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Conserved domains on  [gi|1631970281|ref|NP_001357178|]
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cytosolic non-specific dipeptidase isoform 1 [Homo sapiens]

Protein Classification

M20 family dipeptidase( domain architecture ID 10145395)

M20 family dipeptidase catalyzes the hydrolysis of dipeptides, similar to human cytosolic non-specific dipeptidase which hydrolyzes variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
M20_dipept_like_CNDP cd05676
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ...
7-473 0e+00

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: 976.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281   7 LFKYIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLGGSVELVDIGKQKLPDGSEIPLPPILLGRLG 86
Cdd:cd05676     1 VFKYIDEHQDEFIERLREAVAIQSVSADPEKRPELIRMMEWAAERLEKLGFKVELVDIGTQTLPDGEELPLPPVLLGRLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  87 SDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGME 166
Cdd:cd05676    81 SDPSKKTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEGME 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 167 ESGSEGLDELIFARKDTFFKDVDYVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILL 246
Cdd:cd05676   161 ESGSEGLDELIEARKDTFFSDVDYVCISDNYWLGKKKPCLTYGLRGICYFFIEVEGPNKDLHSGVFGGSVHEPMTDLIAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 247 MGSLVDKRGNILIPGINEAVAAVTEEEHKLYDDIDFDIEEFAKDVGAQILLHSHKKDILMHRWRYPSLSLHGIEGAFSGS 326
Cdd:cd05676   241 MSSLVDSDGKILIPGIYDAVAPLTEEEWELYEKIDFDMEEYREDIGVRRLLYDNKEELLMHRWRYPSLSIHGIEGAFSGP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 327 GAKTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKKFAELRSPNEFKVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFG 406
Cdd:cd05676   321 GAKTVIPAKVIGKFSIRLVPNMDPEVVEKQVTDYLEKVFAELKSPNKLKVYMGHGGKPWVADPDHPNYKAARKATKRVFG 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631970281 407 VEPDLTREGGSIPVTLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRYNYIEGTKMLAAYLYEVSQL 473
Cdd:cd05676   401 VEPDLTREGGSIPITLTFQEATGKNVMLLPIGAADDGAHSQNEKINRRNYIEGTKLLAAYFHELSKL 467
 
Name Accession Description Interval E-value
M20_dipept_like_CNDP cd05676
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ...
7-473 0e+00

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: 976.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281   7 LFKYIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLGGSVELVDIGKQKLPDGSEIPLPPILLGRLG 86
Cdd:cd05676     1 VFKYIDEHQDEFIERLREAVAIQSVSADPEKRPELIRMMEWAAERLEKLGFKVELVDIGTQTLPDGEELPLPPVLLGRLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  87 SDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGME 166
Cdd:cd05676    81 SDPSKKTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEGME 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 167 ESGSEGLDELIFARKDTFFKDVDYVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILL 246
Cdd:cd05676   161 ESGSEGLDELIEARKDTFFSDVDYVCISDNYWLGKKKPCLTYGLRGICYFFIEVEGPNKDLHSGVFGGSVHEPMTDLIAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 247 MGSLVDKRGNILIPGINEAVAAVTEEEHKLYDDIDFDIEEFAKDVGAQILLHSHKKDILMHRWRYPSLSLHGIEGAFSGS 326
Cdd:cd05676   241 MSSLVDSDGKILIPGIYDAVAPLTEEEWELYEKIDFDMEEYREDIGVRRLLYDNKEELLMHRWRYPSLSIHGIEGAFSGP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 327 GAKTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKKFAELRSPNEFKVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFG 406
Cdd:cd05676   321 GAKTVIPAKVIGKFSIRLVPNMDPEVVEKQVTDYLEKVFAELKSPNKLKVYMGHGGKPWVADPDHPNYKAARKATKRVFG 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631970281 407 VEPDLTREGGSIPVTLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRYNYIEGTKMLAAYLYEVSQL 473
Cdd:cd05676   401 VEPDLTREGGSIPITLTFQEATGKNVMLLPIGAADDGAHSQNEKINRRNYIEGTKLLAAYFHELSKL 467
PRK08201 PRK08201
dipeptidase;
10-473 1.24e-104

dipeptidase;


Pssm-ID: 169276 [Multi-domain]  Cd Length: 456  Bit Score: 319.38  E-value: 1.24e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  10 YIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLG-GSVELVDIGKQklpdgseiplpPILLGRLGSD 88
Cdd:PRK08201    8 YLRERREAHLEELKEFLRIPSISALSEHKEDVRKAAEWLAGALEKAGlEHVEIMETAGH-----------PIVYADWLHA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  89 PQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEES 168
Cdd:PRK08201   77 PGKPTVLIYGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIEGEEEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 169 GSEGLDELIFARKDTFFKDVdyVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMG 248
Cdd:PRK08201  157 GSPNLDSFVEEEKDKLAADV--VLISDTTLLGPGKPAICYGLRGLAALEIDVRGAKGDLHSGLYGGAVPNALHALVQLLA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 249 SLVDKRGNILIPGINEAVAAVTEEEHKLYDDIDFDIEEFAKDVGAQILLHSHKKDILMHRWRYPSLSLHGIEGAFSGSGA 328
Cdd:PRK08201  235 SLHDEHGTVAVEGFYDGVRPLTPEEREEFAALGFDEEKLKRELGVDELFGEEGYTALERTWARPTLELNGVYGGFQGEGT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 329 KTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLtkkfaELRSPNEFKVYM--GHGGKPWVSDFSHPHYLAGRRAMKTVFG 406
Cdd:PRK08201  315 KTVIPAEAHAKITCRLVPDQDPQEILDLIEAHL-----QAHTPAGVRVTIrrFDKGPAFVAPIDHPAIQAAARAYEAVYG 389
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631970281 407 VEPDLTREGGSIPVTLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRYNYIEGTKMLAAYLYEVSQL 473
Cdd:PRK08201  390 TEAAFTRMGGSIPVVETFSSQLHIPIVLMGFGLPSENFHAPNEHFHLENFDKGLRTLVEYWHQLAEG 456
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
7-469 6.49e-69

Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism];


Pssm-ID: 223697 [Multi-domain]  Cd Length: 409  Bit Score: 225.43  E-value: 6.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281   7 LFKYIDENQDRYIKKLAKWVAIQSVSAwpekrGEIRRMMEVAAADVKQLGGSVELVDIGkqklpdgsEIPLPPILLGRLG 86
Cdd:COG0624     4 LLEVSLDLLDDILELLKELVRIPSVSA-----GEEAEAAELLAEWLEELGFEVEEDEVG--------PGPGRPNLVARLG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  87 SDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGME 166
Cdd:COG0624    71 GGDGGPTLLLGGHLDVVPAGGGEDWTTDPFEPTIKDGKLYGRGAADMKGGLAAALYALSALKAAGGELPGDVRLLFTADE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 167 ESGSEGLDELIFARKDTFFKDVDYVCISDNYWLGKKKPCITYGLRGICYFFIEVEcSNKDLHSGVYGGSVHEAMTDLILL 246
Cdd:COG0624   151 ESGGAGGKAYLEEGEEALGIRPDYEIVGEPTLESEGGDIIVVGHKGSLWLEVTVK-GKAGHASTTPPDLGRNPIHAAIEA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 247 MGSLVDKRGNILIPGINEavaavteeehklyddidfdieEFAKDVGaqillhshkkdilmhrwrypsLSLHGIEGAFSGS 326
Cdd:COG0624   230 LAELIEELGDLAGEGFDG---------------------PLGLNVG---------------------LILAGPGASVNGG 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 327 GAKTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKKFAELRSpnEFKVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFG 406
Cdd:COG0624   268 DKVNVIPGEAEATVDIRLLPGEDLDDVLEELEAELRAIAPKEGV--EYEIEPGLGEPPLPVPGDSPLVAALAEAAEELLG 345
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631970281 407 VEPdLTREGGsIPVTLTFQEATGKNVMLLPVGSaDDGAHSQNEKLNRYNYIEGTKMLAAYLYE 469
Cdd:COG0624   346 LPP-EVSTGG-GTHDARFFARLGIPAVIFGPGD-IGLAHQPNEYVELEDLVKGAKVLARLLYE 405
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
95-469 5.98e-42

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: 396225 [Multi-domain]  Cd Length: 315  Bit Score: 151.35  E-value: 5.98e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  95 CIYGHLDVQPAALEDGWdsePFTLVErDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEiPVNVRFCLEGMEESGSEGLD 174
Cdd:pfam01546   1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGGMGGAR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 175 ELIFARKDTFFKdVDYV---CISD-NYWLGKKKPCITYGLRGICYFFIEVECsnKDLHSGvYGGSVHEAMTDLILLMGSL 250
Cdd:pfam01546  76 ALIEDGLLEREK-VDAVfglHIGEpTLLEGGIAIGVVTGHRGSLRFRVTVKG--KGGHAS-TPHLGVNAIVAAARLILAL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 251 VDKRGNILIPGiNEAVAAVTeeehklyddidfdieefakdvgaqillhshkkdilmhrwrypslSLHGIEGAFsgsgakT 330
Cdd:pfam01546 152 QDIVSRNVDPL-DPAVVTVG--------------------------------------------NITGIPGGV------N 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 331 VIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKKFAELRSPNEFKVymGHGGKPWVSDfSHPHYLAGRRAMKTVFGVEPD 410
Cdd:pfam01546 181 VIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEY--VEGGAPPLVN-DSPLVAALREAAKELFGLKVE 257
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631970281 411 LTREGGSIpvtlT-----FQEATGKNVMLLpvGSADDGAHSQNEKLNRYNYIEGTKMLAAYLYE 469
Cdd:pfam01546 258 LIVSGSMG----GtdaafFLLGVPPTVVFF--GPGSGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
DapE-ArgE TIGR01910
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ...
19-461 1.30e-25

