithine deacetylase [Mannheimia haemolytica]

Protein Classification

acetylornithine deacetylase( domain architecture ID 11480378)

acetylornithine deacetylase catalyzes the conversion of 2-N-acetyl-L-ornithine to L-ornithine and acetate in the fifth step of the arginine biosynthesis pathway and is a member of the M20 peptidase family

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05111 PRK05111
acetylornithine deacetylase; Provisional
1-379 0e+00

acetylornithine deacetylase; Provisional


:

Pssm-ID: 235346 [Multi-domain]  Cd Length: 383  Bit Score: 754.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   1 MKQIP-FIQRYAQLIELPTISSLVAEEDLSNRRLIELLATWLADFGFKTEILAVEGSRNKYNLLATYGEGEGGLLLAGHT 79
Cdd:PRK05111   1 KMKLPsFIEMYRALIATPSISATDPALDQSNRAVIDLLAGWFEDLGFNVEIQPVPGTRGKFNLLASLGSGEGGLLLAGHT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  80 DTVPFDEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEETTMLGARTFAQHSHIR 159
Cdd:PRK05111  81 DTVPFDEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKPLYILATADEETSMAGARAFAEATAIR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 160 PDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLFQVTHPTMNF 239
Cdd:PRK05111 161 PDCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDELQERYHNPAFTVPYPTLNL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 240 GNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGIPGYECEHSAQIVQVVEKLL 319
Cdd:PRK05111 241 GHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVSERWPGRITVAPLHPPIPGYECPADHQLVRVVEKLL 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493292681 320 GEKCDAVNYCTEAPFIQQL-CPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLIYHFC 379
Cdd:PRK05111 321 GHKAEVVNYCTEAPFIQQLgCPTLVLGPGSIEQAHQPDEYLELSFIKPTRELLRQLIHHFC 381
 
Name Accession Description Interval E-value
PRK05111 PRK05111
acetylornithine deacetylase; Provisional
1-379 0e+00

acetylornithine deacetylase; Provisional


Pssm-ID: 235346 [Multi-domain]  Cd Length: 383  Bit Score: 754.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   1 MKQIP-FIQRYAQLIELPTISSLVAEEDLSNRRLIELLATWLADFGFKTEILAVEGSRNKYNLLATYGEGEGGLLLAGHT 79
Cdd:PRK05111   1 KMKLPsFIEMYRALIATPSISATDPALDQSNRAVIDLLAGWFEDLGFNVEIQPVPGTRGKFNLLASLGSGEGGLLLAGHT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  80 DTVPFDEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEETTMLGARTFAQHSHIR 159
Cdd:PRK05111  81 DTVPFDEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKPLYILATADEETSMAGARAFAEATAIR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 160 PDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLFQVTHPTMNF 239
Cdd:PRK05111 161 PDCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDELQERYHNPAFTVPYPTLNL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 240 GNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGIPGYECEHSAQIVQVVEKLL 319
Cdd:PRK05111 241 GHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVSERWPGRITVAPLHPPIPGYECPADHQLVRVVEKLL 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493292681 320 GEKCDAVNYCTEAPFIQQL-CPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLIYHFC 379
Cdd:PRK05111 321 GHKAEVVNYCTEAPFIQQLgCPTLVLGPGSIEQAHQPDEYLELSFIKPTRELLRQLIHHFC 381
M20_ArgE cd03894
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ...
10-375 4.18e-164

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: 463.99  E-value: 4.18e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  10 YAQLIELPTISSLvaeedlSNRRLIELLATWLADFGFKTEILAVEGsRNKYNLLATYG-EGEGGLLLAGHTDTVPFDEGK 88
Cdd:cd03894    3 LARLVAFDTVSRN------SNLALIEYVADYLAALGVKSRRVPVPE-GGKANLLATLGpGGEGGLLLSGHTDVVPVDGQK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  89 WRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEETTMLGARTFAQHSH---IRPDCAII 165
Cdd:cd03894   76 WSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLIAALAargGRPDAAIV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 166 GEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLFQVTHPTMNFGNIHGG 245
Cdd:cd03894  156 GEPTSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGLRDPPFDPPYPTLNVGLIHGG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 246 DAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGiPGYECEHSAQIVQVVEKLLGE-KCD 324
Cdd:cd03894  236 NAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPEAGIEVEPLFEV-PGLETDEDAPLVRLAAALAGDnKVR 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493292681 325 AVNYCTEAPFIQQL-CPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:cd03894  315 TVAYGTEAGLFQRAgIPTVVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLI 366
AcOrn-deacetyl TIGR01892
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ...
10-375 3.64e-153

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: 436.17  E-value: 3.64e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   10 YAQLIELPTISSLvaeedlSNRRLIELLATWLADFGFKTEILAVEGSRNKYNLLATYG-EGEGGLLLAGHTDTVPFDEGK 88
Cdd:TIGR01892   3 LTKLVAFDSTSFR------PNVDLIDWAQAYLEALGFSVEVQPFPDGAEKSNLVAVIGpSGAGGLALSGHTDVVPYDDAA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   89 WRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEETTMLGARTFAQHSHIRPDCAIIGEP 168
Cdd:TIGR01892  77 WTRDPFRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKMIEAGAGRPRHAIIGEP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  169 TSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLFQVTHPTMNFGNIHGGDAI 248
Cdd:TIGR01892 157 TRLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLREDLDEGFTPPYTTLNIGVIQGGKAV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  249 NRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQY-GDLIEIRhLHDGIPGYECEHSAQIVQVVEKLLGEKCDAVN 327
Cdd:TIGR01892 237 NIIPGACEFVFEWRPIPGMDPEELLQLLETIAQALVRDEpGFEVQIE-VVSTDPGVNTEPDAELVAFLEELSGNAPEVVS 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 493292681  328 YCTEAPFIQQL-CPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:TIGR01892 316 YGTEAPQFQELgAEAVVCGPGDIRQAHQPDEYVEIEDLVRCRAVLARLV 364
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
6-380 8.90e-108

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: 321.45  E-value: 8.90e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   6 FIQRYAQLIELPTISslvaeedLSNRRLIELLATWLADFGFKTEILAVEGSRnkYNLLATY--GEGEGGLLLAGHTDTVP 83
Cdd:COG0624   14 ALELLRELVRIPSVS-------GEEAAAAELLAELLEALGFEVERLEVPPGR--PNLVARRpgDGGGPTLLLYGHLDVVP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  84 FDEG-KWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLT--QIKKPIRILATADEETTMLGARTFAQH--SHI 158
Cdd:COG0624   85 PGDLeLWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAglRLPGNVTLLFTGDEEVGSPGARALVEElaEGL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 159 RPDCAIIGEPTS-LKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREkyhNPLFQvtHPTM 237
Cdd:COG0624  165 KADAAIVGEPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDGRA---DPLFG--RTTL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 238 NFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPmlEQYGDLIEIRHLHDGIPGYECEHSAQIVQVVEK 317
Cdd:COG0624  240 NVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAA--AAPGVEVEVEVLGDGRPPFETPPDSPLVAAARA 317
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493292681 318 LLGE------KCDAVNYCTEAPFIQQL--CPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLIYHFCG 380
Cdd:COG0624  318 AIREvtgkepVLSGVGGGTDARFFAEAlgIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
74-377 4.35e-62

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: 201.81  E-value: 4.35e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   74 LLAGHTDTVPfDEGKWRFnPFQLTEKaGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKK-PIRILATADEETTMLGARTF 152
Cdd:pfam01546   1 LLRGHMDVVP-DEETWGW-PFKSTED-GKLYGRGHDDMKGGLLAALEALRALKEEGLKKgTVKLLFQPDEEGGMGGARAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  153 AQ---HSHIRPDCAI---IGEPTSL------KPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDE 220
Cdd:pfam01546  78 IEdglLEREKVDAVFglhIGEPTLLeggiaiGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  221 LREKYHNPLFQVThptmNFGNIHGGdaINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGI 300
Cdd:pfam01546 158 NVDPLDPAVVTVG----NITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEYVEGGA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  301 PgYECEHS---AQIVQVVEKLLGEKCD----AVNYCTEAPFIQQ-LCPTLV-LGPGSiEQAHQPDEFLEMKYIEPTKELL 371
Cdd:pfam01546 232 P-PLVNDSplvAALREAAKELFGLKVElivsGSMGGTDAAFFLLgVPPTVVfFGPGS-GLAHSPNEYVDLDDLEKGAKVL 309

                  ....*.
gi 493292681  372 TKLIYH 377
Cdd:pfam01546 310 ARLLLK 315
 
Name Accession Description Interval E-value
PRK05111 PRK05111
acetylornithine deacetylase; Provisional
1-379 0e+00

acetylornithine deacetylase; Provisional


Pssm-ID: 235346 [Multi-domain]  Cd Length: 383  Bit Score: 754.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   1 MKQIP-FIQRYAQLIELPTISSLVAEEDLSNRRLIELLATWLADFGFKTEILAVEGSRNKYNLLATYGEGEGGLLLAGHT 79
Cdd:PRK05111   1 KMKLPsFIEMYRALIATPSISATDPALDQSNRAVIDLLAGWFEDLGFNVEIQPVPGTRGKFNLLASLGSGEGGLLLAGHT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  80 DTVPFDEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEETTMLGARTFAQHSHIR 159
Cdd:PRK05111  81 DTVPFDEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKPLYILATADEETSMAGARAFAEATAIR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 160 PDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLFQVTHPTMNF 239
Cdd:PRK05111 161 PDCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDELQERYHNPAFTVPYPTLNL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 240 GNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGIPGYECEHSAQIVQVVEKLL 319
Cdd:PRK05111 241 GHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVSERWPGRITVAPLHPPIPGYECPADHQLVRVVEKLL 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493292681 320 GEKCDAVNYCTEAPFIQQL-CPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLIYHFC 379
Cdd:PRK05111 321 GHKAEVVNYCTEAPFIQQLgCPTLVLGPGSIEQAHQPDEYLELSFIKPTRELLRQLIHHFC 381
M20_ArgE cd03894
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ...
10-375 4.18e-164

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: 463.99  E-value: 4.18e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  10 YAQLIELPTISSLvaeedlSNRRLIELLATWLADFGFKTEILAVEGsRNKYNLLATYG-EGEGGLLLAGHTDTVPFDEGK 88
Cdd:cd03894    3 LARLVAFDTVSRN------SNLALIEYVADYLAALGVKSRRVPVPE-GGKANLLATLGpGGEGGLLLSGHTDVVPVDGQK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  89 WRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEETTMLGARTFAQHSH---IRPDCAII 165
Cdd:cd03894   76 WSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLIAALAargGRPDAAIV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 166 GEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLFQVTHPTMNFGNIHGG 245
Cdd:cd03894  156 GEPTSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGLRDPPFDPPYPTLNVGLIHGG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 246 DAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGiPGYECEHSAQIVQVVEKLLGE-KCD 324
Cdd:cd03894  236 NAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPEAGIEVEPLFEV-PGLETDEDAPLVRLAAALAGDnKVR 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493292681 325 AVNYCTEAPFIQQL-CPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:cd03894  315 TVAYGTEAGLFQRAgIPTVVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLI 366
AcOrn-deacetyl TIGR01892
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ...
10-375 3.64e-153

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: 436.17  E-value: 3.64e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   10 YAQLIELPTISSLvaeedlSNRRLIELLATWLADFGFKTEILAVEGSRNKYNLLATYG-EGEGGLLLAGHTDTVPFDEGK 88
Cdd:TIGR01892   3 LTKLVAFDSTSFR------PNVDLIDWAQAYLEALGFSVEVQPFPDGAEKSNLVAVIGpSGAGGLALSGHTDVVPYDDAA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   89 WRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEETTMLGARTFAQHSHIRPDCAIIGEP 168
Cdd:TIGR01892  77 WTRDPFRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKMIEAGAGRPRHAIIGEP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  169 TSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLFQVTHPTMNFGNIHGGDAI 248
Cdd:TIGR01892 157 TRLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLREDLDEGFTPPYTTLNIGVIQGGKAV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  249 NRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQY-GDLIEIRhLHDGIPGYECEHSAQIVQVVEKLLGEKCDAVN 327
Cdd:TIGR01892 237 NIIPGACEFVFEWRPIPGMDPEELLQLLETIAQALVRDEpGFEVQIE-VVSTDPGVNTEPDAELVAFLEELSGNAPEVVS 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 493292681  328 YCTEAPFIQQL-CPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:TIGR01892 316 YGTEAPQFQELgAEAVVCGPGDIRQAHQPDEYVEIEDLVRCRAVLARLV 364
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
6-380 8.90e-108

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: 321.45  E-value: 8.90e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   6 FIQRYAQLIELPTISslvaeedLSNRRLIELLATWLADFGFKTEILAVEGSRnkYNLLATY--GEGEGGLLLAGHTDTVP 83
Cdd:COG0624   14 ALELLRELVRIPSVS-------GEEAAAAELLAELLEALGFEVERLEVPPGR--PNLVARRpgDGGGPTLLLYGHLDVVP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  84 FDEG-KWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLT--QIKKPIRILATADEETTMLGARTFAQH--SHI 158
Cdd:COG0624   85 PGDLeLWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAglRLPGNVTLLFTGDEEVGSPGARALVEElaEGL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 159 RPDCAIIGEPTS-LKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREkyhNPLFQvtHPTM 237
Cdd:COG0624  165 KADAAIVGEPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDGRA---DPLFG--RTTL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 238 NFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPmlEQYGDLIEIRHLHDGIPGYECEHSAQIVQVVEK 317
Cdd:COG0624  240 NVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAA--AAPGVEVEVEVLGDGRPPFETPPDSPLVAAARA 317
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493292681 318 LLGE------KCDAVNYCTEAPFIQQL--CPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLIYHFCG 380
Cdd:COG0624  318 AIREvtgkepVLSGVGGGTDARFFAEAlgIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
PRK07522 PRK07522
acetylornithine deacetylase; Provisional
11-361 4.18e-95

acetylornithine deacetylase; Provisional


Pssm-ID: 236039 [Multi-domain]  Cd Length: 385  Bit Score: 289.01  E-value: 4.18e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  11 AQLIELPTISslvaeeDLSNRRLIELLATWLADFGFKTEILAVEgSRNKYNLLATYG-EGEGGLLLAGHTDTVPFDEGKW 89
Cdd:PRK07522  11 ERLVAFDTVS------RDSNLALIEWVRDYLAAHGVESELIPDP-EGDKANLFATIGpADRGGIVLSGHTDVVPVDGQAW 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  90 RFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEETTMLGARTFAQHSH---IRPDCAIIG 166
Cdd:PRK07522  84 TSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGCLGVPSMIARLPergVKPAGCIVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 167 EPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYH-NPLFQVTHPTMNFGNIHGG 245
Cdd:PRK07522 164 EPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLADRLAAPGPfDALFDPPYSTLQTGTIQGG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 246 DAINRICACCELQFDMRPLPNMAVQDLYA----MVNEHLKPMLEQYGDLIEIR-HLHDGIPGYECEHSAQIVQVVEKLLG 320
Cdd:PRK07522 244 TALNIVPAECEFDFEFRNLPGDDPEAILAriraYAEAELLPEMRAVHPEAAIEfEPLSAYPGLDTAEDAAAARLVRALTG 323
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 493292681 321 -EKCDAVNYCTEAPFIQQL-CPTLVLGPGSIEQAHQPDEFLEM 361
Cdd:PRK07522 324 dNDLRKVAYGTEAGLFQRAgIPTVVCGPGSIEQAHKPDEFVEL 366
M20_ArgE_DapE-like cd08659
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ...
12-375 1.18e-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: 1.18e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  12 QLIELPTISSlvAEEDLSnrrliELLATWLADFGFKTEilaVEGSRNKYNLLATYGEGEG-GLLLAGHTDTVPF-DEGKW 89
Cdd:cd08659    5 DLVQIPSVNP--PEAEVA-----EYLAELLAKRGYGIE---STIVEGRGNLVATVGGGDGpVLLLNGHIDTVPPgDGDKW 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  90 RFNPFQLTEKAGKLYGLGTADMK-GFFAFVVEVVSQLDLTQIKK-PIRILATADEETTMLGARTFAQHSHI-RPDCAIIG 166
Cdd:cd08659   75 SFPPFSGRIRDGRLYGRGACDMKgGLAAMVAALIELKEAGALLGgRVALLATVDEEVGSDGARALLEAGYAdRLDALIVG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 167 EPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMhqsIGYLMKMRDELREKYHNPLFqvTHPTMNFGNIHGGD 246
Cdd:cd08659  155 EPTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYAL---ADFLAELRTLFEELPAHPLL--GPPTLNVGVINGGT 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 247 AINRICACCELQFDMRPLPNMAVQDLYAMVNEHlkpmLEQYGDLIEIRHLHDGIPGYECEHSAQIVQVVEKLLGEKCDA- 325
Cdd:cd08659  230 QVNSIPDEATLRVDIRLVPGETNEGVIARLEAI----LEEHEAKLTVEVSLDGDPPFFTDPDHPLVQALQAAARALGGDp 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493292681 326 ----VNYCTEAPFIQQL--CPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:cd08659  306 vvrpFTGTTDASYFAKDlgFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
74-377 4.35e-62

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: 201.81  E-value: 4.35e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   74 LLAGHTDTVPfDEGKWRFnPFQLTEKaGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKK-PIRILATADEETTMLGARTF 152
Cdd:pfam01546   1 LLRGHMDVVP-DEETWGW-PFKSTED-GKLYGRGHDDMKGGLLAALEALRALKEEGLKKgTVKLLFQPDEEGGMGGARAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  153 AQ---HSHIRPDCAI---IGEPTSL------KPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDE 220
Cdd:pfam01546  78 IEdglLEREKVDAVFglhIGEPTLLeggiaiGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  221 LREKYHNPLFQVThptmNFGNIHGGdaINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGI 300
Cdd:pfam01546 158 NVDPLDPAVVTVG----NITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEYVEGGA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  301 PgYECEHS---AQIVQVVEKLLGEKCD----AVNYCTEAPFIQQ-LCPTLV-LGPGSiEQAHQPDEFLEMKYIEPTKELL 371
Cdd:pfam01546 232 P-PLVNDSplvAALREAAKELFGLKVElivsGSMGGTDAAFFLLgVPPTVVfFGPGS-GLAHSPNEYVDLDDLEKGAKVL 309

                  ....*.
gi 493292681  372 TKLIYH 377
Cdd:pfam01546 310 ARLLLK 315
PRK08651 PRK08651
succinyl-diaminopimelate desuccinylase; Reviewed
12-375 5.37e-60

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 236323 [Multi-domain]  Cd Length: 394  Bit Score: 198.68  E-value: 5.37e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  12 QLIELPTisslVAEEDLSNRRLIELLATWLADFGFKTEILAVEGS------RNKYNLLATYGEGEGGLLLAGHTDTVPFD 85
Cdd:PRK08651  14 DLIKIPT----VNPPGENYEEIAEFLRDTLEELGFSTEIIEVPNEyvkkhdGPRPNLIARRGSGNPHLHFNGHYDVVPPG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  86 EGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDlTQIKKPIRILATADEETTMLGARTFAQHSHIRPDCAII 165
Cdd:PRK08651  90 EGWSVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLD-PAGDGNIELAIVPDEETGGTGTGYLVEEGKVTPDYVIV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 166 GEPTSLKPI-RAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLFQVTHPTMNFGN--I 242
Cdd:PRK08651 169 GEPSGLDNIcIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYEYDDERGAKPTVTLGGptV 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 243 HGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLhDGIPGYECEHSAQIVQVVEKLLGEK 322
Cdd:PRK08651 249 EGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVEFEIT-PFSEAFVTDPDSELVKALREAIREV 327
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 323 --CDAVNYC----TEA-PFIQQLCPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:PRK08651 328 lgVEPKKTIslggTDArFFGAKGIPTVVYGPGELELAHAPDEYVEVKDVEKAAKVYEEVL 387
PRK08588 PRK08588
succinyl-diaminopimelate desuccinylase; Reviewed
7-373 4.54e-54

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 181490 [Multi-domain]  Cd Length: 377  Bit Score: 182.78  E-value: 4.54e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   7 IQRYAQLIELPTISSlvAEEDLSNrrlieLLATWLADFGFKTEILAVEGSRNkyNLLATYGEGEGGLLLAGHTDTV-PFD 85
Cdd:PRK08588   5 IQILADIVKINSVND--NEIEVAN-----YLQDLFAKHGIESKIVKVNDGRA--NLVAEIGSGSPVLALSGHMDVVaAGD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  86 EGKWRFNPFQLTEKAGKLYGLGTADMK-GFFAFVV---EVVSQLDLTQIKkpIRILATADEETTMLGARTFAQH---SHI 158
Cdd:PRK08588  76 VDKWTYDPFELTEKDGKLYGRGATDMKsGLAALVIamiELKEQGQLLNGT--IRLLATAGEEVGELGAKQLTEKgyaDDL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 159 rpDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIElmhqsigYLMKMRDELREKY-----HNPLFQVT 233
Cdd:PRK08588 154 --DALIIGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAID-------PLLEFYNEQKEYFdsikkHNPYLGGL 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 234 hpTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGIPGYECEHS--AQI 311
Cdd:PRK08588 225 --THVVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNQNGAAQLSLDIYSNHRPVASDKDSklVQL 302
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493292681 312 VQ-VVEKLLGEKCD--AVNYCTEA----------PFIqqlcptlVLGPGSIEQAHQPDEFLE----MKYIEPTKELLTK 373
Cdd:PRK08588 303 AKdVAKSYVGQDIPlsAIPGATDAssflkkkpdfPVI-------IFGPGNNLTAHQVDEYVEkdmyLKFIDIYKEIIIQ 374
M20_ArgE_DapE-like cd08011
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
41-375 1.30e-47

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: 165.25  E-value: 1.30e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  41 LADFGFKTEIlaVEGSRNKYNLLATYGEGEGG--LLLAGHTDTVPFDEGK-WRFNPFQLTEKAGKLYGLGTADMKGFFAF 117
Cdd:cd08011   31 LEDLGYPVEL--HEPPEEIYGVVSNIVGGRKGkrLLFNGHYDVVPAGDGEgWTVDPYSGKIKDGKLYGRGSSDMKGGIAA 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 118 VVEVVSQL--DLTQIKKPIRILATADEETT-MLGARTFAQHSHIRPDCAIIGEPTSLKPIR-AHKGHIGESVRITGRSGH 193
Cdd:cd08011  109 SIIAVARLadAKAPWDLPVVLTFVPDEETGgRAGTKYLLEKVRIKPNDVLIGEPSGSDNIRiGEKGLVWVIIEITGKPAH 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 194 SSDPAKGINAIELmhqsigyLMKMRDELREkyhnplfqvTHPTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLY 273
Cdd:cd08011  189 GSLPHRGESAVKA-------AMKLIERLYE---------LEKTVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVL 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 274 AMVNEHLKPMLEQYGdliEIRHLHDgipGYECEHSAQIVQVVE----KLLGEKcdAVNYCTEAP-----FIQQLCPTLVL 344
Cdd:cd08011  253 SRIIDHLDSIEEVSF---EIKSFYS---PTVSNPDSEIVKKTEeaitEVLGIR--PKEVISVGAsdarfYRNAGIPAIVY 324
                        330       340       350
                 ....*....|....*....|....*....|.
gi 493292681 345 GPGSIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:cd08011  325 GPGRLGQMHAPNEYVEIDELIKVIKVHALVA 355
DapE-ArgE TIGR01910
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ...
7-368 7.04e-46

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: 161.41  E-value: 7.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681    7 IQRYAQLIELPTISS-LVAEEDLSNrrlieLLATWLADFGFKTEILAVEGSR-NKYNLLATYGEGEGG---LLLAGHTDT 81
Cdd:TIGR01910   1 VELLKDLISIPSVNPpGGNEETIAN-----YIKDLLREFGFSTDVIEITDDRlKVLGKVVVKEPGNGNeksLIFNGHYDV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   82 VPF-DEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKP--IRILATADEETTMLGARTFAQHS-H 157
Cdd:TIGR01910  76 VPAgDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNgnIILQSVVDEESGEAGTLYLLQRGyF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  158 IRPDCAIIGEPTSLKPI-RAHKGHIGESVRITGRSGHSSDPAKGINAIE-LMHqsigYLMKMRDELREKY--HNPLFQVT 233
Cdd:TIGR01910 156 KDADGVLIPEPSGGDNIvIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMkLAK----LITELNELEEHIYarNSYGFIPG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  234 HPTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDlyamVNEHLKPMLEQYGDLIEIRHLHD-----GIPGYECEHS 308
Cdd:TIGR01910 232 PITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDE----VKQIIEDVVKALSKSDGWLYENEpvvkwSGPNETPPDS 307
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493292681  309 AQIVQ---VVEKLLGE--KCDAVNYCTEAPF-IQQLCPTLVLGPGSIEQAHQPDEFLEMK-YIEPTK 368
Cdd:TIGR01910 308 RLVKAleaIIKKVRGIepEVLVSTGGTDARFlRKAGIPSIVYGPGDLETAHQVNEYISIKnLVESTK 374
M20_ArgE_DapE-like_fungal cd05652
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
6-359 4.23e-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. 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: 137.02  E-value: 4.23e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   6 FIQRYAQLIELPTISSlvAEEDLSnrrliELLATWLADFGFKTEILAVEGSrNKYNLLATYGEGEG-GLLLAGHTDTVPf 84
Cdd:cd05652    1 LLSLHKSLVEIPSISG--NEAAVG-----DFLAEYLESLGFTVEKQPVENK-DRFNVYAYPGSSRQpRVLLTSHIDTVP- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  85 degkwRFNPFQLTEKAGKLYGLGTADMKGFFAfvVEVVSQLDLTQIKK----PIRILATADEETTMLGARTFAQHSHIRP 160
Cdd:cd05652   72 -----PFIPYSISDGGDTIYGRGSVDAKGSVA--AQIIAVEELLAEGEvpegDLGLLFVVGEETGGDGMKAFNDLGLNTW 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 161 DCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNplfqvthPTMNFG 240
Cdd:cd05652  145 DAVIFGEPTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPSSELLGP-------TTLNIG 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 241 NIHGGDAINRICACCE--LQFDMRPLPNMAVQDLYAMVNEHLKPmleqyGDLIEIRHLHDGIPGY-ECEhsaqivqvVEk 317
Cdd:cd05652  218 RISGGVAANVVPAAAEasVAIRLAAGPPEVKDIVKEAVAGILTD-----TEDIEVTFTSGYGPVDlDCD--------VD- 283
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 493292681 318 llGEKCDAVNYCTEAPFIQQLCPTLVLGPGSIEQAHQPDEFL 359
Cdd:cd05652  284 --GFETDVVAYGTDIPYLKGDHKRYLYGPGSILVAHGPDEAI 323
PRK08737 PRK08737
acetylornithine deacetylase; Provisional
45-365 6.25e-37