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: 107.87  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  19 IKKLAKWVAIQSVSAWPEKRGEIRRMMEvaaADVKQLGGSVELVDIgkqklPDGSEIPLPPILLGRLGSDPQKkTVCIYG 98
Cdd:TIGR01910   1 VELLKDLISIPSVNPPGGNEETIANYIK---DLLREFGFSTDVIEI-----TDDRLKVLGKVVVKEPGNGNEK-SLIFNG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  99 HLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSEGLDELIf 178
Cdd:TIGR01910  72 HYDVVPAGDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLYLL- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 179 arKDTFFKDVDYVCISDNYWLGKkkpcITYGLRGICYFfievecsnkdlHSGVYGGSVHEAMTDLillmGSLVDKRGNIL 258
Cdd:TIGR01910 151 --QRGYFKDADGVLIPEPSGGDN----IVIGHKGSIWF-----------KLRVKGKQAHASFPQF----GVNAIMKLAKL 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 259 IPGINEAvaavteeEHKLYDDIDFDIEefakdvgaqillhshkkdilMHRWRYPSlslhgieGAFSGSGAKTVIPRKVVG 338
Cdd:TIGR01910 210 ITELNEL-------EEHIYARNSYGFI--------------------PGPITFNP-------GVIKGGDWVNSVPDYCEF 255
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 339 KFSIRLVPNMTPEVVGEQVTSYLTKKFAELRSPNEFKVYMGHGGKPWVSDfSHPHYLAGRRAMKTVFGVEPdltrEGGSI 418
Cdd:TIGR01910 256 SIDVRIIPEENLDEVKQIIEDVVKALSKSDGWLYENEPVVKWSGPNETPP-DSRLVKALEAIIKKVRGIEP----EVLVS 330
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1631970281 419 PVTLTFQEATGKNVMLLPVGSADDG-AHSQNEKLNRYNYIEGTK 461
Cdd:TIGR01910 331 TGGTDARFLRKAGIPSIVYGPGDLEtAHQVNEYISIKNLVESTK 374
 
Name Accession Description Interval E-value
M20_dipept_like_CNDP cd05676
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ...
7-473 0e+00

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: 976.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281   7 LFKYIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLGGSVELVDIGKQKLPDGSEIPLPPILLGRLG 86
Cdd:cd05676     1 VFKYIDEHQDEFIERLREAVAIQSVSADPEKRPELIRMMEWAAERLEKLGFKVELVDIGTQTLPDGEELPLPPVLLGRLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  87 SDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGME 166
Cdd:cd05676    81 SDPSKKTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEGME 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 167 ESGSEGLDELIFARKDTFFKDVDYVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILL 246
Cdd:cd05676   161 ESGSEGLDELIEARKDTFFSDVDYVCISDNYWLGKKKPCLTYGLRGICYFFIEVEGPNKDLHSGVFGGSVHEPMTDLIAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 247 MGSLVDKRGNILIPGINEAVAAVTEEEHKLYDDIDFDIEEFAKDVGAQILLHSHKKDILMHRWRYPSLSLHGIEGAFSGS 326
Cdd:cd05676   241 MSSLVDSDGKILIPGIYDAVAPLTEEEWELYEKIDFDMEEYREDIGVRRLLYDNKEELLMHRWRYPSLSIHGIEGAFSGP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 327 GAKTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKKFAELRSPNEFKVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFG 406
Cdd:cd05676   321 GAKTVIPAKVIGKFSIRLVPNMDPEVVEKQVTDYLEKVFAELKSPNKLKVYMGHGGKPWVADPDHPNYKAARKATKRVFG 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631970281 407 VEPDLTREGGSIPVTLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRYNYIEGTKMLAAYLYEVSQL 473
Cdd:cd05676   401 VEPDLTREGGSIPITLTFQEATGKNVMLLPIGAADDGAHSQNEKINRRNYIEGTKLLAAYFHELSKL 467
M20_Dipept_like cd03893
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ...
20-469 0e+00

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: 585.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  20 KKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLGGSVELVDIGkqklpdgseiPLPPILLGRLGSDPQKKTVCIYGH 99
Cdd:cd03893     2 QTLAELVAIPSVSAQPDRREELRRAAEWLADLLRRLGFTVEIVDTS----------NGAPVVFAEFPGAPGAPTVLLYGH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 100 LDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSEGLDELIFA 179
Cdd:cd03893    72 YDVQPAGDEDGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEESGSPSLDQLVEA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 180 RKDtfFKDVDYVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMGSLVDKRGNILI 259
Cdd:cd03893   152 HRD--LLAADAIVISDSTWVGQEQPTLTYGLRGNANFDVEVKGLDHDLHSGLYGGVVPDPMTALAQLLASLRDETGRILV 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 260 PGINEAVAAVTEEEHKLYDDIDfdiEEFAKDVGAqillhshKKDILMHRWRYPSLSLHGIEGAFSGSGAKTVIPRKVVGK 339
Cdd:cd03893   230 PGLYDAVRELPEEEFRLDAGVL---EEVEIIGGT-------TGSVAERLWTRPALTVLGIDGGFPGEGSKTVIPPRARAK 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 340 FSIRLVPNMTPEVVGEQVTSYLTKKFAelrSPNEFKVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFGVEPDLTREGGSIP 419
Cdd:cd03893   300 ISIRLVPGQDPEEASRLLEAHLEKHAP---SGAKVTVSYVEGGMPWRSDPSDPAYQAAKDALRTAYGVEPPLTREGGSIP 376
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1631970281 420 VTLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRYNYIEGTKMLAAYLYE 469
Cdd:cd03893   377 FISVLQEFPQAPVLLIGVGDPDDNAHSPNESLRLGNYKEGTQAEAALLYS 426
M20_dipept_like cd05680
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ...
22-470 5.38e-127

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: 375.88  E-value: 5.38e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  22 LAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLGGS-VELVDigkqklPDGSeiplpPILLGRLGSDPQKKTVCIYGHL 100
Cdd:cd05680     4 LFELLRIPSVSADPAHKGDVRRAAEWLADKLTEAGFEhTEVLP------TGGH-----PLVYAEWLGAPGAPTVLVYGHY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 101 DVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSEGLDELIFAR 180
Cdd:cd05680    73 DVQPPDPLELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIGSPSLPAFLEEN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 181 KDTFfkDVDYVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMGSLVDKRGNILIP 260
Cdd:cd05680   153 AERL--AADVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPNRDLHSGSYGGAVPNPANALARLLASLHDEDGRVAIP 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 261 GINEAVAAVTEEEHKLYDDIDFDIEEFAKDVGAQILLHSHKKDILMHRWRYPSLSLHGIEGAFSGSGAKTVIPRKVVGKF 340
Cdd:cd05680   231 GFYDDVRPLTDAEREAWAALPFDEAAFKASLGVPALGGEAGYTTLERLWARPTLDVNGIWGGYQGEGSKTVIPSKAHAKI 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 341 SIRLVPNMTPEVVGEQVTSYLTkkfAELRSPNEFKVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFGVEPDLTREGGSIPV 420
Cdd:cd05680   311 SMRLVPGQDPDAIADLLEAHLR---AHAPPGVTLSVKPLHGGRPYLVPTDHPALQAAERALEEAFGKPPVFVREGGSIPI 387
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1631970281 421 TLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRYNYIEGTKMLAAYLYEV 470
Cdd:cd05680   388 VALFEKVLGIPTVLMGFGLPDDAIHAPNEKFRLECFHKGIEAIAHLLARL 437
M20_dipept_like_DUG2_type cd05677
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ...
22-463 9.67e-111

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: 334.31  E-value: 9.67e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  22 LAKWVAIQSVSAWPEKR--GEIRRmmevAAADVKQLggsveLVDIG---KQKLPDGSEIPlpPILLGRL---GSDPQKKT 93
Cdd:cd05677     5 LSEFIAFQTVSQSPTTEnaEDSRR----CAIFLRQL-----FKKLGatnCLLLPSGPGTN--PIVLATFsgnSSDAKRKR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  94 VCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGP-VAGWINALEAYQKtgQEIPVNVRFCLEGMEESGSEG 172
Cdd:cd05677    74 ILFYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGPlLAAIYAVAELFQE--GELDNDVVFLIEGEEESGSPG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 173 LDELIFARKDtFFKDVDYVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMGSLVD 252
Cdd:cd05677   152 FKEVLRKNKE-LIGDIDWILLSNSYWLDDNIPCLNYGLRGVIHATIVVSSDKPDLHSGVDGGVLREPTADLIKLLSKLQD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 253 KRGNILIPGINEAVAAVTEEEHKLYDDIdfdIEEFAKDvgaqillHSHKKDILMHRWRYPSLSLHGIEgaFSGSGAKTVI 332
Cdd:cd05677   231 PDGRILIPHFYDPVKPLTEAERARFTAI---AETALIH-------EDTTVDSLIAKWRKPSLTVHTVK--VSGPGNTTVI 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 333 PRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKKFAELRSPNEFKVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFGVEPDLT 412
Cdd:cd05677   299 PKSASASVSIRLVPDQDLDVIKQDLTDYIQSCFAELKSQNHLDIEVLNEAEPWLGDPDNPAYQILREAVTAAWGVEPLYI 378
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1631970281 413 REGGSIPVTLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRYNYIEGTKML 463
Cdd:cd05677   379 REGGSIPTIRFLEKEFNAPAVQLPCGQSSDNAHLDNERLRIKNLYKMREIL 429
PRK08201 PRK08201
dipeptidase;
10-473 1.24e-104

dipeptidase;


Pssm-ID: 169276 [Multi-domain]  Cd Length: 456  Bit Score: 319.38  E-value: 1.24e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  10 YIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLG-GSVELVDIGKQklpdgseiplpPILLGRLGSD 88
Cdd:PRK08201    8 YLRERREAHLEELKEFLRIPSISALSEHKEDVRKAAEWLAGALEKAGlEHVEIMETAGH-----------PIVYADWLHA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  89 PQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEES 168
Cdd:PRK08201   77 PGKPTVLIYGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIEGEEEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 169 GSEGLDELIFARKDTFFKDVdyVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMG 248
Cdd:PRK08201  157 GSPNLDSFVEEEKDKLAADV--VLISDTTLLGPGKPAICYGLRGLAALEIDVRGAKGDLHSGLYGGAVPNALHALVQLLA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 249 SLVDKRGNILIPGINEAVAAVTEEEHKLYDDIDFDIEEFAKDVGAQILLHSHKKDILMHRWRYPSLSLHGIEGAFSGSGA 328
Cdd:PRK08201  235 SLHDEHGTVAVEGFYDGVRPLTPEEREEFAALGFDEEKLKRELGVDELFGEEGYTALERTWARPTLELNGVYGGFQGEGT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 329 KTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLtkkfaELRSPNEFKVYM--GHGGKPWVSDFSHPHYLAGRRAMKTVFG 406
Cdd:PRK08201  315 KTVIPAEAHAKITCRLVPDQDPQEILDLIEAHL-----QAHTPAGVRVTIrrFDKGPAFVAPIDHPAIQAAARAYEAVYG 389
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631970281 407 VEPDLTREGGSIPVTLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRYNYIEGTKMLAAYLYEVSQL 473
Cdd:PRK08201  390 TEAAFTRMGGSIPVVETFSSQLHIPIVLMGFGLPSENFHAPNEHFHLENFDKGLRTLVEYWHQLAEG 456
M20_dipept_Sso-CP2 cd05681
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ...
18-467 1.30e-86