acetylornithine deacetylase; Provisional


Pssm-ID: 181544 [Multi-domain]  Cd Length: 364  Bit Score: 137.25  E-value: 6.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  45 GFKTEIlaVEGSRNKYNLLATYGEGEggLLLAGHTDTVPfDEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQ 124
Cdd:PRK08737  42 GFQVEV--IDHGAGAVSLYAVRGTPK--YLFNVHLDTVP-DSPHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANA 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 125 LDltqikKPIRILATADEET-TMLGARTFAQHSHiRPDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDP-AKGIN 202
Cdd:PRK08737 117 GD-----GDAAFLFSSDEEAnDPRCVAAFLARGI-PYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKqDPSAS 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 203 AIelmHQSIGYLMKMRDELREKYHNPLFQVTHPTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKP 282
Cdd:PRK08737 191 AL---HQAMRWGGQALDHVESLAHARFGGLTGLRFNIGRVEGGIKANMIAPAAELRFGFRPLPSMDVDGLLATFAGFAEP 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 283 MLEQYGDLIEIRHLHDGIPGYECEHSAQIVQVVEKLLGEKCDAVNYCTEAP-FIQQLCPTLVLGPGSIEQAHQPDEFLEM 361
Cdd:PRK08737 268 AAATFEETFRGPSLPSGDIARAEERRLAARDVADALDLPIGNAVDFWTEASlFSAAGYTALVYGPGDIAQAHTADEFVTL 347

                 ....
gi 493292681 362 KYIE 365
Cdd:PRK08737 348 DQLQ 351
PRK08652 PRK08652
acetylornithine deacetylase; Provisional
12-378 1.48e-34

acetylornithine deacetylase; Provisional


Pssm-ID: 236324 [Multi-domain]  Cd Length: 347  Bit Score: 130.26  E-value: 1.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  12 QLIELPTISslvAEEDlsnrRLIELLATWLADFGFKTEIlavEGSRNKYNLLAtygEGEGGLLLAGHTDTVPFdegkwRF 91
Cdd:PRK08652  10 QLVKIPSPS---GQED----EIALHIMEFLESLGYDVHI---ESDGEVINIVV---NSKAELFVEVHYDTVPV-----RA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  92 NPFqltEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEETTMLGARTFAqhSHIRPDCAIIGEPTSL 171
Cdd:PRK08652  72 EFF---VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVSDEEEGGRGSALFA--ERYRPKMAIVLEPTDL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 172 KPIRAHKGHIGESVRITGRSGHSSDPAKGINAIElmhQSIGYLMKMRDELREKyhNPLFQvthPTMNFGNIHGGDAINRI 251
Cdd:PRK08652 147 KVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIE---KAFEMLEKLKELLKAL--GKYFD---PHIGIQEIIGGSPEYSI 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 252 CACCELQFDMRPLPNMAVQDlyamVNEHLKPMLEQYGDLIEIRHLHDgipGYECEHSAQIVQVVEKLLGEK--------- 322
Cdd:PRK08652 219 PALCRLRLDARIPPEVEVED----VLDEIDPILDEYTVKYEYTEIWD---GFELDEDEEIVQLLEKAMKEVglepeftvm 291
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493292681 323 ---CDAVNycteapFIQQLCPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLIYHF 378
Cdd:PRK08652 292 rswTDAIN------FRYNGTKTVVWGPGELDLCHTKFERIDVREVEKAKEFLKALNEIL 344
M20_ArgE_DapE-like cd03895
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
57-380 2.89e-34

M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 130.51  E-value: 2.89e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  57 RNKYNLLATY-GEGEGG--LLLAGHTDTVPFDEGK-WRFNPFQLTEKAGKLYGLGTADMKG-----FFAFvvEVVSQLDL 127
Cdd:cd03895   58 AGAPNVVGTHrPRGETGrsLILNGHIDVVPEGPVElWTRPPFEATIVDGWMYGRGAGDMKAglaanLFAL--DALRAAGL 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 128 tQIKKPIRILATADEETTMLGARTFAQHSHiRPDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELM 207
Cdd:cd03895  136 -QPAADVHFQSVVEEECTGNGALAALMRGY-RADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKA 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 208 HQSIGYLMKMRDELREKYH-NPLF-QVTHP-TMNFGNIHGGDAINRICACCElqFDMRP--LPNMAVQDLYAMVNEHLK- 281
Cdd:cd03895  214 MHLIQALQELEREWNARKKsHPHFsDHPHPiNFNIGKIEGGDWPSSVPAWCV--LDCRIgiYPGESPEEARREIEECVAd 291
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 282 ------------PMLEQYGDLIEirhlhdgipGYECEHSAQIVQVV----EKLLGEKCD--AVNYCTEAPFIQQL--CPT 341
Cdd:cd03895  292 aaatdpwlsnhpPEVEWNGFQAE---------GYVLEPGSDAEQVLaaahQAVFGTPPVqsAMTATTDGRFFVLYgdIPA 362
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 493292681 342 LVLGPGSiEQAHQPDEFLEMKYI-EPTKELLTkLIYHFCG 380
Cdd:cd03895  363 LCYGPGS-RDAHGFDESVDLESLrKITKTIAL-FIAEWCG 400
M20_ArgE_DapE-like cd08013
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
21-379 3.63e-34

M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 129.90  E-value: 3.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  21 SLVAEEDLSNRRLIELLATWLADFGFKTEILavEGSRNKYNLLATYgEGEGG---LLLAGHTDTVPFDegKWRFNPFQLT 97
Cdd:cd08013   19 SLSATGGAGEAEIATYVAAWLAHRGIEAHRI--EGTPGRPSVVGVV-RGTGGgksLMLNGHIDTVTLD--GYDGDPLSGE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  98 EKAGKLYGLGTADMKGFFAfvVEVVSQLDLTqiKKPIR---ILA-TADEETTMLGARTFAQHShIRPDCAIIGEPTSLKP 173
Cdd:cd08013   94 IADGRVYGRGTLDMKGGLA--ACMAALADAK--EAGLRgdvILAaVADEEDASLGTQEVLAAG-WRADAAIVTEPTNLQI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 174 IRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLfqVTHPTMNFGNIHGGDAINRICA 253
Cdd:cd08013  169 IHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALEEYQQELPERPVDPL--LGRASVHASLIKGGEEPSSYPA 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 254 CCELQFDMRPLP----NMAVQDLYAMVNEhLKPMLEQYGDLIEIRHLHDgiPGYECEHSAQIVQVV----EKLLGEKC-- 323
Cdd:cd08013  247 RCTLTIERRTIPgetdESVLAELTAILGE-LAQTVPNFSYREPRITLSR--PPFEVPKEHPFVQLVaahaAKVLGEAPqi 323
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493292681 324 DAVNYCTEAPFIQQL-CPTLVLGPgSIEQAHQPDEFLEMKYIEPTKELLTKLIYHFC 379
Cdd:cd08013  324 RSETFWTDAALLAEAgIPSVVFGP-SGAGLHAKEEWVDVESIRQLREVLSAVVREFC 379
M20_CPDG2 cd03885
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ...
32-375 8.85e-34

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: 128.48  E-value: 8.85e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  32 RLIELLATWLADFGFKTEILAVEGSRNkyNLLATY-GEGEGGLLLAGHTDTVpFDEGKWRFNPFqlTEKAGKLYGLGTAD 110
Cdd:cd03885   23 RVAELLAEELEALGFTVERRPLGEFGD--HLIATFkGTGGKRVLLIGHMDTV-FPEGTLAFRPF--TVDGDRAYGPGVAD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 111 MKGFFAFVVEVVSQLDLTQIKK--PIRILATADEETTMLGARTFAQHSHIRPDCAIIGEPTSL--KPIRAHKGHIGESVR 186
Cdd:cd03885   98 MKGGLVVILHALKALKAAGGRDylPITVLLNSDEEIGSPGSRELIEEEAKGADYVLVFEPARAdgNLVTARKGIGRFRLT 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 187 ITGRSGHSS-DPAKGINAI-ELMHQSIGyLMKMRDELRekyhnplfqvtHPTMNFGNIHGGDAINRICACCELQFDMRpL 264
Cdd:cd03885  178 VKGRAAHAGnAPEKGRSAIyELAHQVLA-LHALTDPEK-----------GTTVNVGVISGGTRVNVVPDHAEAQVDVR-F 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 265 PNMA-----VQDLYAMVNEHLKPMLEqygdlIEIRHLHDGIPGYECEHSAQIVQVVEKL---LGEKCD--AVNYCTEAPF 334
Cdd:cd03885  245 ATAEeadrvEEALRAIVATTLVPGTS-----VELTGGLNRPPMEETPASRRLLARAQEIaaeLGLTLDweATGGGSDANF 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 493292681 335 IQQL-CPTL-VLGP-GsiEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:cd03885  320 TAALgVPTLdGLGPvG--GGAHTEDEYLELDSLVPRIKLLARLL 361
M20_DapE_proteobac cd03891
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ...
34-357 1.78e-32

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: 124.92  E-value: 1.78e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  34 IELLATWLADFGFKTEILAVEGSRNkynLLATYGEGEGGLLLAGHTDTVPF-DEGKWRFNPFQLTEKAGKLYGLGTADMK 112
Cdd:cd03891   21 QDLIAERLKALGFTCERLEFGGVKN---LWARRGTGGPHLCFAGHTDVVPPgDLEGWSSDPFSPTIKDGMLYGRGAADMK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 113 G----FFAFVVEVVSQLDltQIKKPIRILATADEETTML-GART---FAQHSHIRPDCAIIGEPTSLKpirahkgHIGES 184
Cdd:cd03891   98 GgiaaFVAAAERFVAKHP--NHKGSISFLITSDEEGPAIdGTKKvleWLKARGEKIDYCIVGEPTSEK-------KLGDT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 185 VRI------------TGRSGHSSDPAKGINAIELMHQSIGYLMKMR-DElrekyHNPLFQVThpTMNFGNIHGG-DAINR 250
Cdd:cd03891  169 IKIgrrgslngkltiKGKQGHVAYPHLADNPIHLLAPILAELTATVlDE-----GNEFFPPS--SLQITNIDVGnGATNV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 251 ICACCELQFDMRPLPNMAVQDLYAMVNEHLKpmleQYGDLIEIRHLHDG-----IPGyecEHSAQIVQVVEKLLGekcda 325
Cdd:cd03891  242 IPGELKAKFNIRFNDEHTGESLKARIEAILD----KHGLDYDLEWKLSGepfltKPG---KLVDAVSAAIKEVTG----- 309
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 493292681 326 vnYCTE---------APFIQQL-CPTLVLGPGSiEQAHQPDE 357
Cdd:cd03891  310 --ITPElstsggtsdARFIASYgCPVVEFGLVN-ATIHKVNE 348
M20_ArgE_DapE-like cd05651
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
13-375 4.83e-29

M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 115.10  E-value: 4.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  13 LIELPTISSlvaEEDlsnrRLIELLATWLADFGFKTEilavegsRNKYNLLA---TYGEGEGGLLLAGHTDTVPFDEGkW 89
Cdd:cd05651    9 LIATPSFSR---EEH----KTADLIENYLEQKGIPFK-------RKGNNVWAengHFDEGKPTLLLNSHHDTVKPNAG-W 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  90 RFNPFQLTEKAGKLYGLGTADMKGffafvvEVVSQL-------DLTQIKKPIRILATADEETT-MLGARTFAqhSHIRP- 160
Cdd:cd05651   74 TKDPFEPVEKGGKLYGLGSNDAGA------SVVSLLatflhlySEGPLNYNLIYAASAEEEISgKNGIESLL--PHLPPl 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 161 DCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPaKGINAIelmHQSIGYLMKMRDELREKYHNPLfqvTHPTMNFG 240
Cdd:cd05651  146 DLAIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAARN-EGDNAI---YKALDDIQWLRDFRFDKVSPLL---GPVKMTVT 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 241 NIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDlieiRHLHDGIPgyeCEHSaqivqVVEKLLG 320
Cdd:cd05651  219 QINAGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIRGNLKSEIKPRSF----RLNSSAIP---PDHP-----IVQAAIA 286
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493292681 321 EKCDAVNYCTEAPFIQQLCPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:cd05651  287 AGRTPFGSPTLSDQALMPFPSVKIGPGDSSRSHTADEFIELSEIEEGIDIYIELL 341
M20_yscS_like cd05675
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ...
10-321 1.83e-28

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: 115.15  E-value: 1.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  10 YAQLIELPTISSLvaEEDLSNRRLIELLATWLADFGFKTEILAVEGSRNKYNLLATYGEG---EGGLLLAGHTDTVPFDE 86
Cdd:cd05675    4 LQELIRIDTTNSG--DGTGSETRAAEVLAARLAEAGIQTEIFVVESHPGRANLVARIGGTdpsAGPLLLLGHIDVVPADA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  87 GKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQI--KKPIRILATADEET-TMLGARTFAQHshiRPDC- 162
Cdd:cd05675   82 SDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFkpKRDLVFAFVADEEAgGENGAKWLVDN---HPELf 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 163 -----AI---------IGEPTSLKPIR-AHKGHIGESVRITGRSGHSSDPAKGiNAI----------------------- 204
Cdd:cd05675  159 dgatfALneggggslpVGKGRRLYPIQvAEKGIAWMKLTVRGRAGHGSRPTDD-NAItrlaealrrlgahnfpvrltdet 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 205 ---------------ELMHQSIGYLMKMRDELREKyhNPLFQ-VTHPTMNFGNIHGGDAINRICACCELQFDMRPLPNMA 268
Cdd:cd05675  238 ayfaqmaelaggeggALMLTAVPVLDPALAKLGPS--APLLNaMLRNTASPTMLDAGYATNVLPGRATAEVDCRILPGQS 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493292681 269 VQdlyaMVNEHLKPMLEQYGdlIEIRHLHDgIPGYECEHSAQIVQVVEKLLGE 321
Cdd:cd05675  316 EE----EVLDTLDKLLGDPD--VSVEAVHL-EPATESPLDSPLVDAMEAAVQA 361
M20_dimer pfam07687
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ...
175-287 2.44e-28

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: 106.66  E-value: 2.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  175 RAHKGHIGESVRITGRSGHSSDPAKGINAIELMhqsigylMKMRDELREKYHNPLFQVTHPTMNFGNIHGGDAINRICAC 254
Cdd:pfam07687   1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLL-------ARLLAELPAEYGDIGFDFPRTTLNITGIEGGTATNVIPAE 73
                          90       100       110
                  ....*....|....*....|....*....|...
gi 493292681  255 CELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQY 287
Cdd:pfam07687  74 AEAKFDIRLLPGEDLEELLEEIEAILEKELPEG 106
PRK13009 PRK13009
succinyl-diaminopimelate desuccinylase; Reviewed
34-377 5.44e-28

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 237265 [Multi-domain]  Cd Length: 375  Bit Score: 112.87  E-value: 5.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  34 IELLATWLADFGFKTEILAVEGSRNkynLLATYGEGEGGLLLAGHTDTVPF-DEGKWRFNPFQLTEKAGKLYGLGTADMK 112
Cdd:PRK13009  25 QDLLAERLEALGFTCERMDFGDVKN---LWARRGTEGPHLCFAGHTDVVPPgDLEAWTSPPFEPTIRDGMLYGRGAADMK 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 113 GFFA-FVVEVVSQL-DLTQIKKPIRILATADEE------TT-MLgaRTFAQHsHIRPDCAIIGEPTSLKpirahkgHIGE 183
Cdd:PRK13009 102 GSLAaFVVAAERFVaAHPDHKGSIAFLITSDEEgpaingTVkVL--EWLKAR-GEKIDYCIVGEPTSTE-------RLGD 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 184 SVRI------------TGRSGHSSDPAKGINAIELMHQSIGYLMKMR-DElrekyHNPLFQVThpTMNFGNIHGG-DAIN 249
Cdd:PRK13009 172 VIKNgrrgsltgkltvKGVQGHVAYPHLADNPIHLAAPALAELAATEwDE-----GNEFFPPT--SLQITNIDAGtGATN 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 250 RICACCELQFDMRPLPNMAVQDLYAMVNEhlkpMLEQYGDLIEIRHLHDGIP-----GyecEHSAQIVQVVEKLLGEKcd 324
Cdd:PRK13009 245 VIPGELEAQFNFRFSTEHTAESLKARVEA----ILDKHGLDYTLEWTLSGEPfltppG---KLVDAVVAAIEAVTGIT-- 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493292681 325 avnycTE---------APFIQQLCPTLV-LGP--GSIeqaHQPDEFLEMKYIEPtkelLTKlIYH 377
Cdd:PRK13009 316 -----PElstsggtsdARFIADYGAQVVeFGPvnATI---HKVNECVSVADLEK----LTR-IYE 367
M20_ArgE_DapE-like cd05649
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
12-360 6.51e-28

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: 112.90  E-value: 6.51e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  12 QLIELPTISslvAEEdlsnRRLIELLATWLADFGFKTEILAVEGsrnkyNLLATYGEGEGGLLLAGHTDTVPF-DEGKWR 90
Cdd:cd05649    6 DLIQIPSES---GEE----KGVVERIEEEMEKLGFDEVEIDPMG-----NVIGYIGGGKKKILFDGHIDTVGIgNIDNWK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  91 FNPFQLTEKAGKLYGLGTADMKGFFAFVV---EVVSQLDLTQIKKPIRILATADEET-TMLGARTFAQHSHIRPDCAIIG 166
Cdd:cd05649   74 FDPYEGYETDGKIYGRGTSDQKGGLASMVyaaKIMKDLGLRDFAYTILVAGTVQEEDcDGVCWQYISKADKIKPDFVVSG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 167 EPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIelmhqsigylMKMRDELRE-KYHNPLFQvTHPTMNFGNIHGG 245
Cdd:cd05649  154 EPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAV----------YKMADIIQDiRQLNPNFP-EAPFLGRGTLTVT 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 246 DAINR---ICAC---CELQFDMRplpnMAVQDLYAMVNEHLK--PMLEQYGDLIEIRHLHDGIPGY-------EC----- 305
Cdd:cd05649  223 DIFSTspsRCAVpdsCRISIDRR----LTVGETWEGCLEEIRalPAVKKYGDDVAVSMYNYDRPSYtgevyesERyfptw 298
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493292681 306 ------EHSAQIVQVVEKLLGEK--CDAVNYCTEAPFIQ--QLCPTLVLGPGSIEQAHQPDEFLE 360
Cdd:cd05649  299 llpedhELVKALLEAYKALFGARplIDKWTFSTNGVSIMgrAGIPCIGFGPGAENQAHAPNEYTW 363
PRK13004 PRK13004
YgeY family selenium metabolism-linked hydrolase;
61-373 2.40e-25

YgeY family selenium metabolism-linked hydrolase;


Pssm-ID: 183836 [Multi-domain]  Cd Length: 399  Bit Score: 105.79  E-value: 2.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  61 NLLATYGEGEGGLLLAGHTDTVPF-DEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQL-DLTqIKKPIRILA 138
Cdd:PRK13004  60 NVLGYIGHGKKLIAFDAHIDTVGIgDIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIkDLG-LDDEYTLYV 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 139 TA---DEETTMLGARTFAQHSHIRPDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLM 215
Cdd:PRK13004 139 TGtvqEEDCDGLCWRYIIEEDKIKPDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELE 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 216 KMRDELREkyhnplfqvtHPTMNFGNIHGGDAINR---ICAC---CELQFDMRPL----PNMAVQDLYAMVN-EHLKPML 284
Cdd:PRK13004 219 ELNPNLKE----------DPFLGKGTLTVSDIFSTspsRCAVpdsCAISIDRRLTvgetWESVLAEIRALPAvKKANAKV 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 285 EQY--------GDLIEIRHLhdgIPGYECEHSAQIVQVVEK----LLGE--KCDAVNYCTEAPFIQQL--CPTLVLGPGS 348
Cdd:PRK13004 289 SMYnydrpsytGLVYPTECY---FPTWLYPEDHEFVKAAVEaykgLFGKapEVDKWTFSTNGVSIAGRagIPTIGFGPGK 365
                        330       340
                 ....*....|....*....|....*
gi 493292681 349 IEQAHQPDEflemkYIEptKELLTK 373
Cdd:PRK13004 366 EPLAHAPNE-----YTW--KEQLVK 383
M20_ArgE_LysK cd05653
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ...
13-272 1.37e-23

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: 100.12  E-value: 1.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  13 LIELPTISSLVAEEdlsnRRLIELLATWLADFGFKTEILAVEgsrnkyNLLATYGEGEGGLLLAGHTDTVPfdeGkwrFN 92
Cdd:cd05653    7 LLDLLSIYSPSGEE----ARAAKFLEEIMKELGLEAWVDEAG------NAVGGAGSGPPDVLLLGHIDTVP---G---EI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  93 PFQLTEkaGKLYGLGTADMKGFFAFVVEVVSQLDLtqiKKPIR--ILATADEETTMLGARtFAQHSHIRPDCAIIGEPTS 170
Cdd:cd05653   71 PVRVEG--GVLYGRGAVDAKGPLAAMILAASALNE---ELGARvvVAGLVDEEGSSKGAR-ELVRRGPRPDYIIIGEPSG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 171 LKPIR-AHKGHIGESVRITGRSGHSSDPakGINAIELMHQSIgYLMKMRDELREKYHNPLFQVThPTMnfgnIHGGDAIN 249
Cdd:cd05653  145 WDGITlGYRGSLLVKIRCEGRSGHSSSP--ERNAAEDLIKKW-LEVKKWAEGYNVGGRDFDSVV-PTL----IKGGESSN 216
                        250       260
                 ....*....|....*....|....
gi 493292681 250 RICACCELQFDMR-PLPNMAVQDL 272
Cdd:cd05653  217 GLPQRAEATIDLRlPPRLSPEEAI 240
PepD2 COG2195
Di- or tripeptidase [Amino acid transport and metabolism];
7-375 2.90e-23

Di- or tripeptidase [Amino acid transport and metabolism];


Pssm-ID: 441798 [Multi-domain]  Cd Length: 364  Bit Score: 99.35  E-value: 2.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   7 IQRYAQLIELPTISSlvAEEDLSNrrlieLLATWLADFGFKTEIlavegsRNKYNLL----ATYGEGEGGLLLAGHTDTV 82
Cdd:COG2195    6 LERFLEYVKIPTPSD--HEEALAD-----YLVEELKELGLEVEE------DEAGNVIatlpATPGYNVPTIGLQAHMDTV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  83 PFDEGKwrfnPFQLTEKAGKLYGLGT----ADMKGFFAFVVEVVSQLDLTQIK-KPIRILATADEETTMLGARTFaQHSH 157
Cdd:COG2195   73 PQFPGD----GIKPQIDGGLITADGTttlgADDKAGVAAILAALEYLKEPEIPhGPIEVLFTPDEEIGLRGAKAL-DVSK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 158 IRPDCAII--GEPtslkpirahkghIGE-----------SVRITGRSGHSSD-PAKGINAIELMHQSIgYLMKmRDELRE 223
Cdd:COG2195  148 LGADFAYTldGGE------------EGEleyecagaadaKITIKGKGGHSGDaKEKMINAIKLAARFL-AALP-LGRIPE 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 224 KYhnplfqvthpTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYG-DLIEIRHlHDGIPG 302
Cdd:COG2195  214 ET----------EGNEGFIHGGSATNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGvGVVEVEI-EDQYPN 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 303 YECEHSAQIVQVVEKL---LGEKCD--AVNYCTEAPFI--QQLcPTLVLGPGsIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:COG2195  283 WKPEPDSPIVDLAKEAyeeLGIEPKikPIRGGLDGGILsfKGL-PTPNLGPG-GHNFHSPDERVSIESMEKAWELLVEIL 360
PRK06837 PRK06837
ArgE/DapE family deacylase;
60-314 1.01e-22

ArgE/DapE family deacylase;