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: 271.91  E-value: 1.30e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  18 YIKKLAKWVAIQSVSAwpeKRGEIRRMMEVAAADVKQLGGSVELVdigkqklpdgsEIPLPPILLGRLGSDpQKKTVCIY 97
Cdd:cd05681     1 YLEDLRDLLKIPSVSA---QGRGIPETADFLKEFLRRLGAEVEIF-----------ETDGNPIVYAEFNSG-DAKTLLFY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  98 GHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSEGLDELI 177
Cdd:cd05681    66 NHYDVQPAEPLELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSPNLEKFV 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 178 FARKDTFFKDvdyVCIsdnyWLG-----KKKPCITYGLRGICYFFIEVECSNKDLHSGvYGGSVHEAMTDLILLMGSLVD 252
Cdd:cd05681   146 AEHADLLKAD---GCI----WEGggknpKGRPQISLGVKGIVYVELRVKTADFDLHSS-YGAIVENPAWRLVQALNSLRD 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 253 KRGNILIPGINEAVAAVTEEEHKLYDDIDFDIEEFAKDVGAQILLHSHKKDILMHRWRYPSLSLHGIEGAFSGSGAKTVI 332
Cdd:cd05681   218 EDGRVLIPGFYDDVRPLSEAERALIDTYDFDPEELRKTYGLKRPLQVEGKDPLRALFTEPTCNINGIYSGYTGEGSKTIL 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 333 PRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKkfaelrspNEF---KVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFGVEP 409
Cdd:cd05681   298 PSEAFAKLDFRLVPDQDPAKILSLLRKHLDK--------NGFddiEIHDLLGEKPFRTDPDAPFVQAVIESAKEVYGQDP 369
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1631970281 410 DLTRE-GGSIPVTlTFQEATGKNVMLLPVGSADDGAHSQNEKLNRYNYIEGTKMLAAYL 467
Cdd:cd05681   370 IVLPNsAGTGPMY-PFYDALEVPVVAIGVGNAGSNAHAPNENIRIADYYKGIEHTEELL 427
PRK09104 PRK09104
hypothetical protein; Validated
1-450 4.35e-79

hypothetical protein; Validated


Pssm-ID: 236379 [Multi-domain]  Cd Length: 464  Bit Score: 253.67  E-value: 4.35e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281   1 MAALTTLFKYIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLGGSVELVDIgkqklpdgseiPLPPI 80
Cdd:PRK09104    2 MADLDPVLDHIDANLDASLERLFALLRIPSISTDPAYAADCRKAADWLVADLASLGFEASVRDT-----------PGHPM 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  81 LLGRL-GSDPQKKTVCIYGHLDVQPAALEDGWDSEPFT--LVER-DGK--LYGRGSTDDKGPVAGWINALEAYQKTGQEI 154
Cdd:PRK09104   71 VVAHHeGPTGDAPHVLFYGHYDVQPVDPLDLWESPPFEprIKETpDGRkvIVARGASDDKGQLMTFVEACRAWKAVTGSL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 155 PVNVRFCLEGMEESGSEGLDELIFARKDTFFKDVDYVCisDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGG 234
Cdd:PRK09104  151 PVRVTILFEGEEESGSPSLVPFLEANAEELKADVALVC--DTGMWDRETPAITTSLRGLVGEEVTITAADRDLHSGLFGG 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 235 SVHEAMTDLILLMGSLVDKRGNILIPGINEAVAAVTEEEHKLYDDIDFDIEEFAKDVGAQILLHSHKKDILMHRWRYPSL 314
Cdd:PRK09104  229 AAANPIRVLTRILAGLHDETGRVTLPGFYDGVEELPPEILAQWKALGFTAEAFLGPVGLSIPAGEKGRSVLEQIWSRPTC 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 315 SLHGIEGAFSGSGAKTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKkfaelRSPNEFKV-YMGHGGKPWVS-DFSHP 392
Cdd:PRK09104  309 EINGIWGGYTGEGFKTVIPAEASAKVSFRLVGGQDPAKIREAFRAYVRA-----RLPADCSVeFHDHGGSPAIAlPYDSP 383
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1631970281 393 HYLAGRRAMKTVFGVEPDLTREGGSIPVTLTFQEATGKNVMLLPVGSADDGAHSQNEK 450
Cdd:PRK09104  384 ALAAAKAALSDEWGKPAVLIGSGGSIPIVGDFKRILGMDSLLVGFGLDDDRIHSPNEK 441
PRK07907 PRK07907
hypothetical protein; Provisional
11-451 1.48e-77

hypothetical protein; Provisional


Pssm-ID: 236127 [Multi-domain]  Cd Length: 449  Bit Score: 249.05  E-value: 1.48e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  11 IDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLG-GSVELVDigkqklPDGSeiplpPILLGRLGSDP 89
Cdd:PRK07907   13 VAELLPRVRADLEELVRIPSVAADPFRREEVARSAEWVADLLREAGfDDVRVVS------ADGA-----PAVIGTRPAPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  90 QKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYqktGQEIPVNVRFCLEGMEESG 169
Cdd:PRK07907   82 GAPTVLLYAHHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALRAL---GGDLPVGVTVFVEGEEEMG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 170 SEGLDELIFARKDTFFKDVDYVCISDNYWLGkkKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMGS 249
Cdd:PRK07907  159 SPSLERLLAEHPDLLAADVIVIADSGNWSVG--VPALTTSLRGNADVVVTVRTLEHAVHSGQFGGAAPDALTALVRLLAT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 250 LVDKRGNILIPGINEAVAAvteeehklyDDIDFDIEEFAKDV----GAQILLHSHKKDILmhrWRYPSLSLHGIEgAFSG 325
Cdd:PRK07907  237 LHDEDGNVAVDGLDATEPW---------LGVDYDEERFRADAgvldGVELIGTGSVADRL---WAKPAITVIGID-APPV 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 326 SGAKTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKkfaelRSP--NEFKVYMGHGGKPWVSDFSHPHYLAGRRAMKT 403
Cdd:PRK07907  304 AGASNALPPSARARLSLRVAPGQDAAEAQDALVAHLEA-----HAPwgAHVTVERGDAGQPFAADASGPAYDAARAAMRE 378
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1631970281 404 VFGVEPDLTREGGSIPVTLTFQEA-TGKNVMLLPVGSADDGAHSQNEKL 451
Cdd:PRK07907  379 AWGKDPVDMGMGGSIPFIAELQEAfPQAEILVTGVEDPKTRAHSPNESV 427
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
7-469 6.49e-69

Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism];


Pssm-ID: 223697 [Multi-domain]  Cd Length: 409  Bit Score: 225.43  E-value: 6.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281   7 LFKYIDENQDRYIKKLAKWVAIQSVSAwpekrGEIRRMMEVAAADVKQLGGSVELVDIGkqklpdgsEIPLPPILLGRLG 86
Cdd:COG0624     4 LLEVSLDLLDDILELLKELVRIPSVSA-----GEEAEAAELLAEWLEELGFEVEEDEVG--------PGPGRPNLVARLG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  87 SDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGME 166
Cdd:COG0624    71 GGDGGPTLLLGGHLDVVPAGGGEDWTTDPFEPTIKDGKLYGRGAADMKGGLAAALYALSALKAAGGELPGDVRLLFTADE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 167 ESGSEGLDELIFARKDTFFKDVDYVCISDNYWLGKKKPCITYGLRGICYFFIEVEcSNKDLHSGVYGGSVHEAMTDLILL 246
Cdd:COG0624   151 ESGGAGGKAYLEEGEEALGIRPDYEIVGEPTLESEGGDIIVVGHKGSLWLEVTVK-GKAGHASTTPPDLGRNPIHAAIEA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 247 MGSLVDKRGNILIPGINEavaavteeehklyddidfdieEFAKDVGaqillhshkkdilmhrwrypsLSLHGIEGAFSGS 326
Cdd:COG0624   230 LAELIEELGDLAGEGFDG---------------------PLGLNVG---------------------LILAGPGASVNGG 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 327 GAKTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKKFAELRSpnEFKVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFG 406
Cdd:COG0624   268 DKVNVIPGEAEATVDIRLLPGEDLDDVLEELEAELRAIAPKEGV--EYEIEPGLGEPPLPVPGDSPLVAALAEAAEELLG 345
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631970281 407 VEPdLTREGGsIPVTLTFQEATGKNVMLLPVGSaDDGAHSQNEKLNRYNYIEGTKMLAAYLYE 469
Cdd:COG0624   346 LPP-EVSTGG-GTHDARFFARLGIPAVIFGPGD-IGLAHQPNEYVELEDLVKGAKVLARLLYE 405
PRK06446 PRK06446
hypothetical protein; Provisional
16-473 8.95e-54

hypothetical protein; Provisional


Pssm-ID: 235802 [Multi-domain]  Cd Length: 436  Bit Score: 186.50  E-value: 8.95e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  16 DRYIKKLAKWVAIQSVSAwpekRGE-IRRMMEVAAADVKQLGGSVELVdigkqklpdgsEIPLPPILLGRLGSDpQKKTV 94
Cdd:PRK06446    2 DEELYTLIEFLKKPSISA----TGEgIEETANYLKDTMEKLGIKANIE-----------RTKGHPVVYGEINVG-AKKTL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  95 CIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGqEIPVNVRFCLEGMEESGSEGLD 174
Cdd:PRK06446   66 LIYNHYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKH-KLNVNVKFLYEGEEEIGSPNLE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 175 ELIFARKDTFfkDVDYVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSgVYGGSVHEAMTDLILLMGSLVDKR 254
Cdd:PRK06446  145 DFIEKNKNKL--KADSVIMEGAGLDPKGRPQIVLGVKGLLYVELVLRTGTKDLHS-SNAPIVRNPAWDLVKLLSTLVDGE 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 255 GNILIPGINEAVAAVTEEEHKLYDDIDFDIEEFAKDVGAQILLHSHKKDILMHRWRYPSLSLHGIEGAFSGSGAKTVIPR 334
Cdd:PRK06446  222 GRVLIPGFYDDVRELTEEERELLKKYDIDVEELRKALGFKELKYSDREKIAEALLTEPTCNIDGFYSGYTGKGSKTIVPS 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 335 KVVGKFSIRLVPNMTPevvgEQVTSYLTKKFAELRSPNEFKVymgHGG-KPWVSDFSHPHYLAGRRAMKTVFGVEPDL-- 411
Cdd:PRK06446  302 RAFAKLDFRLVPNQDP----YKIFELLKKHLQKVGFNGEIIV---HGFeYPVRTSVNSKVVKAMIESAKRVYGTEPVVip 374
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631970281 412 ----TREGGSIPVTLTFQEAtgknVMLLPVGSADDGAHSQNEKLNRYNYIEGTKMLAAYLYEVSQL 473
Cdd:PRK06446  375 nsagTQPMGLFVYKLGIRDI----VSAIGVGGYYSNAHAPNENIRIDDYYKAIKHTEEFLKLYSTL 436
M20_dipept_like cd05678
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ...
79-467 5.86e-48