Pssm-ID: 180721 [Multi-domain]  Cd Length: 427  Bit Score: 98.92  E-value: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  60 YNLLATY-GEGEGG--LLLAGHTDTVPfdEG---KWRFNPFQLTEKAGKLYGLGTADMKGFFA---FVVEVVSQLDLtQI 130
Cdd:PRK06837  84 PNVVGTYrPAGKTGrsLILQGHIDVVP--EGpldLWSRPPFDPVIVDGWMYGRGAADMKAGLAamlFALDALRAAGL-AP 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 131 KKPIRILATADEETTMLGARTFAQHSHiRPDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQS 210
Cdd:PRK06837 161 AARVHFQSVIEEESTGNGALSTLQRGY-RADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHL 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 211 IGYLMKMRDEL-REKYHNPLF-QVTHP-TMNFGNIHGGDAINRICACCElqFDMRP--LPNMAVQDLYA----------- 274
Cdd:PRK06837 240 IQALRELEAEWnARKASDPHFeDVPHPiNFNVGIIKGGDWASSVPAWCD--LDCRIaiYPGVTAADAQAeieaclaaaar 317
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 493292681 275 ---MVNEHLkPMLEQYGDLIEirhlhdgipGYECEHSAQIVQV 314
Cdd:PRK06837 318 ddrFLSNNP-PEVVWSGFLAE---------GYVLEPGSEAEAA 350
PRK06915 PRK06915
peptidase;
61-380 4.88e-21

peptidase;


Pssm-ID: 180745 [Multi-domain]  Cd Length: 422  Bit Score: 93.99  E-value: 4.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  61 NLLATY-GEGEG-GLLLAGHTDTVPF-DEGKWRFNPFQLTEKAGKLYGLGTADMKG---FFAFVVEVVSQLDLtQIKKPI 134
Cdd:PRK06915  82 NIVATLkGSGGGkSMILNGHIDVVPEgDVNQWDHHPYSGEVIGGRIYGRGTTDMKGgnvALLLAMEALIESGI-ELKGDV 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 135 RILATADEETTmlGARTFAqhSHIR---PDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIE-LMH-- 208
Cdd:PRK06915 161 IFQSVIEEESG--GAGTLA--AILRgykADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEkSMFvi 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 209 QSIGYLMKMRDelrEKYHNPLFQ-VTHPT-MNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDlyamVNEHLKPMLEQ 286
Cdd:PRK06915 237 DHLRKLEEKRN---DRITDPLYKgIPIPIpINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEA----AKEEFENWIAE 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 287 YGDLIE--IRHLHD-------GIPG-YECEHS--AQIVQVVEKLLGEK--CDAVNYCTEAPFIQQL--CPTLVLGPGSIE 350
Cdd:PRK06915 310 LNDVDEwfVEHPVEvewfgarWVPGeLEENHPlmTTLEHNFVEIEGNKpiIEASPWGTDGGLLTQIagVPTIVFGPGETK 389
                        330       340       350
                 ....*....|....*....|....*....|
gi 493292681 351 QAHQPDEFLEMKYIEPTKELLTKLIYHFCG 380
Cdd:PRK06915 390 VAHYPNEYIEVDKMIAAAKIIALTLLDWCE 419
PRK13983 PRK13983
M20 family metallo-hydrolase;
35-358 2.57e-20

M20 family metallo-hydrolase;


Pssm-ID: 237578 [Multi-domain]  Cd Length: 400  Bit Score: 91.45  E-value: 2.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  35 ELLATWLADFGFKT-EILAVEGSRNKY----NLLATY--GEGEGGLLLAGHTDTVPF-DEGKWRFNPFQLTEKAGKLYGL 106
Cdd:PRK13983  34 EYLESLLKEYGFDEvERYDAPDPRVIEgvrpNIVAKIpgGDGKRTLWIISHMDVVPPgDLSLWETDPFKPVVKDGKIYGR 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 107 GTAD-MKGFFA--FVVEVVSQLDLTQiKKPIRILATADEETtmlGAR-----TFAQHSHI-RPDCAII----GEPTSLKP 173
Cdd:PRK13983 114 GSEDnGQGIVSslLALKALMDLGIRP-KYNLGLAFVSDEET---GSKygiqyLLKKHPELfKKDDLILvpdaGNPDGSFI 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 174 IRAHKGHIGESVRITGRSGHSSDPAKGINA-IELMHqsigYLMKMRDELREKYH--NPLFQVTH----PTMNFGNIhggD 246
Cdd:PRK13983 190 EIAEKSILWLKFTVKGKQCHASTPENGINAhRAAAD----FALELDEALHEKFNakDPLFDPPYstfePTKKEANV---D 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 247 AINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGIPGYECEHSAQIVQ----VVEKLLGEk 322
Cdd:PRK13983 263 NINTIPGRDVFYFDCRVLPDYDLDEVLKDIKEIADEFEEEYGVKIEVEIVQREQAPPPTPPDSEIVKklkrAIKEVRGI- 341
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 493292681 323 cdAVNYC-----TEAPFIQQL-CPTLVLGPGsIEQAHQPDEF 358
Cdd:PRK13983 342 --EPKVGgigggTVAAFLRKKgYPAVVWSTL-DETAHQPNEY 380
M20_PAAh_like cd03896
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ...
14-370 2.80e-20

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: 91.00  E-value: 2.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  14 IELPTIsslvAEEDLSnrrliELLATWLADFGF-KTEILAVegsrnkYNLLATY-GEGEG-GLLLAGHTDTVpFDEGkwr 90
Cdd:cd03896   10 IPAPTF----REGARA-----DLVAEWMADLGLgDVERDGR------GNVVGRLrGTGGGpALLFSAHLDTV-FPGD--- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  91 fNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQI--KKPIRILATADEE--TTMLGARTFAQHSHIRPDCAIIG 166
Cdd:cd03896   71 -TPATVRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAalKGDVVFAANVGEEglGDLRGARYLLSAHGARLDYFVVA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 167 EPTSLKPiraHKGHIGESV-RIT--GRSGHSSDPAKGINAIELMHQSIGYLmkmrdelrEKYHNPlfQVTHPTMNFGNIH 243
Cdd:cd03896  150 EGTDGVP---HTGAVGSKRfRITtvGPGGHSYGAFGSPSAIVAMAKLVEAL--------YEWAAP--YVPKTTFAAIRGG 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 244 GGDAINRICACCELQFDMRPLPNMA----VQDLYAMVNE------HLKPMLEQYGDLieirhlhdgiPGYECEHSAQIVQ 313
Cdd:cd03896  217 GGTSVNRIANLCSMYLDIRSNPDAEladvQREVEAVVSKlaakhlRVKARVKPVGDR----------PGGEAQGTEPLVN 286
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493292681 314 VV-----EKLLGEKCDAvnYCTEA-PFIQQLCPTLVLGPGSIEQAHQPDEflemkYIEPTKEL 370
Cdd:cd03896  287 AAvaahrEVGGDPRPGS--SSTDAnPANSLGIPAVTYGLGRGGNAHRGDE-----YVLKDDML 342
PRK13013 PRK13013
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
11-358 8.14e-20

acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;


Pssm-ID: 237268 [Multi-domain]  Cd Length: 427  Bit Score: 90.20  E-value: 8.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  11 AQLIELPTISSlvaeEDLSNRRLIELLATWLADFGFKTEILAVEGSRN------KYNLLATY-GEGEGGLL-LAGHTDTV 82
Cdd:PRK13013  21 QDLIRIPTLNP----PGRAYREICEFLAARLAPRGFEVELIRAEGAPGdsetypRWNLVARRqGARDGDCVhFNSHHDVV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  83 PFDEGkWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKP--IRILATADEETTMLGARTF-AQH---S 156
Cdd:PRK13013  97 EVGHG-WTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAgsIEISGTADEESGGFGGVAYlAEQgrfS 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 157 HIRPDCAIIGEPTSLKPI-RAHKGHIGESVRITGRSGHSSDPAKGINAIELMHqsiGYLMKMRDELRekyhnPLFQVT-- 233
Cdd:PRK13013 176 PDRVQHVIIPEPLNKDRIcLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMG---AVLAEIEERLF-----PLLATRrt 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 234 ----------HPTMNFGNIHGG--------DAINRICAC--CELQFDMRPLpnmaVQDLYAMVNEHLKPMLEQY-----G 288
Cdd:PRK13013 248 ampvvpegarQSTLNINSIHGGepeqdpdyTGLPAPCVAdrCRIVIDRRFL----IEEDLDEVKAEITALLERLkrarpG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 289 DLIEIRHLHDGIPGYeCEHSAQIVQVV----EKLLGEKCDAVnyctEAP---------FIQQLCPTLVLGPGSIEQAHQP 355
Cdd:PRK13013 324 FAYEIRDLFEVLPTM-TDRDAPVVRSVaaaiERVLGRQADYV----VSPgtydqkhidRIGKLKNCIAYGPGILDLAHQP 398

                 ...
gi 493292681 356 DEF 358
Cdd:PRK13013 399 DEW 401
PRK06133 PRK06133
glutamate carboxypeptidase; Reviewed
31-375 6.62e-19

glutamate carboxypeptidase; Reviewed


Pssm-ID: 235710 [Multi-domain]  Cd Length: 410  Bit Score: 87.38  E-value: 6.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  31 RRLIELLATWLADFGFKTEILAVEGSRNKyNLLATY-GEGEGGLLLAGHTDTVpFDEGKWRFNPFQltEKAGKLYGLGTA 109
Cdd:PRK06133  60 KQVAALLAERLKALGAKVERAPTPPSAGD-MVVATFkGTGKRRIMLIAHMDTV-YLPGMLAKQPFR--IDGDRAYGPGIA 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 110 DMKGFFAFV---VEVVSQLDLTQIKKpIRILATADEETTMLGARTF-----AQHshirpDCAIIGEPTSLKP--IRAHKG 179
Cdd:PRK06133 136 DDKGGVAVIlhaLKILQQLGFKDYGT-LTVLFNPDEETGSPGSRELiaelaAQH-----DVVFSCEPGRAKDalTLATSG 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 180 HIGESVRITGRSGHS-SDPAKGINA-IELMHQsigyLMKMRDELREkyhnplfqVTHPTMNFGNIHGGDAINRICACCEL 257
Cdd:PRK06133 210 IATALLEVKGKASHAgAAPELGRNAlYELAHQ----LLQLRDLGDP--------AKGTTLNWTVAKAGTNRNVIPASASA 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 258 QFDMRPLPNMAV----QDLYAMVNEHLKPMLEqygdlIEIRhLHDGIPGYE--------CEHSAQI-------VQVVEKL 318
Cdd:PRK06133 278 QADVRYLDPAEFdrleADLQEKVKNKLVPDTE-----VTLR-FERGRPPLEanaasralAEHAQGIygelgrrLEPIDMG 351
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493292681 319 LGEKCDA--VNYCTEAPFIQQLCptlVLGPGsieqAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:PRK06133 352 TGGGTDAafAAGSGKAAVLEGFG---LVGFG----AHSNDEYIELNSIVPRLYLLTRMI 403
M20_ArgE_DapE-like cd05650
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
35-364 2.85e-18

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: 85.59  E-value: 2.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  35 ELLATWLADFGFKT-EILAVEGSRNKY--NLLATYGEGEGGLL-LAGHTDTVPF-DEGKWRFNPFQLTEKAGKLYGLGTA 109
Cdd:cd05650   30 DYLEKKLREYGFYTlERYDAPDERGIIrpNIVAKIPGGNDKTLwIISHLDTVPPgDLSLWETDPWEPVVKDGKIYGRGVE 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 110 D-MKGFFA--FVVEVVSQLDLTQiKKPIRILATADEET-TMLGARTFAQHSHI-RPDCAII----GEPTSLKPIRAHKGH 180
Cdd:cd05650  110 DnQQGIVSslLALKAIIKNGITP-KYNFGLLFVADEEDgSEYGIQYLLNKFDLfKKDDLIIvpdfGTEDGEFIEIAEKSI 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 181 IGESVRITGRSGHSSDPAKGINAielMHQSIGYLMKMRDELREKYH--NPLFQVTH----PTMNFGNIhggDAINRICAC 254
Cdd:cd05650  189 LWIKVNVKGKQCHASTPENGINA---FVAASNFALELDELLHEKFDekDDLFNPPYstfePTKKEANV---PNVNTIPGY 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 255 CELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGIPGYECEHSAQIV----QVVEKLLG--EKCDAVNY 328
Cdd:cd05650  263 DVFYFDCRVLPTYKLDEVLKFVNKIISDFENSYGAGITYEIVQKEQAPPATPEDSEIVvrlsKAIKKVRGreAKLIGIGG 342
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 493292681 329 CTEAPFIQQL-CPTLVLGPGsIEQAHQPDEFLEMKYI 364
Cdd:cd05650  343 GTVAAFLRKKgYPAVVWSTL-DETAHQPNEYIRISHI 378
PRK09133 PRK09133
hypothetical protein; Provisional
10-204 5.04e-17

hypothetical protein; Provisional


Pssm-ID: 236388 [Multi-domain]  Cd Length: 472  Bit Score: 82.36  E-value: 5.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  10 YAQLIELPTISSLVaeedlSNRRLIELLATWLADFGFKTEILAVEGSR-NKYNLLATY-GEGEGG-LLLAGHTDTVPFDE 86
Cdd:PRK09133  43 YKELIEINTTASTG-----STTPAAEAMAARLKAAGFADADIEVTGPYpRKGNLVARLrGTDPKKpILLLAHMDVVEAKR 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  87 GKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDlTQIKKPIR--ILA-TADEE-TTMLGARTFAQH--SHIRP 160
Cdd:PRK09133 118 EDWTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLK-REGFKPKRdiILAlTGDEEgTPMNGVAWLAENhrDLIDA 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493292681 161 DCAI----------IGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGiNAI 204
Cdd:PRK09133 197 EFALneggggtldeDGKPVLLTVQAGEKTYADFRLEVTNPGGHSSRPTKD-NAI 249
PRK04443 PRK04443
[LysW]-lysine hydrolase;
13-207 2.56e-16

[LysW]-lysine hydrolase;


Pssm-ID: 235299 [Multi-domain]  Cd Length: 348  Bit Score: 79.23  E-value: 2.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  13 LIELPTISSLVAEEdlsnRRLIELLATWLADFGFKTEILAVEgsrnkyNLLATYGEGEGGLLLAGHTDTVPFDEgkwrfn 92
Cdd:PRK04443  12 LKGLVEIPSPSGEE----AAAAEFLVEFMESHGREAWVDEAG------NARGPAGDGPPLVLLLGHIDTVPGDI------ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  93 PFQLteKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATaDEETTMLGARTFAQHSHiRPDCAIIGEPTSLK 172
Cdd:PRK04443  76 PVRV--EDGVLWGRGSVDAKGPLAAFAAAAARLEALVRARVSFVGAV-EEEAPSSGGARLVADRE-RPDAVIIGEPSGWD 151
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 493292681 173 PIR-AHKGHIGESVRITGRSGHSSDPakGINAIELM 207
Cdd:PRK04443 152 GITlGYKGRLLVTYVATSESFHSAGP--EPNAAEDA 185
M20_18_42 cd18669
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ...
61-170 5.04e-16

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: 75.93  E-value: 5.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  61 NLLATYGEGEGG--LLLAGHTDTVPFDEGKWRFNPFQ-LTEKAGKLYGLGTADMKGFFAFVVEVVSQL--DLTQIKKPIR 135
Cdd:cd18669    1 NVIARYGGGGGGkrVLLGAHIDVVPAGEGDPRDPPFFvDTVEEGRLYGRGALDDKGGVAAALEALKLLkeNGFKLKGTVV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 493292681 136 ILATADEETTMlGARTFAQHS-----HIRPDCAIIGEPTS 170
Cdd:cd18669   81 VAFTPDEEVGS-GAGKGLLSKdaleeDLKVDYLFVGDATP 119
M20_ArgE-related cd08012
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ...
20-281 5.73e-16

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: 78.65  E-value: 5.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  20 SSLVAEEDLSNRRLIELLATWLADFGFKTEILAVEGSRNKYNLLATY-GEGEGGLL--LAGHTDTVPFDEGKWRFNPFQL 96
Cdd:cd08012   25 PQLVPKEDNAGRHVLEALTPYSTENGGPLVIDHVSYVKGRGNIIVEYpGTVDGKTVsfVGSHMDVVTANPETWEFDPFSL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  97 TEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILAT--ADEE-TTMLGARTFAQHSHirpdcaiiGEPTSLK- 172
Cdd:cd08012  105 SIDGDKLYGRGTTDCLGHVALVTELFRQLATEKPALKRTVVAVfiANEEnSEIPGVGVDALVKS--------GLLDNLKs 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 173 ------------PIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKM--------RDELREKYHNPlfQV 232
Cdd:cd08012  177 gplywvdsadsqPCIGTGGMVTWKLTATGKLFHSGLPHKAINALELVMEALAEIQKRfyidfpphPKEEVYGFATP--ST 254
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 493292681 233 THPTMnFGNIHGGdaINRICACCELQFDMRPLPNMAVQDLYAMVNEHLK 281
Cdd:cd08012  255 MKPTQ-WSYPGGS--INQIPGECTICGDCRLTPFYDVKEVREKLEEYVD 300
M20_like cd02697
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ...
35-265 6.72e-16

M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc.


Pssm-ID: 349869 [Multi-domain]  Cd Length: 394  Bit Score: 78.37  E-value: 6.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  35 ELLATWLADFGFKTEILAVE-------GSRNKYNLLA--TYGEGEGGLLLAGHTDTVPFDEGkWRFNPFQLTEKAGKLYG 105
Cdd:cd02697   29 ERTAALLQGFGFEAERHPVPeaevrayGMESITNLIVrrRYGDGGRTVALNAHGDVVPPGDG-WTRDPYGAVVEDGVMYG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 106 LGTADMKGFFA---FVVEVVSQLDLTqIKKPIRILATADEETT-MLGARTFAQHSHIRPDCAIIGEpTSLKPIRAHKGHI 181
Cdd:cd02697  108 RAAAVSKSDFAsftFAVRALESLGAP-LRGAVELHFTYDEEFGgELGPGWLLRQGLTKPDLLIAAG-FSYEVVTAHNGCL 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 182 GESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKyHNPLFQVTHPTMNFGNIHGGDAINRICACCELQFDM 261
Cdd:cd02697  186 QMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYALNAQYRQV-SSQVEGITHPYLNVGRIEGGTNTNVVPGKVTFKLDR 264

                 ....
gi 493292681 262 RPLP 265
Cdd:cd02697  265 RMIP 268
Zinc_peptidase_like cd03873
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
61-169 1.28e-15

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: 74.77  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  61 NLLATYGEGEGG--LLLAGHTDTVPFDEGKWRFNPFQ-LTEKAGKLYGLGTADMKGFFAFVVEVVSQL--DLTQIKKPIR 135
Cdd:cd03873    1 NLIARLGGGEGGksVALGAHLDVVPAGEGDNRDPPFAeDTEEEGRLYGRGALDDKGGVAAALEALKRLkeNGFKPKGTIV 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 493292681 136 ILATADEETTMlGARTFAQHS-----HIRPDCAIIGEPT 169
Cdd:cd03873   81 VAFTADEEVGS-GGGKGLLSKfllaeDLKVDAAFVIDAT 118
M20_yscS cd05674
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ...
7-239 1.29e-15

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: 78.07  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   7 IQRYAQLIELPTISSLVAEEDLSNRRLIEL--LATWLA-DFGFKTEILAVEgSRNKYNLLATYgegEGG------LLLAG 77
Cdd:cd05674    1 IERLSGAVQIPTVSFDDMPPIDEDERWDAFykFHDYLEkTFPLVHKTLKVE-VVNEYGLLYTW---EGSdpslkpLLLMA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  78 HTDTVP---FDEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLdLTQIKKPIR--ILATA-DEETT-MLGAR 150
Cdd:cd05674   77 HQDVVPvnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELL-LKRGFKPRRtiILAFGhDEEVGgERGAG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 151 TFAQHSHIR--PDCA--------------IIGEPTSLkPIRAHKGHIGESVRITGRSGHSSDPAKginaielmHQSIGYL 214
Cdd:cd05674  156 AIAELLLERygVDGLaaildeggavlegvFLGVPFAL-PGVAEKGYMDVEITVHTPGGHSSVPPK--------HTGIGIL 226
                        250       260
                 ....*....|....*....|....*
gi 493292681 215 MKMRDELREKYHNPLFQVTHPTMNF 239
Cdd:cd05674  227 SEAVAALEANPFPPKLTPGNPYYGM 251
M20_DapE_actinobac cd05647
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ...
57-372 2.42e-15

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: 76.33  E-value: 2.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  57 RNKYNLLATYGEG-EGGLLLAGHTDTVPFDE---GKWrfnpfqltEKAGKLYGLGTADMKG-------FFAFVVEVVSQL 125
Cdd:cd05647   39 RDGNTVVARTERGlASRVILAGHLDTVPVAGnlpSRV--------EEDGVLYGCGATDMKAgdavqlkLAATLAAATLKH 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 126 DLTQI---KKPIrilatADEETTMlgARTFAQH-SHIRPDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGI 201
Cdd:cd05647  111 DLTLIfydCEEV-----AAELNGL--GRLAEEHpEWLAADFAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGE 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 202 NAIelmHQSIGYLMKMrDELREKYHNPLFQVTHPTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVqdlyAMVNEHLK 281
Cdd:cd05647  184 NAI---HKLAPILARL-AAYEPRTVNIDGLTYREGLNAVFISGGVAGNVIPDEARVNLNYRFAPDKSL----AEAIAHVR 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 282 PMLEQYGDLIEIRhlhDGIPGYECEHSAQIVQVVEKLLGEKCDAVNYCTE-APFIQQLCPTLVLGPGSIEQAHQPDEFLE 360
Cdd:cd05647  256 EVFEGLGYEIEVT---DLSPGALPGLDHPVARDLIEAVGGKVRAKYGWTDvARFSALGIPAVNFGPGDPLLAHKRDEQVP 332
                        330
                 ....*....|..
gi 493292681 361 MKYIEPTKELLT 372
Cdd:cd05647  333 VEQITACAAILR 344
PRK07906 PRK07906
hypothetical protein; Provisional
35-195 2.63e-15

hypothetical protein; Provisional


Pssm-ID: 181163 [Multi-domain]  Cd Length: 426  Bit Score: 76.81  E-value: 2.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  35 ELLATWLADFGFKTEIlaVEGSRNKYNLLATYgEGE----GGLLLAGHTDTVPFDEGKWRFNPFQLTEKAGKLYGLGTAD 110
Cdd:PRK07906  29 EYVAEKLAEVGLEPTY--LESAPGRANVVARL-PGAdpsrPALLVHGHLDVVPAEAADWSVHPFSGEIRDGYVWGRGAVD 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 111 MKGFFAFVVEVVSQLDLTQIKKP--IRILATADEETTM-LGARTFAQHshiRPD----C--AI---------IGEPTSLK 172
Cdd:PRK07906 106 MKDMDAMMLAVVRHLARTGRRPPrdLVFAFVADEEAGGtYGAHWLVDN---HPElfegVteAIsevggfsltVPGRDRLY 182
                        170       180
                 ....*....|....*....|....
gi 493292681 173 PIR-AHKGHIGESVRITGRSGHSS 195
Cdd:PRK07906 183 LIEtAEKGLAWMRLTARGRAGHGS 206
dapE-gram_pos TIGR01900
succinyl-diaminopimelate desuccinylase; This model represents a clade of ...
74-365 7.06e-15

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: 75.01  E-value: 7.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   74 LLAGHTDTVPFDE---GKWRfnpfqltekAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEE----TTM 146
Cdd:TIGR01900  61 ILAGHLDTVPIADnlpSRVE---------GGRLYGRGAVDMKGGLAVMLALAATLDRTEPRHDLTLVFYEREEgpaeENG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  147 LGaRTFAQHSH-IRPDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIelmHQSIGYLMKMRD-ELREK 224
Cdd:TIGR01900 132 LG-RLLREHPEwLAGDLAVLLEPTDGKIEAGCQGTLRATVTFHGRRAHSARSWMGENAI---HKAAPILARLAAyEPREV 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  225 YHNPL--FQVTHPTMnfgnIHGGDAINRICACCELQFDMRPLPNMAVqdlyAMVNEHLKPMLEQYGDLIEIRhlhDGIPG 302
Cdd:TIGR01900 208 TVDGLtyREGLNAVR----IEGGVAGNVIPDECEVNVNYRFAPDRSL----EQARAHVRELFEGDGAEVEVT---DLSPG 276
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493292681  303 YECEHSAQIVQVVEKLLGEKCDAVNYCTE-APFIQQLCPTLVLGPGSIEQAHQPDEFLEMKYIE 365
Cdd:TIGR01900 277 ARPGLDNPLAAELVAAVGGEVRAKYGWTDvARFSALGIPAVNFGPGDPALAHQDDEHVPVAQLT 340
M20_PepV cd03888
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ...
42-207 1.28e-14