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


Pssm-ID: 349927 [Multi-domain]  Cd Length: 466  Bit Score: 171.51  E-value: 5.86e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  79 PILLGRLGSDPQKKTVCIYGHLDVQPAaLEDGWDSE-PFT--LVERDGK--------------------LYGRGSTDDKG 135
Cdd:cd05678    48 PLLLAEKPISDARKTVLFYMHLDGQPV-DPSKWDQKsPYTpvLKRKDAAgnweeinwdaifsnldpewrVFARAAADDKG 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 136 PVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSEGLDELIFARKDTFfkDVDYVCISDNYWLGKKKPCITYGLRGICY 215
Cdd:cd05678   127 PIMMMLAALDALKAGGIAPKFNVKIILDSEEEKGSPSLPKAVKEYKELL--AADALIIMDGPAHATNKPTLTFGCRGIAT 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 216 FFIEVECSNKDLHSGVYGGSVHEAMTDLILLMGSLVDKRGNILIPGINEAVaAVTEEEHKLYDDIDFDIEEFAKDVGaqI 295
Cdd:cd05678   205 ATLTTYGAKVPQHSGHYGNYAPNPAFRLSSLLASMKDDTGKVTIPGFYDGI-SIDEETQKILAAVPDDEESINKRLG--I 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 296 LLHSHKKDILMHRWRYPSLSLHGIEGAFSGSGAKTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKK--FAELRSPNE 373
Cdd:cd05678   282 AQTDKVGRNYQEALQYPSLNVRGMESGWKGDKVRTIIPEIAEAEIDIRLVPESDGPYLLDLVKAHIEKQgyFVTDRAPTD 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 374 ---------FKVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFGVEPDLTR-EGGSIPVTlTFQEATGKNVMLLPVGSADDG 443
Cdd:cd05678   362 eerlahdkiAKFTYRNGADAFRTDINSPIGNWLRKALTDEFGEEPIQIRmMGGTVPIA-PFVNVLDIPAIIVPMVNMDNN 440
                         410       420
                  ....*....|....*....|....
gi 1631970281 444 AHSQNEKLNRYNYIEGTKMLAAYL 467
Cdd:cd05678   441 QHSPNENLRIGNIRTGIRTCYAIL 464
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
95-469 5.98e-42

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: 396225 [Multi-domain]  Cd Length: 315  Bit Score: 151.35  E-value: 5.98e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  95 CIYGHLDVQPAALEDGWdsePFTLVErDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEiPVNVRFCLEGMEESGSEGLD 174
Cdd:pfam01546   1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGGMGGAR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 175 ELIFARKDTFFKdVDYV---CISD-NYWLGKKKPCITYGLRGICYFFIEVECsnKDLHSGvYGGSVHEAMTDLILLMGSL 250
Cdd:pfam01546  76 ALIEDGLLEREK-VDAVfglHIGEpTLLEGGIAIGVVTGHRGSLRFRVTVKG--KGGHAS-TPHLGVNAIVAAARLILAL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 251 VDKRGNILIPGiNEAVAAVTeeehklyddidfdieefakdvgaqillhshkkdilmhrwrypslSLHGIEGAFsgsgakT 330
Cdd:pfam01546 152 QDIVSRNVDPL-DPAVVTVG--------------------------------------------NITGIPGGV------N 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 331 VIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKKFAELRSPNEFKVymGHGGKPWVSDfSHPHYLAGRRAMKTVFGVEPD 410
Cdd:pfam01546 181 VIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEY--VEGGAPPLVN-DSPLVAALREAAKELFGLKVE 257
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631970281 411 LTREGGSIpvtlT-----FQEATGKNVMLLpvGSADDGAHSQNEKLNRYNYIEGTKMLAAYLYE 469
Cdd:pfam01546 258 LIVSGSMG----GtdaafFLLGVPPTVVFF--GPGSGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
M20_dipept_dapE cd05682
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ...
66-465 6.23e-29

uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.


Pssm-ID: 349931 [Multi-domain]  Cd Length: 451  Bit Score: 118.59  E-value: 6.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  66 KQKLPDGS----EIP-LPPILLGRL-GSDPQKKTVCIYGHLDVQPAAleDGWDSE--PFTLVERDGKLYGRGSTDDKGPV 137
Cdd:cd05682    42 AQNIKGAKvevvELEgRTPLLFVEIpGTEQDDDTVLLYGHMDKQPPF--TGWDEGlgPTKPVIRGDKLYGRGGADDGYAI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 138 AGWINALEAYQKTGQEIPVNVrFCLEGMEESGSEGLDELIFARKDTfFKDVDYV-CI---SDNY---WLgkkkpciTYGL 210
Cdd:cd05682   120 FASLTAIKALQEQGIPHPRCV-VLIEACEESGSADLPFYLDKLKER-IGNVDLVvCLdsgCGNYeqlWL-------TTSL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 211 RGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMGSLVD-KRGNILIPGINEAVAAVTEEEHKLYDDIDFD--IEEF 287
Cdd:cd05682   191 RGVLGGDLTVQVLNEGVHSGDASGIVPSSFRILRQLLSRIEDeNTGEVKLDEQHCDIPAHRYEQAKKIAEILGEavYEEF 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 288 AKDVGAQiLLHSHKKDILMHRWRYPSLSLHGIEGAFSGSGAKTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKKfae 367
Cdd:cd05682   271 PFVSGVQ-PVTTDLVQLYLNRTWKPQLSVTGADGLPPASTAGNVLRPETTLKLSLRLPPTVDAEKASAALKKLLETD--- 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 368 lrSPNEFKV----------YMGHGGKPWVSDfshphylAGRRAMKTVFGVEPDLTREGGSIPVTLTFQEATGK-NVMLLP 436
Cdd:cd05682   347 --PPYNAKVtfksdgagsgWNAPLLSPWLAK-------ALNEASQLFFGKPAAYQGEGGSIPFMNMLGEKFPKaQFIVTG 417
                         410       420
                  ....*....|....*....|....*....
gi 1631970281 437 VGSADDGAHSQNEKLNrynyIEGTKMLAA 465
Cdd:cd05682   418 VLGPKSNAHGPNEFLH----IPYTKKLTA 442
M20_ArgE_DapE-like cd08659
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ...
22-465 3.08e-28

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: 115.09  E-value: 3.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  22 LAKWVAIQSVSawpekrGEIRRMMEVAAADVKQLGGSVELVDIGKQklpdgseiplpPILLGRLGSDPQKKtVCIYGHLD 101
Cdd:cd08659     3 LQDLVQIPSVN------PPEAEVAEYLAELLAKRGYGIESTIVEGR-----------GNLVATVGGGDGPV-LLLNGHID 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 102 VQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSEGLDELIFARK 181
Cdd:cd08659    65 TVPPGDGDKWSFPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLEAGY 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 182 DtffKDVDYVCI---SDNYwlgkkkpcITYGLRGICYFFIEvecsnkdlhsgVYGGSVHEAMTDLillmgslvdkrgnil 258
Cdd:cd08659   145 A---DRLDALIVgepTGLD--------VVYAHKGSLWLRVT-----------VHGKAAHSSMPEL--------------- 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 259 ipGINeAVAAVteeehklyddIDF--DIEEFAKDVGAQILLhshkkdilmhrwRYPSLSLHGIEGafsGSGAKtVIPRKV 336
Cdd:cd08659   188 --GVN-AIYAL----------ADFlaELRTLFEELPAHPLL------------GPPTLNVGVING---GTQVN-SIPDEA 238
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 337 VGKFSIRLVPNMTPEVVGEQVTSYLTKKFAELrspnEFKVYMGHgGKPWVSDFSHPHYLAGRRAMKTVFGvEPDLTREGG 416
Cdd:cd08659   239 TLRVDIRLVPGETNEGVIARLEAILEEHEAKL----TVEVSLDG-DPPFFTDPDHPLVQALQAAARALGG-DPVVRPFTG 312
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1631970281 417 SIPVTLtFQEATGKNVMLLPVGSAdDGAHSQNEKLNRYNYIEGTKMLAA 465
Cdd:cd08659   313 TTDASY-FAKDLGFPVVVYGPGDL-ALAHQPDEYVSLEDLLRAAEIYKE 359
PRK07079 PRK07079
hypothetical protein; Provisional
22-269 4.13e-28

hypothetical protein; Provisional


Pssm-ID: 235928 [Multi-domain]  Cd Length: 469  Bit Score: 116.17  E-value: 4.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  22 LAKWVAIQSVSAWPEKRGEIRRMM--EVAAAdVKQLGGSVELVDigkQKLPDGseiplPPILLGRLGSDPQKKTVCIYGH 99
Cdd:PRK07079   23 LARRVAYRTESQNPDRAPALRAYLtdEIAPA-LAALGFTCRIVD---NPVAGG-----GPFLIAERIEDDALPTVLIYGH 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 100 LDVQPAaLEDGWDS--EPFTLVERDGKLYGRGSTDDKGpvAGWIN--ALEAYQKT-GQEIPVNVRFCLEGMEESGSEGLD 174
Cdd:PRK07079   94 GDVVRG-YDEQWREglSPWTLTEEGDRWYGRGTADNKG--QHTINlaALEQVLAArGGRLGFNVKLLIEMGEEIGSPGLA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 175 ELIFARKDTFFKDVdyVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMGSLVDKR 254
Cdd:PRK07079  171 EVCRQHREALAADV--LIASDGPRLSAERPTLFLGSRGAVNFRLRVNLRDGAHHSGNWGGLLRNPGTVLAHAIASLVDAR 248
                         250       260
                  ....*....|....*....|
gi 1631970281 255 GNILIPG-----INEAVAAV 269
Cdd:PRK07079  249 GRIQVPGlrpppLPAAVRAA 268
M20_dipept_like cd05679
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ...
14-265 8.03e-27

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: 112.21  E-value: 8.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  14 NQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMM-EVAAADVKQLGGSVELVDigkQKLPDGSeiplpPILLGRLGSDPQKK 92
Cdd:cd05679     2 DSGAFLAELARRVAVPTESQEPARKPELRAYLdQEMRPRFERLGFTVHIHD---NPVAGRA-----PFLIAERIEDPSLP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  93 TVCIYGHLDVQP---AALEDGWDsePFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKT-GQEIPVNVRFCLEGMEES 168
Cdd:cd05679    74 TLLIYGHGDVVPgyeGRWRDGRD--PWTVTVWGERWYGRGTADNKGQHSINMAALRQVLEArGGKLGFNVKFLIEMGEEM 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 169 GSEGLDELIFARKDTFFKDVdyVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMG 248
Cdd:cd05679   152 GSPGLRAFCFSHREALKADL--FIASDGPRLAADRPTMFLGSRGGLNFELRVNLREGGHHSGNWGGLLANPGIILANAIA 229
                         250
                  ....*....|....*..
gi 1631970281 249 SLVDKRGNILIPGINEA 265
Cdd:cd05679   230 SLVDGKGRIKLPALKPA 246
DapE-ArgE TIGR01910
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ...
19-461 1.30e-25

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: 107.87  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  19 IKKLAKWVAIQSVSAWPEKRGEIRRMMEvaaADVKQLGGSVELVDIgkqklPDGSEIPLPPILLGRLGSDPQKkTVCIYG 98
Cdd:TIGR01910   1 VELLKDLISIPSVNPPGGNEETIANYIK---DLLREFGFSTDVIEI-----TDDRLKVLGKVVVKEPGNGNEK-SLIFNG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  99 HLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSEGLDELIf 178
Cdd:TIGR01910  72 HYDVVPAGDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLYLL- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 179 arKDTFFKDVDYVCISDNYWLGKkkpcITYGLRGICYFfievecsnkdlHSGVYGGSVHEAMTDLillmGSLVDKRGNIL 258
Cdd:TIGR01910 151 --QRGYFKDADGVLIPEPSGGDN----IVIGHKGSIWF-----------KLRVKGKQAHASFPQF----GVNAIMKLAKL 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 259 IPGINEAvaavteeEHKLYDDIDFDIEefakdvgaqillhshkkdilMHRWRYPSlslhgieGAFSGSGAKTVIPRKVVG 338
Cdd:TIGR01910 210 ITELNEL-------EEHIYARNSYGFI--------------------PGPITFNP-------GVIKGGDWVNSVPDYCEF 255
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 339 KFSIRLVPNMTPEVVGEQVTSYLTKKFAELRSPNEFKVYMGHGGKPWVSDfSHPHYLAGRRAMKTVFGVEPdltrEGGSI 418
Cdd:TIGR01910 256 SIDVRIIPEENLDEVKQIIEDVVKALSKSDGWLYENEPVVKWSGPNETPP-DSRLVKALEAIIKKVRGIEP----EVLVS 330
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1631970281 419 PVTLTFQEATGKNVMLLPVGSADDG-AHSQNEKLNRYNYIEGTK 461
Cdd:TIGR01910 331 TGGTDARFLRKAGIPSIVYGPGDLEtAHQVNEYISIKNLVESTK 374
M20_18_42 cd18669
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ...
80-210 1.04e-24

M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).


Pssm-ID: 349948 [Multi-domain]  Cd Length: 198  Bit Score: 100.97  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  80 ILLGRLGSDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVR 159
Cdd:cd18669     1 NVIARYGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1631970281 160 FCLEGMEESGSEGLDELIFARKDTFFKDVDYVCISDNYWLGKKKPCITYGL 210
Cdd:cd18669    81 VAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTPL 131
Zinc_peptidase_like cd03873
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
80-207 4.85e-24

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: 99.04  E-value: 4.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  80 ILLGRLGSDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVR 159
Cdd:cd03873     1 NLIARLGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1631970281 160 FCLEGMEESGSEGLDELIFARKDTFFKDVDYVCISDNYWLGKKKPCIT 207
Cdd:cd03873    81 VAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAFVIDATAGPILQKGVV 128
PRK08651 PRK08651
succinyl-diaminopimelate desuccinylase; Reviewed
22-416 1.14e-20

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 236323 [Multi-domain]  Cd Length: 394  Bit Score: 93.52  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  22 LAKWVAIQSVSAWPEKRGEIRrmmEVAAADVKQLGGSVELVDIGKQKLPdgSEIPLPPILLGRLGSDpqKKTVCIYGHLD 101
Cdd:PRK08651   12 LKDLIKIPTVNPPGENYEEIA---EFLRDTLEELGFSTEIIEVPNEYVK--KHDGPRPNLIARRGSG--NPHLHFNGHYD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 102 VQPAAleDGWDS-EPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGqeiPVNVRFCLEGMEESGSEGLDELIfar 180
Cdd:PRK08651   85 VVPPG--EGWSVnVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDPAG---DGNIELAIVPDEETGGTGTGYLV--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 181 kDTFFKDVDYVCI-----SDNYWlgkkkpcitYGLRGICYFFIEvecsnkdlhsgVYGGSVHEAMTDLillmgslvdkrg 255
Cdd:PRK08651  157 -EEGKVTPDYVIVgepsgLDNIC---------IGHRGLVWGVVK-----------VYGKQAHASTPWL------------ 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 256 nilipGIN--EAVAAVTEEEHKLYDDIdfdieefakdvgaqillhSHKKDILMHRWRYPSLSLHG--IEGafsgsGAKT- 330
Cdd:PRK08651  204 -----GINafEAAAKIAERLKSSLSTI------------------KSKYEYDDERGAKPTVTLGGptVEG-----GTKTn 255
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 331 VIPRKVvgKFSI--RLVPNMTPEVVGEQVTSYLTKKFAELRSPNEFKV--YMghggKPWVSDFSHPHYLAGRRAMKTVFG 406
Cdd:PRK08651  256 IVPGYC--AFSIdrRLIPEETAEEVRDELEALLDEVAPELGIEVEFEItpFS----EAFVTDPDSELVKALREAIREVLG 329
                         410
                  ....*....|
gi 1631970281 407 VEPDLTREGG 416
Cdd:PRK08651  330 VEPKKTISLG 339
M20_PepV cd03888
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ...
9-174 1.90e-18

M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.


Pssm-ID: 349884 [Multi-domain]  Cd Length: 449  Bit Score: 87.30  E-value: 1.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281   9 KYIDENQDRYIKKLAKWVAIQSVSAWPEKR---GE-IRRMMEVAAADVKQLGGSVELVD--IGKQKLPDGSEIplppill 82
Cdd:cd03888     1 EEIDKYKDEILEDLKELVAIPSVRDEATEGapfGEgPRKALDKFLDLAKRLGFKTKNIDnyAGYAEYGEGEEV------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  83 grlgsdpqkktVCIYGHLDVQPAAleDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCL 162
Cdd:cd03888    74 -----------LGILGHLDVVPAG--EGWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIF 140
                         170
                  ....*....|..
gi 1631970281 163 EGMEESGSEGLD 174
Cdd:cd03888   141 GTDEETGWKCIE 152
M20_yscS_like cd05675
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ...
86-184 2.71e-18

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: 86.64  E-value: 2.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  86 GSDPQKKTVCIYGHLDVQPAALEDgWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGM 165
Cdd:cd05675    60 GTDPSAGPLLLLGHIDVVPADASD-WSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVAD 138
                          90       100
                  ....*....|....*....|
gi 1631970281 166 EESGSE-GLDELIFARKDTF 184
Cdd:cd05675   139 EEAGGEnGAKWLVDNHPELF 158
M20_ArgE cd03894
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ...
22-418 1.24e-15

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: 78.02  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  22 LAKWVAIQSVSAWPEKRgeirrMMEVAAADVKQLGGSVELVDIGKQKLPDgseiplppiLLGRLGSDPQKKtVCIYGHLD 101
Cdd:cd03894     3 LARLVAFDTVSRNSNLA-----LIEYVADYLAALGVKSRRVPVPEGGKAN---------LLATLGPGGEGG-LLLSGHTD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 102 VQPAAlEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEgmEESGSEGLDELIFARK 181
Cdd:cd03894    68 VVPVD-GQKWSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYD--EEVGCLGVRHLIAALA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 182 DTFFKDvDYVCISDNYWLgkkKPCItyGLRGICYFFIEV---ECSNKDLHSGVyggSVHEAMTDLIllmGSLVDKRgnil 258
Cdd:cd03894   145 ARGGRP-DAAIVGEPTSL---QPVV--AHKGIASYRIRVrgrAAHSSLPPLGV---NAIEAAARLI---GKLRELA---- 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 259 ipgineavaavtEEEHKLYDDIDFDIEefakdvgaqillhshkkdilmhrwrYPSLSLHGIEGafsGSgAKTVIPRKVVG 338
Cdd:cd03894   209 ------------DRLAPGLRDPPFDPP-------------------------YPTLNVGLIHG---GN-AVNIVPAECEF 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 339 KFSIRLVPNMTPEVVGEQVTSYLtkKFAELRSPNEFKVYMGHGGKPWVSDFSHP-----HYLAGRRAMKTV-FGVE-PDL 411
Cdd:cd03894   248 EFEFRPLPGEDPEAIDARLRDYA--EALLEFPEAGIEVEPLFEVPGLETDEDAPlvrlaAALAGDNKVRTVaYGTEaGLF 325
                         410
                  ....*....|....*
gi 1631970281 412 TREG--------GSI 418
Cdd:cd03894   326 QRAGiptvvcgpGSI 340
M20_DapE_proteobac cd03891
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ...
22-193 1.72e-15