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: 74.97  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  42 ADFGFKTEILavegsrNKYNLLATYGEGEGGLLLAGHTDTVPFDEGkWRFNPFQLTEKAGKLYGLGTADMKG-----FFA 116
Cdd:cd03888   49 KRLGFKTKNI------DNYAGYAEYGEGEEVLGILGHLDVVPAGEG-WTTDPFKPVIKDGKLYGRGTIDDKGptiaaLYA 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 117 fvVEVVSQLDLtQIKKPIRILATADEETTMLGARTFAQHSHIrPDCA---------IIGE-------------PTSLKPI 174
Cdd:cd03888  122 --LKILKDLGL-PLKKKIRLIFGTDEETGWKCIEHYFEHEEY-PDFGftpdaefpvINGEkgivtvdltfkidDDKGYRL 197
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493292681 175 ---------------------RAHKGHIGES-----------------VRITGRSGHSSDPAKGINAIELM 207
Cdd:cd03888  198 isikggeatnmvpdkaeavipGKDKEELALSaatdlkgnieiddggveLTVTGKSAHASAPEKGVNAITLL 268
PRK00466 PRK00466
acetyl-lysine deacetylase; Validated
29-266 1.98e-14

acetyl-lysine deacetylase; Validated


Pssm-ID: 166979 [Multi-domain]  Cd Length: 346  Bit Score: 73.66  E-value: 1.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  29 SNRRLIELLATWLADFGFKTEILAvegSRNKYNLlatygeGEGGLLLAGHTDTVPfdegkWRFNPFQLTEkagKLYGLGT 108
Cdd:PRK00466  28 NETNATKFFEKISNELNLKLEILP---DSNSFIL------GEGDILLASHVDTVP-----GYIEPKIEGE---VIYGRGA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 109 ADMKGFFAFVVEVVSQLDLTQIKkpIRILATADEETTMLGARTFAQhSHIRPDCAIIGEPT-SLKPIRAHKGHIGESVRI 187
Cdd:PRK00466  91 VDAKGPLISMIIAAWLLNEKGIK--VMVSGLADEESTSIGAKELVS-KGFNFKHIIVGEPSnGTDIVVEYRGSIQLDIMC 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 188 TGRSGHSSDPAKGInAIELMHQSIGYLmkmrdELREKYHNPLFQVTHptmnfgnIHGGDAINRICACCELQFDMR-PLPN 266
Cdd:PRK00466 168 EGTPEHSSSAKSNL-IVDISKKIIEVY-----KQPENYDKPSIVPTI-------IRAGESYNVTPAKLYLHFDVRyAINN 234
M20_Dipept_like cd03893
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ...
8-377 6.27e-13

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: 69.66  E-value: 6.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   8 QRYAQLIELPTISSlVAEEDLSNRRLIELLATWLADFGFKTEIlaVEGSRNKYNLLATYGEGEGG--LLLAGHTDTVP-F 84
Cdd:cd03893    2 QTLAELVAIPSVSA-QPDRREELRRAAEWLADLLRRLGFTVEI--VDTSNGAPVVFAEFPGAPGAptVLLYGHYDVQPaG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  85 DEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQL--DLTQIKKPIRILATADEET--TMLGARTFAQHSHIRP 160
Cdd:cd03893   79 DEDGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALmqQGGDLPVNVKFIIEGEEESgsPSLDQLVEAHRDLLAA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 161 DCAIIGEPTSLKPIR-----AHKGHIGESVRITGRSG--HSS-------DP-AKGINAIELMHQSIGYLM---------- 215
Cdd:cd03893  159 DAIVISDSTWVGQEQptltyGLRGNANFDVEVKGLDHdlHSGlyggvvpDPmTALAQLLASLRDETGRILvpglydavre 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 216 -------KMRDEL-------REKYHNPLFQVTHPTMNFGNIHGG----DAINRICACCELQFDMRPLPNMAVQDLYAMVN 277
Cdd:cd03893  239 lpeeefrLDAGVLeeveiigGTTGSVAERLWTRPALTVLGIDGGfpgeGSKTVIPPRARAKISIRLVPGQDPEEASRLLE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 278 EHLK---PmleqYGDLIEIRHLHDGIPgYECEHSAQIVQVVEKLLGEKCDA-VNYCTEA---PFIQQL-----CPTLVLG 345
Cdd:cd03893  319 AHLEkhaP----SGAKVTVSYVEGGMP-WRSDPSDPAYQAAKDALRTAYGVePPLTREGgsiPFISVLqefpqAPVLLIG 393
                        410       420       430
                 ....*....|....*....|....*....|...
gi 493292681 346 PGSIE-QAHQPDEFLEMKYIEPTKELLTKLIYH 377
Cdd:cd03893  394 VGDPDdNAHSPNESLRLGNYKEGTQAEAALLYS 426
PRK08554 PRK08554
peptidase; Reviewed
41-187 7.14e-13

peptidase; Reviewed


Pssm-ID: 236285 [Multi-domain]  Cd Length: 438  Bit Score: 69.42  E-value: 7.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  41 LADFGFKTEILAVEGSrnkYNLLATYGEGEGGLLLAGHTDTVPFDEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVE 120
Cdd:PRK08554  37 LESWGIESELIEKDGY---YAVYGEIGEGKPKLLFMAHFDVVPVNPEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVML 113
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493292681 121 VVSQLDLTQIKKPIRILATADEETTMLGARTFAQHSH---IRPDCAIIGEPTSLKPI-RAHKGhIGESVRI 187
Cdd:PRK08554 114 ALKELSKEPLNGKVIFAFTGDEEIGGAMAMHIAEKLReegKLPKYMINADGIGMKPIiRRRKG-FGVTIRV 183
PRK08596 PRK08596
acetylornithine deacetylase; Validated
73-379 9.33e-13

acetylornithine deacetylase; Validated


Pssm-ID: 181495 [Multi-domain]  Cd Length: 421  Bit Score: 68.91  E-value: 9.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  73 LLLAGHTDTVPFDEGK-WRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRIL--ATADEETTMLGA 149
Cdd:PRK08596  80 LIINGHMDVAEVSADEaWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIfqSVIGEEVGEAGT 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 150 RTFAQHSHiRPDCAIIGEPTSLkpirahkgHI-GESVRITG--------------RSG--HSSDPAKGINAIELMHQSIG 212
Cdd:PRK08596 160 LQCCERGY-DADFAVVVDTSDL--------HMqGQGGVITGwitvkspqtfhdgtRRQmiHAGGGLFGASAIEKMMKIIQ 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 213 YLmkmrDELREKY----HNPLFQVTHPTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHL-------- 280
Cdd:PRK08596 231 SL----QELERHWavmkSYPGFPPGTNTINPAVIEGGRHAAFIADECRLWITVHFYPNETYEQVIKEIEEYIgkvaaadp 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 281 -------------KPMLEQYGDL---IEIRHLHDGIPGYECEHsaqivqvvEKLLGEK--CDAVNYCTEAPFIQQL-CPT 341
Cdd:PRK08596 307 wlrenppqfkwggESMIEDRGEIfpsLEIDSEHPAVKTLSSAH--------ESVLSKNaiLDMSTTVTDGGWFAEFgIPA 378
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 493292681 342 LVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLIYHFC 379
Cdd:PRK08596 379 VIYGPGTLEEAHSVNEKVEIEQLIEYTKVITAFIYEWC 416
PRK07338 PRK07338
hydrolase;
73-263 1.18e-12

hydrolase;


Pssm-ID: 235995 [Multi-domain]  Cd Length: 402  Bit Score: 68.45  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  73 LLLAGHTDTVpFDEGkwrfNPFQLTE--KAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPI--RILATADEETTMLG 148
Cdd:PRK07338  95 VLLTGHMDTV-FPAD----HPFQTLSwlDDGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLgyDVLINPDEEIGSPA 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 149 ART----FAQHSHirpdCAIIGEPT----SLKPIRAHKGHIgeSVRITGRSGHSS-DPAKGINAIEL---MHQSIGYLMK 216
Cdd:PRK07338 170 SAPllaeLARGKH----AALTYEPAlpdgTLAGARKGSGNF--TIVVTGRAAHAGrAFDEGRNAIVAaaeLALALHALNG 243
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 493292681 217 MRDELrekyhnplfqvthpTMNFGNIHGGDAINRICACCELQFDMRP 263
Cdd:PRK07338 244 QRDGV--------------TVNVAKIDGGGPLNVVPDNAVLRFNIRP 276
PRK07079 PRK07079
hypothetical protein; Provisional
6-113 2.55e-12

hypothetical protein; Provisional


Pssm-ID: 235928 [Multi-domain]  Cd Length: 469  Bit Score: 68.02  E-value: 2.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   6 FIQRYAQLIELPTISSLVAEEDLSNRRLIELLATWLADFGFKTEILAVEGSRNKYNLLATYGEGEG--GLLLAGHTDTVP 83
Cdd:PRK07079  19 FFADLARRVAYRTESQNPDRAPALRAYLTDEIAPALAALGFTCRIVDNPVAGGGPFLIAERIEDDAlpTVLIYGHGDVVR 98
                         90       100       110
                 ....*....|....*....|....*....|..
gi 493292681  84 FDEGKWR--FNPFQLTEKAGKLYGLGTADMKG 113
Cdd:PRK07079  99 GYDEQWRegLSPWTLTEEGDRWYGRGTADNKG 130
M20_peptT_like cd05683
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ...
61-375 3.59e-12

M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.


Pssm-ID: 349932 [Multi-domain]  Cd Length: 368  Bit Score: 67.09  E-value: 3.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  61 NLLATY-GEGEGG--LLLAGHTDTVpfDEGKWRFNPfqlTEKAGKLYGLGT----ADMKGFFAFVVEVVSQLDLTQIK-K 132
Cdd:cd05683   55 NLICTLkADKEEVpkILFTSHMDTV--TPGINVKPP---QIADGYIYSDGTtilgADDKAGIAAILEAIRVIKEKNIPhG 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 133 PIRILATADEETTMLGART-----------FAQHSHIRPDCAIIGEPTSLKPirahkghigeSVRITGRSGHSS-DPAKG 200
Cdd:cd05683  130 QIQFVITVGEESGLVGAKAldpelidadygYALDSEGDVGTIIVGAPTQDKI----------NAKIYGKTAHAGtSPEKG 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 201 INAIELMHQSIgylMKMrdelrekyhnPLFQVTH-PTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEH 279
Cdd:cd05683  200 ISAINIAAKAI---SNM----------KLGRIDEeTTANIGKFQGGTATNIVTDEVNIEAEARSLDEEKLDAQVKHMKET 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 280 LKPMLEQYGDLIEIRhLHDGIPGYECEHSAQIVQVVEKLLGE-----KCDAVNYCTEAPFIQQL-CPTLVLGPGsIEQAH 353
Cdd:cd05683  267 FETTAKEKGAHAEVE-VETSYPGFKINEDEEVVKLAKRAANNlgleiNTTYSGGGSDANIINGLgIPTVNLGIG-YENIH 344
                        330       340
                 ....*....|....*....|..
gi 493292681 354 QPDEFLEMKYIEPTKELLTKLI 375
Cdd:cd05683  345 TTNERIPIEDLYDTAVLVVEII 366
M20_dipept_like_CNDP cd05676
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ...
6-113 8.81e-12

M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine.


Pssm-ID: 349925 [Multi-domain]  Cd Length: 467  Bit Score: 66.09  E-value: 8.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   6 FIQRYAQLIELPTISSlvaeeDLSNR----RLIELLATWLADFGFKTEIlaVEGSRNKYN----------LLATYGE--G 69
Cdd:cd05676   12 FIERLREAVAIQSVSA-----DPEKRpeliRMMEWAAERLEKLGFKVEL--VDIGTQTLPdgeelplppvLLGRLGSdpS 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 493292681  70 EGGLLLAGHTDTVPFD-EGKWRFNPFQLTEKAGKLYGLGTADMKG 113
Cdd:cd05676   85 KKTVLIYGHLDVQPAKlEDGWDTDPFELTEKDGKLYGRGSTDDKG 129
M20_AcylaseI_like cd05646
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ...
73-287 2.08e-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: 64.60  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  73 LLLAGHTDTVPFDEGKWRFNPFQLTEKA-GKLYGLGTADMKGFFAFVVEVVSQLDLT--QIKKPIRILATADEET-TMLG 148
Cdd:cd05646   67 ILLNSHTDVVPVFEEKWTHDPFSAHKDEdGNIYARGAQDMKCVGIQYLEAIRRLKASgfKPKRTIHLSFVPDEEIgGHDG 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 149 ARTFAQHSHIR---PDCAI---IGEPTSlkpirAHKGHIGE------SVRITGRSGHSSDPAKGiNAIELMHQSIGYLMK 216
Cdd:cd05646  147 MEKFVKTEEFKklnVGFALdegLASPTE-----EYRVFYGErspwwvVITAPGTPGHGSKLLEN-TAGEKLRKVIESIME 220
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493292681 217 MRDELREKYHN----PLFQVThpTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQY 287
Cdd:cd05646  221 FRESQKQRLKSnpnlTLGDVT--TVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGRGV 293
PRK07205 PRK07205
hypothetical protein; Provisional
43-144 3.45e-10

hypothetical protein; Provisional


Pssm-ID: 235965 [Multi-domain]  Cd Length: 444  Bit Score: 61.25  E-value: 3.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  43 DFGFKTEIlavegSRNKYNLLATYGEGEGGLLLAGHTDTVPF-DEGKWRFNPFQLTEKAGKLYGLGTADMKG-FFAFVVE 120
Cdd:PRK07205  53 GLGFKTYL-----DPKGYYGYAEIGQGEELLAILCHLDVVPEgDLSDWQTPPFEAVEKDGCLFGRGTQDDKGpSMAALYA 127
                         90       100
                 ....*....|....*....|....*
gi 493292681 121 VVSQLDL-TQIKKPIRILATADEET 144
Cdd:PRK07205 128 VKALLDAgVQFNKRIRFIFGTDEET 152
M20_dipept_Sso-CP2 cd05681
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ...
13-136 6.46e-09