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: 77.54  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  22 LAKWVAIQSVSawPEKRGeirrMMEVAAADVKQLGGSVELVDIGKQKlpdgseiplppILLGRLGSDPqkKTVCIYGHLD 101
Cdd:cd03891     4 AKELIRRPSVT--PDDAG----AQDLIAERLKALGFTCERLEFGGVK-----------NLWARRGTGG--PHLCFAGHTD 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 102 VQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSE-G----LDEL 176
Cdd:cd03891    65 VVPPGDLEGWSSDPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIdGtkkvLEWL 144
                         170
                  ....*....|....*..
gi 1631970281 177 IfARKDTFfkdvDYvCI 193
Cdd:cd03891   145 K-ARGEKI----DY-CI 155
PRK06915 PRK06915
peptidase;
10-172 2.55e-15

peptidase;


Pssm-ID: 180745 [Multi-domain]  Cd Length: 422  Bit Score: 77.81  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  10 YIDENQDRYIKKLAKWVAIQSVSawpekrGEIRRMMEVAAADVKQLGGSVELVDIGKQKLPDG-------SEIPLPPILL 82
Cdd:PRK06915   11 YIESHEEEAVKLLKRLIQEKSVS------GDESGAQAIVIEKLRELGLDLDIWEPSFKKLKDHpyfvsprTSFSDSPNIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  83 GRLGSDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCL 162
Cdd:PRK06915   85 ATLKGSGGGKSMILNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQS 164
                         170
                  ....*....|
gi 1631970281 163 EGMEESGSEG 172
Cdd:PRK06915  165 VIEEESGGAG 174
dipeptidaselike TIGR01887
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ...
91-174 8.94e-15

dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.


Pssm-ID: 273854 [Multi-domain]  Cd Length: 447  Bit Score: 76.26  E-value: 8.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  91 KKTVCIYGHLDVQPAAleDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGS 170
Cdd:TIGR01887  67 EEVLGILGHLDVVPAG--DGWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEESGW 144

                  ....
gi 1631970281 171 EGLD 174
Cdd:TIGR01887 145 KCID 148
PRK07318 PRK07318
dipeptidase PepV; Reviewed
90-174 1.09e-14

dipeptidase PepV; Reviewed


Pssm-ID: 235988 [Multi-domain]  Cd Length: 466  Bit Score: 76.03  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  90 QKKTVCIYGHLDVQPAAleDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGqeIPVN--VRFCLEGMEE 167
Cdd:PRK07318   78 GEEVLGILGHLDVVPAG--DGWDTDPYEPVIKDGKIYARGTSDDKGPTMAAYYALKIIKELG--LPLSkkVRFIVGTDEE 153

                  ....*..
gi 1631970281 168 SGSEGLD 174
Cdd:PRK07318  154 SGWKCMD 160
PRK09133 PRK09133
hypothetical protein; Provisional
12-191 3.04e-14

hypothetical protein; Provisional


Pssm-ID: 236388 [Multi-domain]  Cd Length: 472  Bit Score: 74.65  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  12 DENQDRYIKKlaKWVAIQSVSAwpekRGEIRRMMEVAAADVKQLGGSVELVDIGKQKLPDGSeiplppiLLGRL-GSDPq 90
Cdd:PRK09133   35 DQQAARDLYK--ELIEINTTAS----TGSTTPAAEAMAARLKAAGFADADIEVTGPYPRKGN-------LVARLrGTDP- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  91 KKTVCIYGHLDVQPAALEDgWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESG- 169
Cdd:PRK09133  101 KKPILLLAHMDVVEAKRED-WTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKRDIILALTGDEEGTp 179
                         170       180
                  ....*....|....*....|..
gi 1631970281 170 SEGLDELIFARKDTFfkDVDYV 191
Cdd:PRK09133  180 MNGVAWLAENHRDLI--DAEFA 199
PRK07205 PRK07205
hypothetical protein; Provisional
9-168 3.33e-14

hypothetical protein; Provisional


Pssm-ID: 235965 [Multi-domain]  Cd Length: 444  Bit Score: 74.35  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281   9 KYIDEN-QDRYIKKLAKWVAIQSVSAWPEKR---GE-IRRMMEVAAADVKQLGGSVELvDigkqklPDG----SEIplpp 79
Cdd:PRK07205    3 SYITEKvQDACVAAIKTLVSYPSVLNEGENGtpfGQaIQDVLEATLDLCQGLGFKTYL-D------PKGyygyAEI---- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  80 illgrlGSdpQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVR 159
Cdd:PRK07205   72 ------GQ--GEELLAILCHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIR 143

                  ....*....
gi 1631970281 160 FCLEGMEES 168
Cdd:PRK07205  144 FIFGTDEET 152
PRK13983 PRK13983
M20 family metallo-hydrolase;
12-187 3.61e-14

M20 family metallo-hydrolase;


Pssm-ID: 237578 [Multi-domain]  Cd Length: 400  Bit Score: 74.11  E-value: 3.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  12 DENQDRYIKKLAKWVAIQSVSawPEKRGEirrmMEVAAAD-----VKQLG-GSVELVDIGKQKLPDGSEiplpPILLGRL 85
Cdd:PRK13983    1 DELRDEMIELLSELIAIPAVN--PDFGGE----GEKEKAEyleslLKEYGfDEVERYDAPDPRVIEGVR----PNIVAKI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  86 GSDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDD-KGPVAGWInALEAYQKTGQEIPVNVRFCLEG 164
Cdd:PRK13983   71 PGGDGKRTLWIISHMDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNgQGIVSSLL-ALKALMDLGIRPKYNLGLAFVS 149
                         170       180
                  ....*....|....*....|....
gi 1631970281 165 MEESGSE-GLDELIFARKDTFFKD 187
Cdd:PRK13983  150 DEETGSKyGIQYLLKKHPELFKKD 173
PRK08596 PRK08596
acetylornithine deacetylase; Validated
4-304 3.87e-14

acetylornithine deacetylase; Validated


Pssm-ID: 181495 [Multi-domain]  Cd Length: 421  Bit Score: 73.92  E-value: 3.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281   4 LTTLFKYIDENQDRYIKKLAKWVAIQSVSawPEKRGEIRRMMEVAAAdVKQLGGSVELVDIgkqklpdgseIPLPPILLG 83
Cdd:PRK08596    1 VSQLLEQIELRKDELLELLKTLVRFETPA--PPARNTNEAQEFIAEF-LRKLGFSVDKWDV----------YPNDPNVVG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  84 RL-GSDPQK-KTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFC 161
Cdd:PRK08596   68 VKkGTESDAyKSLIINGHMDVAEVSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 162 LEGMEESGSEGLDELIfarKDTFFKDVDYVC-ISDNYWLGKKkpcityglrGICYFFIEVEcSNKDLHSG---------- 230
Cdd:PRK08596  148 SVIGEEVGEAGTLQCC---ERGYDADFAVVVdTSDLHMQGQG---------GVITGWITVK-SPQTFHDGtrrqmihagg 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 231 -VYGGSVHEAMTDLILLMGSL-----VDKRGNILIPG---INEAV------AAVTEEEHKLYDDIDFDIEEFAKDVGAQI 295
Cdd:PRK08596  215 gLFGASAIEKMMKIIQSLQELerhwaVMKSYPGFPPGtntINPAVieggrhAAFIADECRLWITVHFYPNETYEQVIKEI 294
                         330
                  ....*....|..
gi 1631970281 296 ---LLHSHKKDI 304
Cdd:PRK08596  295 eeyIGKVAAADP 306
dipeptidase TIGR01886
dipeptidase PepV; This model represents a small clade of dipeptidase enzymes which are members ...
83-174 6.21e-14

dipeptidase PepV; This model represents a small clade of dipeptidase enzymes which are members of the larger M25 subfamily of metalloproteases. Two characterized enzymes are included in the seed. One, from Lactococcus lactis has been shown to act on a wide range of dipeptides, but not larger peptides. The enzyme from Lactobacillus delbrueckii was originally characterized as a Xaa-His dipeptidase, specifically a carnosinase (beta-Ala-His) by complementation of an E. coli mutant. Further study, including the crystallization of the enzyme, has shown it to also be a non-specific dipeptidase. This group also includes enzymes from Streptococcus and Enterococcus. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 130941 [Multi-domain]  Cd Length: 466  Bit Score: 73.76  E-value: 6.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  83 GRLGSDPQKKTVCIYGHLDVQPAAleDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCL 162
Cdd:TIGR01886  70 GHVEYGAGDERLGIIGHMDVVPAG--EGWTRDPFEPEIDEGRIYARGASDDKGPSLAAYYAMKILKELGLPPSKKIRFVV 147
                          90
                  ....*....|..
gi 1631970281 163 EGMEESGSEGLD 174
Cdd:TIGR01886 148 GTNEETGWVDMD 159
PRK07522 PRK07522
acetylornithine deacetylase; Provisional
98-156 1.48e-13

acetylornithine deacetylase; Provisional


Pssm-ID: 236039 [Multi-domain]  Cd Length: 385  Bit Score: 71.76  E-value: 1.48e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1631970281  98 GHLDVQPAAlEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPV 156
Cdd:PRK07522   71 GHTDVVPVD-GQAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPL 128
M20_ArgE_DapE-like cd08011
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
91-263 3.77e-13

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: 70.49  E-value: 3.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  91 KKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEES-G 169
Cdd:cd08011    60 GKRLLFNGHYDVVPAGDGEGWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETgG 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 170 SEGLDELIfarkDTFFKDVDYVCI-----SDNywlgkkkpcITYGLRGICYFFIEVecsnkdLHSGVYGGSVHEAMTDLI 244
Cdd:cd08011   140 RAGTKYLL----EKVRIKPNDVLIgepsgSDN---------IRIGEKGLVWVIIEI------TGKPAHGSLPHRGESAVK 200
                         170
                  ....*....|....*....
gi 1631970281 245 LLMgSLVDKRGNiLIPGIN 263
Cdd:cd08011   201 AAM-KLIERLYE-LEKTVN 217
M20_CPDG2 cd03885
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ...
18-181 1.85e-12

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: 68.39  E-value: 1.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  18 YIKKLAKWVAIQSVSAWPEkrgEIRRMMEVAAADVKQLGGSVELVDIGKqklpDGseiplpPILLGRLGSDPQKKTVCIy 97
Cdd:cd03885     1 MLDLLERLVNIESGTYDKE---GVDRVAELLAEELEALGFTVERRPLGE----FG------DHLIATFKGTGGKRVLLI- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  98 GHLD-VQPaalEDGWDSEPFTlvERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSEGLDEL 176
Cdd:cd03885    67 GHMDtVFP---EGTLAFRPFT--VDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSREL 141

                  ....*..
gi 1631970281 177 I--FARK 181
Cdd:cd03885   142 IeeEAKG 148
PRK13009 PRK13009
succinyl-diaminopimelate desuccinylase; Reviewed
92-167 2.92e-12

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 237265 [Multi-domain]  Cd Length: 375  Bit Score: 67.80  E-value: 2.92e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631970281  92 KTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEE 167
Cdd:PRK13009   59 PHLCFAGHTDVVPPGDLEAWTSPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEE 134
M20_ArgE_DapE-like cd03895
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
27-172 4.88e-12

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: 67.33  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  27 AIQSVSAWPEKRGEIRRMMEVAAADVKQLGGSVELVDIGKQKL---PDGSEI----PLPPILLGRLGSDPQK-KTVCIYG 98
Cdd:cd03895     2 FLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDRWEIDVEKLkhhPGFSPVavdyAGAPNVVGTHRPRGETgRSLILNG 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631970281  99 HLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSEG 172
Cdd:cd03895    82 HIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTGNG 155
PRK08588 PRK08588
succinyl-diaminopimelate desuccinylase; Reviewed
91-172 1.31e-11

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 181490 [Multi-domain]  Cd Length: 377  Bit Score: 66.06  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  91 KKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGS 170
Cdd:PRK08588   59 SPVLALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEEVGE 138

                  ..
gi 1631970281 171 EG 172
Cdd:PRK08588  139 LG 140
M20_ArgE_DapE-like cd05650
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
92-195 5.92e-11

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: 64.02  E-value: 5.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  92 KTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSE 171
Cdd:cd05650    70 KTLWIISHLDTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSE 149
                          90       100
                  ....*....|....*....|....*
gi 1631970281 172 -GLDELIfaRKDTFFKDVDYVCISD 195
Cdd:cd05650   150 yGIQYLL--NKFDLFKKDDLIIVPD 172
PRK13013 PRK13013
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
81-219 8.71e-11

acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;


Pssm-ID: 237268 [Multi-domain]  Cd Length: 427  Bit Score: 63.63  E-value: 8.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  81 LLGRLGSDPQKKTVCIYGHLDVQPAAleDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRF 160
Cdd:PRK13013   74 LVARRQGARDGDCVHFNSHHDVVEVG--HGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEI 151
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631970281 161 CLEGMEESGS-EGLDELifARKDTFFKD-VDYVCISDNywLGKKKPCItyGLRGICYFFIE 219
Cdd:PRK13013  152 SGTADEESGGfGGVAYL--AEQGRFSPDrVQHVIIPEP--LNKDRICL--GHRGVWWAEVE 206
PRK08262 PRK08262
M20 family peptidase;
86-172 1.00e-10

M20 family peptidase;


Pssm-ID: 236208 [Multi-domain]  Cd Length: 486  Bit Score: 63.42  E-value: 1.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  86 GSDPQKKTVCIYGHLDVQPAA--LEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLE 163
Cdd:PRK08262  106 GSDPSLKPIVLMAHQDVVPVApgTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFG 185

                  ....*....
gi 1631970281 164 GMEESGSEG 172
Cdd:PRK08262  186 HDEEVGGLG 194
M20_ArgE_DapE-like cd05651
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
88-176 1.40e-10

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: 62.33  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  88 DPQKKTVCIYGHLD-VQPAAledGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGqEIPVNVRFCLEGME 166
Cdd:cd05651    52 DEGKPTLLLNSHHDtVKPNA---GWTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEG-PLNYNLIYAASAEE 127
                          90
                  ....*....|.
gi 1631970281 167 E-SGSEGLDEL 176
Cdd:cd05651   128 EiSGKNGIESL 138
PRK08554 PRK08554
peptidase; Reviewed
79-171 2.74e-10

peptidase; Reviewed


Pssm-ID: 236285 [Multi-domain]  Cd Length: 438  Bit Score: 62.10  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  79 PILLGRLGSDPQKktVCIYGHLDVQPAALEDgWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKtgQEIPVNV 158
Cdd:PRK08554   53 YAVYGEIGEGKPK--LLFMAHFDVVPVNPEE-WNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSK--EPLNGKV 127
                          90
                  ....*....|...
gi 1631970281 159 RFCLEGMEESGSE 171
Cdd:PRK08554  128 IFAFTGDEEIGGA 140
PRK06156 PRK06156
dipeptidase;
90-173 2.13e-09

dipeptidase;


Pssm-ID: 235720 [Multi-domain]  Cd Length: 520  Bit Score: 59.60  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  90 QKKTVCIYGHLDVQPA-----ALEDGWDSePFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGqeIPVNVRFCL-- 162
Cdd:PRK06156  108 GSDKVGILTHADVVPAnpelwVLDGTRLD-PFKVTLVGDRLYGRGTEDDKGAIVTALYAMKAIKDSG--LPLARRIELlv 184
                          90
                  ....*....|.
gi 1631970281 163 EGMEESGSEGL 173
Cdd:PRK06156  185 YTTEETDGDPL 195
PRK07906 PRK07906
hypothetical protein; Provisional
81-184 7.77e-09

hypothetical protein; Provisional


Pssm-ID: 181163 [Multi-domain]  Cd Length: 426  Bit Score: 57.55  E-value: 7.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  81 LLGRL-GSDPQKKTVCIYGHLDVQPAALEDgWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVR 159
Cdd:PRK07906   54 VVARLpGADPSRPALLVHGHLDVVPAEAAD-WSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLV 132
                          90       100
                  ....*....|....*....|....*.
gi 1631970281 160 FCLEGMEESGSE-GLDELIFARKDTF 184
Cdd:PRK07906  133 FAFVADEEAGGTyGAHWLVDNHPELF 158
PRK06837 PRK06837
ArgE/DapE family deacylase;
79-151 3.06e-08

ArgE/DapE family deacylase;


Pssm-ID: 180721 [Multi-domain]  Cd Length: 427  Bit Score: 55.78  E-value: 3.06e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631970281  79 PILLGRL-GSDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTG 151
Cdd:PRK06837   84 PNVVGTYrPAGKTGRSLILQGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAG 157
M20_yscS cd05674
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ...
86-146 4.20e-08

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: 55.34  E-value: 4.20e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631970281  86 GSDPQKKTVCIYGHLDVQPAA--LEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEA 146
Cdd:cd05674    64 GSDPSLKPLLLMAHQDVVPVNpeTEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVEL 126
PRK13004 PRK13004
YgeY family selenium metabolism-linked hydrolase;
7-143 8.09e-08

YgeY family selenium metabolism-linked hydrolase;


Pssm-ID: 183836 [Multi-domain]  Cd Length: 399  Bit Score: 54.18  E-value: 8.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281   7 LFKYIDENQDRY----IKKLAKWVAIQSVSawpekrGEIRRMMEVAAADVKQLG-GSVELVDIGKqklpdgseiplppiL 81
Cdd:PRK13004    2 PFKLILMLAEKYkadmTRFLRDLIRIPSES------GDEKRVVKRIKEEMEKVGfDKVEIDPMGN--------------V 61
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631970281  82 LGRLGsdPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINA 143
Cdd:PRK13004   62 LGYIG--HGKKLIAFDAHIDTVGIGDIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYA 121
M20_ArgE_DapE-like cd05649
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
19-151 1.03e-07

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: 53.96  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  19 IKKLAKWVAIQSVSawpekrGEIRRMMEVAAADVKQLG-GSVELVDIGKqklpdgseiplppiLLGRLGSDPqkKTVCIY 97
Cdd:cd05649     1 TRFLRDLIQIPSES------GEEKGVVERIEEEMEKLGfDEVEIDPMGN--------------VIGYIGGGK--KKILFD 58
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1631970281  98 GHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTG 151
Cdd:cd05649    59 GHIDTVGIGNIDNWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLG 112
PRK06133 PRK06133
glutamate carboxypeptidase; Reviewed
15-231 2.93e-07

glutamate carboxypeptidase; Reviewed


Pssm-ID: 235710 [Multi-domain]  Cd Length: 410  Bit Score: 52.33  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  15 QDRYIKKLAKWVAIQSVSAWPEKrgeIRRMMEVAAADVKQLGGSVELVDIGKQKlpdgseiplPPILLGRLGSDPQKKTV 94
Cdd:PRK06133   36 QPAYLDTLKELVSIESGSGDAEG---LKQVAALLAERLKALGAKVERAPTPPSA---------GDMVVATFKGTGKRRIM 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  95 CIyGHLDV--QPAALEDgwdsEPFTlvERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSEG 172
Cdd:PRK06133  104 LI-AHMDTvyLPGMLAK----QPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGSPG 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1631970281 173 LDELIfarkDTFFKDVDYVCisdNYWLGKKKPCITYGLRGICYFFIEVEcsNKDLHSGV 231
Cdd:PRK06133  177 SRELI----AELAAQHDVVF---SCEPGRAKDALTLATSGIATALLEVK--GKASHAGA 226
M20_AcylaseI_like cd05646
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ...
53-134 5.83e-07

M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.