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: 57.35  E-value: 6.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  13 LIELPTISslvaeedLSNRRLIE---LLATWLADFGFKTEILavEGSRNKYnLLATYGEG-EGGLLLAGHTDTVPFDE-G 87
Cdd:cd05681    8 LLKIPSVS-------AQGRGIPEtadFLKEFLRRLGAEVEIF--ETDGNPI-VYAEFNSGdAKTLLFYNHYDVQPAEPlE 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 493292681  88 KWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRI 136
Cdd:cd05681   78 LWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNI 126
Ac-peptdase-euk TIGR01880
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ...
4-285 9.26e-09

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: 56.72  E-value: 9.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681    4 IPFIQRYAQLIELPTISSLVAEEDlsnrrlIELLATWLadfGFKTEILAVegsrnkynllatygegegglLLAGHTDTVP 83
Cdd:TIGR01880  34 VDFLIKQADELGLARKTIEFVPGK------PVVVLTWP---GSNPELPSI--------------------LLNSHTDVVP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   84 FDEGKWRFNPFQ-LTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLT--QIKKPIRILATADEET-TMLGARTFAQHSHIR 159
Cdd:TIGR01880  85 VFREHWTHPPFSaFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASgfKFKRTIHISFVPDEEIgGHDGMEKFAKTDEFK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  160 P-------DCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGiNAIELMHQSIGYLMKMRDE----LREKYHNP 228
Cdd:TIGR01880 165 AlnlgfalDEGLASPDDVYRVFYAERVPWWVVVTAPGNPGHGSKLMEN-TAMEKLEKSVESIRRFRESqfqlLQSNPDLA 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 493292681  229 LFQVThpTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLE 285
Cdd:TIGR01880 244 IGDVT--SVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADAGE 298
PRK07473 PRK07473
M20/M25/M40 family metallo-hydrolase;
68-256 2.07e-08

M20/M25/M40 family metallo-hydrolase;


Pssm-ID: 168961 [Multi-domain]  Cd Length: 376  Bit Score: 55.56  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  68 EGEGGLLLAGHTDTV-PFdeGKWRFNPFQltEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKK--PIRILATADEET 144
Cdd:PRK07473  73 QGEPGILIAGHMDTVhPV--GTLEKLPWR--REGNKCYGPGILDMKGGNYLALEAIRQLARAGITTplPITVLFTPDEEV 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 145 TMLGARTFAQHSHIRPDCAIIGEPTslkpiRAHKGHI-GE------SVRITGRSGHS-SDPAKGINAIELMHQSIGYLMK 216
Cdd:PRK07473 149 GTPSTRDLIEAEAARNKYVLVPEPG-----RPDNGVVtGRyaiarfNLEATGRPSHAgATLSEGRSAIREMARQILAIDA 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 493292681 217 MRDElrekyhnplfqvtHPTMNFGNIHGGDAINRICACCE 256
Cdd:PRK07473 224 MTTE-------------DCTFSVGIVHGGQWVNCVATTCT 250
PRK07318 PRK07318
dipeptidase PepV; Reviewed
45-144 6.36e-08

dipeptidase PepV; Reviewed


Pssm-ID: 235988 [Multi-domain]  Cd Length: 466  Bit Score: 54.08  E-value: 6.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  45 GFKTEilAVEGsrnkYNLLATYGEGEGGLLLAGHTDTVPFDEGkWRFNPFQLTEKAGKLYGLGTADMKG-----FFAfvV 119
Cdd:PRK07318  60 GFKTK--NVDN----YAGHIEYGEGEEVLGILGHLDVVPAGDG-WDTDPYEPVIKDGKIYARGTSDDKGptmaaYYA--L 130
                         90       100
                 ....*....|....*....|....*
gi 493292681 120 EVVSQLDLTqIKKPIRILATADEET 144
Cdd:PRK07318 131 KIIKELGLP-LSKKVRFIVGTDEES 154
PRK07907 PRK07907
hypothetical protein; Provisional
2-113 4.67e-07

hypothetical protein; Provisional


Pssm-ID: 236127 [Multi-domain]  Cd Length: 449  Bit Score: 51.44  E-value: 4.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   2 KQIPFIQR-YAQLIELPTISSLVAEEDlSNRRLIELLATWLADFGF-KTEILAVEGSRNkynLLATYgEGEGG---LLLA 76
Cdd:PRK07907  15 ELLPRVRAdLEELVRIPSVAADPFRRE-EVARSAEWVADLLREAGFdDVRVVSADGAPA---VIGTR-PAPPGaptVLLY 89
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 493292681  77 GHTDTVP-FDEGKWRFNPFQLTEKAGKLYGLGTADMKG 113
Cdd:PRK07907  90 AHHDVQPpGDPDAWDSPPFELTERDGRLYGRGAADDKG 127
M20_dipept_like cd05679
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ...
31-113 2.67e-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: 349928 [Multi-domain]  Cd Length: 448  Bit Score: 49.03  E-value: 2.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  31 RRLIELLATWLADFGFKTEILAVEGSRNKYNLLATYGEGEGG--LLLAGHTDTVPFDEGKWR--FNPFQLTEKAGKLYGL 106
Cdd:cd05679   31 AYLDQEMRPRFERLGFTVHIHDNPVAGRAPFLIAERIEDPSLptLLIYGHGDVVPGYEGRWRdgRDPWTVTVWGERWYGR 110

                 ....*..
gi 493292681 107 GTADMKG 113
Cdd:cd05679  111 GTADNKG 117
M20_Acy1L2-like cd09849
M20 Peptidase aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ...
155-370 2.02e-05

M20 Peptidase aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase)-like subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli , to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Aminoacylase 1 (ACY1) proteins 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 the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).


Pssm-ID: 349947 [Multi-domain]  Cd Length: 389  Bit Score: 46.32  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 155 HSHIRPDCAIIGEPTSlkpirahKGHIGESVRITGRSGHS-SDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLfqvt 233
Cdd:cd09849  171 HALDLGEDKALINPES-------NGFIGKKVKFTGKESHAgSAPFSGINALNAATLAINNVNAQRETFKESDKVRF---- 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 234 HPTMnfgnIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHlhdgIPGYE--CEHSAQI 311
Cdd:cd09849  240 HPII----TKGGDIVNVVPADVRVESYVRARSIDYMKEANSKVNRALRASAMAVGAEVEIKE----LPGYLpiLQDRDLD 311
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 312 VQVVEKL--LGEKCD-----AVNYCTEAPFIQQLCPTLVLGPGSIEQAHQPDEFL----EMKYIEPTKEL 370
Cdd:cd09849  312 NFLKENLqdLGLIERiidggDFTGSFDFGDLSHLMPTLHPMFGGVEGALHTRDFKivdpEFAYILPAKAL 381
PRK06446 PRK06446
hypothetical protein; Provisional
7-143 2.05e-05

hypothetical protein; Provisional


Pssm-ID: 235802 [Multi-domain]  Cd Length: 436  Bit Score: 46.29  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   7 IQRYAQLIELPTISSlvaeedlsNRRLIELLATWLADF----GFKTEILAVEGsrNKYnllaTYGEGEGG----LLLAGH 78
Cdd:PRK06446   5 LYTLIEFLKKPSISA--------TGEGIEETANYLKDTmeklGIKANIERTKG--HPV----VYGEINVGakktLLIYNH 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493292681  79 TDTVPFDE-GKWRFNPFQLTEKAGKLYGLGTADMKG-FFAFVVEVVSQLDLTQIKKPIRILATADEE 143
Cdd:PRK06446  71 YDVQPVDPlSEWKRDPFSATIENGRIYARGASDNKGtLMARLFAIKHLIDKHKLNVNVKFLYEGEEE 137
M20_dipept_like cd05680
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ...
7-122 3.25e-05

uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.


Pssm-ID: 349929 [Multi-domain]  Cd Length: 437  Bit Score: 45.76  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681   7 IQRYAQLIELPTISSLVA-EEDLsnRRLIELLATWLADFGF-KTEILAVEGsrnkynLLATYGEGEGG-----LLLAGHT 79
Cdd:cd05680    1 LEELFELLRIPSVSADPAhKGDV--RRAAEWLADKLTEAGFeHTEVLPTGG------HPLVYAEWLGApgaptVLVYGHY 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 493292681  80 DTVPFD-EGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVV 122
Cdd:cd05680   73 DVQPPDpLELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAV 116
M20_ArgE_RocB cd05654
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ...
58-227 4.33e-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: 45.41  E-value: 4.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  58 NKYNLLATY-GEGEG--GLLLAGHTDTVPFDE-GKWR---FNPFQLTE-----------------KAGK-LYGLGTADMK 112
Cdd:cd05654   56 GRRNVTALVkGKKPSkrTIILISHFDTVGIEDyGELKdiaFDPDELTKafseyveeldeevredlLSGEwLFGRGTMDMK 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 113 GFFAFVVEVVSQL-DLTQIKKPIRILATADEETT---MLGART----FAQHSHIRPDCAIIGEPTSLK----PIRA-HKG 179
Cdd:cd05654  136 SGLAVHLALLEQAsEDEDFDGNLLLMAVPDEEVNsrgMRAAVPalleLKKKHDLEYKLAINSEPIFPQydgdQTRYiYTG 215
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 493292681 180 HIGE---SVRITGRSGHSSDPAKGINAiELMHQSIGYLMKMRDELREKYHN 227
Cdd:cd05654  216 SIGKilpGFLCYGKETHVGEPFAGINA-NLMASEITARLELNADLCEKVEG 265
M20_dipept_like_DUG2_type cd05677
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ...
11-113 8.05e-05

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: 44.26  E-value: 8.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  11 AQLIELPTISSLVAEED-LSNRRLIELLATWLADFGFKTEILAVEGSRNKYNLLATYG-----EGEGGLLLAGHTDTVPF 84
Cdd:cd05677    6 SEFIAFQTVSQSPTTENaEDSRRCAIFLRQLFKKLGATNCLLLPSGPGTNPIVLATFSgnssdAKRKRILFYGHYDVIPA 85
                         90       100       110
                 ....*....|....*....|....*....|
gi 493292681  85 DE-GKWRFNPFQLTEKAGKLYGLGTADMKG 113
Cdd:cd05677   86 GEtDGWDTDPFTLTCENGYLYGRGVSDNKG 115
M20_Acy1 cd03886
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ...
185-333 8.91e-05

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: 44.13  E-value: 8.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 185 VRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDelREkyhnplFQVTHP-TMNFGNIHGGDAINRICACCELQFDMRP 263
Cdd:cd03886  176 ITVKGKGGHGASPHLGVDPIVAAAQIVLALQTVVS--RE------LDPLEPaVVTVGKFHAGTAFNVIPDTAVLEGTIRT 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 264 LPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGIPGY-ECEHSAQIVQVVEKLLGEKC-----------DAVNYCTE 331
Cdd:cd03886  248 FDPEVREALEARIKRLAEGIAAAYGATVELEYGYGYPAVInDPELTELVREAAKELLGEEAvvepepvmgseDFAYYLEK 327

                 ..
gi 493292681 332 AP 333
Cdd:cd03886  328 VP 329
PRK06156 PRK06156
dipeptidase;
78-155 2.11e-04

dipeptidase;


Pssm-ID: 235720 [Multi-domain]  Cd Length: 520  Bit Score: 43.03  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  78 HTDTVPFDEGKW-----RFNPFQLTEKAGKLYGLGTADMKGFFA---FVVEVV--SQLDLtqiKKPIRILATADEETTML 147
Cdd:PRK06156 117 HADVVPANPELWvldgtRLDPFKVTLVGDRLYGRGTEDDKGAIVtalYAMKAIkdSGLPL---ARRIELLVYTTEETDGD 193

                 ....*...
gi 493292681 148 GARTFAQH 155
Cdd:PRK06156 194 PLKYYLER 201
PRK08201 PRK08201
dipeptidase;
12-136 6.08e-04

dipeptidase;


Pssm-ID: 169276 [Multi-domain]  Cd Length: 456  Bit Score: 41.65  E-value: 6.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681  12 QLIELPTISSLvAEEDLSNRRLIELLATWLADFGF-KTEILAVEGSRNKYnllATYGEGEGG--LLLAGHTDTVPFDEGK 88
Cdd:PRK08201  22 EFLRIPSISAL-SEHKEDVRKAAEWLAGALEKAGLeHVEIMETAGHPIVY---ADWLHAPGKptVLIYGHYDVQPVDPLN 97
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 493292681  89 -WRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRI 136
Cdd:PRK08201  98 lWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNV 146
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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