Pssm-ID: 349898 [Multi-domain]  Cd Length: 391  Bit Score: 51.50  E-value: 5.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  53 KQLGGSVELVDIGKQKlpdgseiplPPILLGRLGSDPQKKTVCIYGHLDVQPaALEDGWDSEPFTLVE-RDGKLYGRGST 131
Cdd:cd05646    35 DELGLPVRVIEVVPGK---------PVVVLTWEGSNPELPSILLNSHTDVVP-VFEEKWTHDPFSAHKdEDGNIYARGAQ 104

                  ...
gi 1631970281 132 DDK 134
Cdd:cd05646   105 DMK 107
PRK05111 PRK05111
acetylornithine deacetylase; Provisional
81-135 2.25e-06

acetylornithine deacetylase; Provisional


Pssm-ID: 235346 [Multi-domain]  Cd Length: 383  Bit Score: 49.44  E-value: 2.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1631970281  81 LLGRLGSDPQKKTVCiyGHLDVQPAAlEDGWDSEPFTLVERDGKLYGRGSTDDKG 135
Cdd:PRK05111   63 LLASLGSGEGGLLLA--GHTDTVPFD-EGRWTRDPFTLTEHDGKLYGLGTADMKG 114
M20_ArgE_LysK cd05653
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ...
84-229 1.36e-05

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: 46.96  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  84 RLGSDPQKKTVCIYGHLDVQPAALEdgwdsepfTLVErDGKLYGRGSTDDKGPVAGWINALEAyqkTGQEIPVNVRFCLE 163
Cdd:cd05653    47 VGGAGSGPPDVLLLGHIDTVPGEIP--------VRVE-GGVLYGRGAVDAKGPLAAMILAASA---LNEELGARVVVAGL 114
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631970281 164 GMEESGSEGLDELIfARKDTFfkdvDYVCISD-NYWLGkkkpcITYGLRGIcyFFIEVECSNKDLHS 229
Cdd:cd05653   115 VDEEGSSKGARELV-RRGPRP----DYIIIGEpSGWDG-----ITLGYRGS--LLVKIRCEGRSGHS 169
PRK07473 PRK07473
M20/M25/M40 family metallo-hydrolase;
41-179 1.50e-05

M20/M25/M40 family metallo-hydrolase;


Pssm-ID: 168961 [Multi-domain]  Cd Length: 376  Bit Score: 47.09  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  41 IRRMMEVAAADVKQLGGSVELVDiGKQKLPDGSEIPLPpillgrlGSDPQKKTVCIYGHLD-VQP-AALEDgwdsEPFtl 118
Cdd:PRK07473   33 VNRMLDLAARDMAIMGATIERIP-GRQGFGDCVRARFP-------HPRQGEPGILIAGHMDtVHPvGTLEK----LPW-- 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631970281 119 vERDG-KLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSEGLDELIFA 179
Cdd:PRK07473   99 -RREGnKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPITVLFTPDEEVGTPSTRDLIEA 159
M20_ArgE-related cd08012
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ...
86-254 1.68e-05

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: 47.07  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  86 GSDPqKKTVCIYG-HLDVQPAALEDgWDSEPFTLVeRDG-KLYGRGSTDDKGPVAgwiNALEAYQKTGQEIP------VN 157
Cdd:cd08012    73 GTVD-GKTVSFVGsHMDVVTANPET-WEFDPFSLS-IDGdKLYGRGTTDCLGHVA---LVTELFRQLATEKPalkrtvVA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281 158 VRFCLEGMEESGSEGLDELIfarKDtffKDVDYVCISDNYWL--GKKKPCItyGLRGICYFFIEVecSNKDLHSGVyggs 235
Cdd:cd08012   147 VFIANEENSEIPGVGVDALV---KS---GLLDNLKSGPLYWVdsADSQPCI--GTGGMVTWKLTA--TGKLFHSGL---- 212
                         170       180
                  ....*....|....*....|.
gi 1631970281 236 VHEAMTDLILLMGSL--VDKR 254
Cdd:cd08012   213 PHKAINALELVMEALaeIQKR 233
M20_ArgE_DapE-like_fungal cd05652
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
81-173 5.30e-05

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: 45.34  E-value: 5.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  81 LLGRLGSDPQKKTVcIYGHLDVQPAALedgwdsePFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQ--EIPVNV 158
Cdd:cd05652    49 VYAYPGSSRQPRVL-LTSHIDTVPPFI-------PYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEvpEGDLGL 120
                          90
                  ....*....|....*
gi 1631970281 159 RFCLEgmEESGSEGL 173
Cdd:cd05652   121 LFVVG--EETGGDGM 133
M20_dimer pfam07687
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ...
293-367 8.70e-05

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: 41.56  E-value: 8.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631970281 293 AQIL--LHSHKKDILmHRWRYPSLSLHGIEGAFsgsgAKTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKKFAE 367
Cdd:pfam07687  34 ARLLaeLPAEYGDIG-FDFPRTTLNITGIEGGT----ATNVIPAEAEAKFDIRLLPGEDLEELLEEIEAILEKELPE 105
PRK07338 PRK07338
hydrolase;
6-170 1.53e-04

hydrolase;


Pssm-ID: 235995 [Multi-domain]  Cd Length: 402  Bit Score: 43.80  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281   6 TLFKYIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAAdvkQLGGSVELVDIGKQKL--PDGSEI--PLPPIL 81
Cdd:PRK07338    7 AVLDLIDDRQAPMLEQLIAWAAINSGSRNLDGLARMAELLADAFA---ALPGEIELIPLPPVEVidADGRTLeqAHGPAL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  82 lgRLGSDPQ-KKTVCIYGHLD-VQPAaledgwdSEPFTLVER--DGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVN 157
Cdd:PRK07338   84 --HVSVRPEaPRQVLLTGHMDtVFPA-------DHPFQTLSWldDGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLG 154
                         170
                  ....*....|...
gi 1631970281 158 VRFCLEGMEESGS 170
Cdd:PRK07338  155 YDVLINPDEEIGS 167
Ac-peptdase-euk TIGR01880
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ...
60-184 1.62e-04

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: 43.63  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  60 ELVDIGKQKLPDGSEIPLppILLGRLGSDPQKKTVCIYGHLDVQPAALEDgWDSEPFT-LVERDGKLYGRGSTDDKGPVA 138
Cdd:TIGR01880  42 DELGLARKTIEFVPGKPV--VVLTWPGSNPELPSILLNSHTDVVPVFREH-WTHPPFSaFKDEDGNIYARGAQDMKCVGV 118
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1631970281 139 GWINALEAYQKTGQEIPVNVRFCLEGMEESGseGLDEL-IFARKDTF 184
Cdd:TIGR01880 119 QYLEAVRNLKASGFKFKRTIHISFVPDEEIG--GHDGMeKFAKTDEF 163
M20_like cd02697
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ...
92-171 1.87e-04

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: 43.70  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  92 KTVCIYGHLDVQPAAleDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSE 171
Cdd:cd02697    74 RTVALNAHGDVVPPG--DGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGE 151
M20_ArgE_DapE-like cd08013
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
92-179 2.17e-04

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: 43.23  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  92 KTVCIYGHLDvqpAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGqeIPVNVRFCLEGMEESGSE 171
Cdd:cd08013    69 KSLMLNGHID---TVTLDGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAG--LRGDVILAAVADEEDASL 143

                  ....*...
gi 1631970281 172 GLDELIFA 179
Cdd:cd08013   144 GTQEVLAA 151
M20_DapE_actinobac cd05647
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ...
93-182 3.29e-04

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: 42.81  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  93 TVCIYGHLDVQPAAledgwDSEPFTlVERDGKLYGRGSTDDKGPVAGWINAleAYQKTGQEIPVNVRFCLEGMEESGSE- 171
Cdd:cd05647    55 RVILAGHLDTVPVA-----GNLPSR-VEEDGVLYGCGATDMKAGDAVQLKL--AATLAAATLKHDLTLIFYDCEEVAAEl 126
                          90
                  ....*....|..
gi 1631970281 172 -GLDELIFARKD 182
Cdd:cd05647   127 nGLGRLAEEHPE 138
M20_PAAh_like cd03896
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ...
82-180 3.90e-04

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: 42.47  E-value: 3.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  82 LGRLGSDPQKKTVCIYGHLD-VQPAaledgwdSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRF 160
Cdd:cd03896    45 VGRLRGTGGGPALLFSAHLDtVFPG-------DTPATVRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVF 117
                          90       100
                  ....*....|....*....|
gi 1631970281 161 clegMEESGSEGLDELIFAR 180
Cdd:cd03896   118 ----AANVGEEGLGDLRGAR 133
PRK08737 PRK08737
acetylornithine deacetylase; Provisional
99-146 2.00e-03

acetylornithine deacetylase; Provisional


Pssm-ID: 181544 [Multi-domain]  Cd Length: 364  Bit Score: 40.18  E-value: 2.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1631970281  99 HLDVQPAAleDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEA 146
Cdd:PRK08737   71 HLDTVPDS--PHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANA 116
PRK08652 PRK08652
acetylornithine deacetylase; Provisional
61-172 4.26e-03

acetylornithine deacetylase; Provisional


Pssm-ID: 236324 [Multi-domain]  Cd Length: 347  Bit Score: 39.36  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  61 LVDIGKQKLPDGSEIPLPPIL---LGRLGSDP--------------QKKTVCIYGHLDVQPAAledgwdSEPFtlvERDG 123
Cdd:PRK08652    8 LKQLVKIPSPSGQEDEIALHImefLESLGYDVhiesdgevinivvnSKAELFVEVHYDTVPVR------AEFF---VDGV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1631970281 124 KLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCleGMEESGSEG 172
Cdd:PRK08652   79 YVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFV--SDEEEGGRG 125
PRK04443 PRK04443
[LysW]-lysine hydrolase;
83-172 4.95e-03

[LysW]-lysine hydrolase;


Pssm-ID: 235299 [Multi-domain]  Cd Length: 348  Bit Score: 39.17  E-value: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  83 GRLGSDPqkKTVCIYGHLDVQPAALedgwdsePftlVE-RDGKLYGRGSTDDKGPVAGWINALeayqkTGQEIPVNVRFC 161
Cdd:PRK04443   53 GPAGDGP--PLVLLLGHIDTVPGDI-------P---VRvEDGVLWGRGSVDAKGPLAAFAAAA-----ARLEALVRARVS 115
                          90
                  ....*....|...
gi 1631970281 162 LEGM--EESGSEG 172
Cdd:PRK04443  116 FVGAveEEAPSSG 128
PRK00466 PRK00466
acetyl-lysine deacetylase; Validated
98-229 5.84e-03

acetyl-lysine deacetylase; Validated


Pssm-ID: 166979 [Multi-domain]  Cd Length: 346  Bit Score: 38.61  E-value: 5.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970281  98 GHLDVQPAALEDGWDSEpftlverdgKLYGRGSTDDKGPVAGWINALEAYQKTGqeipVNVRFCLEGMEESGSEGLDELI 177
Cdd:PRK00466   67 SHVDTVPGYIEPKIEGE---------VIYGRGAVDAKGPLISMIIAAWLLNEKG----IKVMVSGLADEESTSIGAKELV 133
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1631970281 178 fARKDTFfkdvDYVCISDnywlgkkkPCITYGL----RGICYffIEVECSNKDLHS 229
Cdd:PRK00466  134 -SKGFNF----KHIIVGE--------PSNGTDIvveyRGSIQ--LDIMCEGTPEHS 174
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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