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Conserved domains on  [gi|612671875|gb|EZS87961|]
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hypothetical protein W470_01590 [Staphylococcus aureus VET0159R]

Protein Classification

M20 peptidase aminoacylase family protein( domain architecture ID 10145373)

M20 peptidase aminoacylase family protein such as Bacillus subtilis N-acetylcysteine deacetylase that probably catalyzes the deacetylation of N-acetylcysteine (NAC) to acetate and cysteine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
M20_Acy1_YxeP-like cd05669
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ...
2-373 0e+00

M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.


:

Pssm-ID: 349919 [Multi-domain]  Cd Length: 371  Bit Score: 626.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   2 GLKDQAVAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDLPLTTGLVAEVGQGPSCIAVRADIDALPIQEFVEQDF 81
Cdd:cd05669    1 AFYQQLIEWRRYLHQHPELSNQEFETTKKIRRWLEEKGIRILDLPLKTGVVAEIGGGGPIIALRADIDALPIEEETGLPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  82 KSENEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGFHNDPSRPIGT 161
Cdd:cd05669   81 ASQNKGVMHACGHDFHTASLLGAAVLLKEREAELKGTVRLIFQPAEETGAGAKKVIEAGALDDVSAIFGFHNKPDLPVGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 162 FAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIADHA 241
Cdd:cd05669  161 IGLKSGALMAAVDRFEIEIAGKGAHAAKPENGVDPIVAASQIINALQTIVSRNISPLESAVVSVTRIHAGNTWNVIPDSA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 242 YVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAIAVAQHVGYKVEMMEQPLTiGED 321
Cdd:cd05669  241 ELEGTVRTFDAEVRQLVKERFEQIVEGIAAAFGAKIEFKWHSGPPAVINDEELTDLASEVAAQAGYEVVHAEPSLG-GED 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 612671875 322 FSGYSQHFPSVFALIGSHSEYDLHHPQYKPDERILEKAPEYFVEFVKRLLHE 373
Cdd:cd05669  320 FAFYQQKIPGVFAFIGSNGTYELHHPAFNPDEEALPVAADYFAELAERLLEH 371
 
Name Accession Description Interval E-value
M20_Acy1_YxeP-like cd05669
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ...
2-373 0e+00

M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.


Pssm-ID: 349919 [Multi-domain]  Cd Length: 371  Bit Score: 626.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   2 GLKDQAVAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDLPLTTGLVAEVGQGPSCIAVRADIDALPIQEFVEQDF 81
Cdd:cd05669    1 AFYQQLIEWRRYLHQHPELSNQEFETTKKIRRWLEEKGIRILDLPLKTGVVAEIGGGGPIIALRADIDALPIEEETGLPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  82 KSENEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGFHNDPSRPIGT 161
Cdd:cd05669   81 ASQNKGVMHACGHDFHTASLLGAAVLLKEREAELKGTVRLIFQPAEETGAGAKKVIEAGALDDVSAIFGFHNKPDLPVGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 162 FAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIADHA 241
Cdd:cd05669  161 IGLKSGALMAAVDRFEIEIAGKGAHAAKPENGVDPIVAASQIINALQTIVSRNISPLESAVVSVTRIHAGNTWNVIPDSA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 242 YVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAIAVAQHVGYKVEMMEQPLTiGED 321
Cdd:cd05669  241 ELEGTVRTFDAEVRQLVKERFEQIVEGIAAAFGAKIEFKWHSGPPAVINDEELTDLASEVAAQAGYEVVHAEPSLG-GED 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 612671875 322 FSGYSQHFPSVFALIGSHSEYDLHHPQYKPDERILEKAPEYFVEFVKRLLHE 373
Cdd:cd05669  320 FAFYQQKIPGVFAFIGSNGTYELHHPAFNPDEEALPVAADYFAELAERLLEH 371
amidohydrolases TIGR01891
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ...
8-359 3.19e-166

amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273857 [Multi-domain]  Cd Length: 363  Bit Score: 468.75  E-value: 3.19e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875    8 VAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILD-LPLTTGLVAEVGQGP--SCIAVRADIDALPIQEFVEQDFKSE 84
Cdd:TIGR01891   2 TDIRRHLHEHPELSFEEFKTSSLIAEALESLGIEVRRgVGGATGVVATIGGGKpgPVVALRADMDALPIQEQTDLPYKST 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   85 NEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGFHNDPSRPIGTFAI 164
Cdd:TIGR01891  82 NPGVMHACGHDLHTAILLGTAKLLKKLADLLEGTVRLIFQPAEEGGGGATKMIEDGVLDDVDAILGLHPDPSIPAGTVGL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  165 KTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIADHAYVQ 244
Cdd:TIGR01891 162 RPGTIMAAADKFEVTIHGKGAHAARPHLGRDALDAAAQLVVALQQIVSRNVDPSRPAVVSVGIIEAGGAPNVIPDKASMS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  245 GTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAIAVAQHVGYKVEMMEQPLTI--GEDF 322
Cdd:TIGR01891 242 GTVRSLDPEVRDQIIDRIERIVEGAAAMYGAKVELNYDRGLPAVTNDPALTQILKEVARHVVGPENVAEDPEVTmgSEDF 321
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 612671875  323 SGYSQHFPSVFALIGSHSE-----YDLHHPQYKPDERILEKA 359
Cdd:TIGR01891 322 AYYSQKVPGAFFFLGIGNEgtglsHPLHHPRFDIDEEALALG 363
AbgB COG1473
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ...
3-371 8.42e-159

Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441082 [Multi-domain]  Cd Length: 386  Bit Score: 450.72  E-value: 8.42e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   3 LKDQAVAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDLPLTTGLVAEVGQGPS--CIAVRADIDALPIQEFVEQD 80
Cdd:COG1473    9 LAPELIALRRDLHAHPELSFEEFRTAAYVAEELRELGIEVTTGVGGTGVVAVLKGGKPgpTIALRADMDALPIQEQTGLP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  81 FKSENEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETHALK--DVQAVLGFHNDPSRP 158
Cdd:COG1473   89 YASKNPGVMHACGHDGHTAMLLGAAKALAELRDELKGTVRLIFQPAEEGGGGAKAMIEDGLLDrpDVDAIFGLHVWPGLP 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 159 IGTFAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIA 238
Cdd:COG1473  169 VGTIGVRPGPIMAAADSFEITIKGKGGHAAAPHLGIDPIVAAAQIVTALQTIVSRNVDPLDPAVVTVGIIHGGTAPNVIP 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 239 DHAYVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAIAVAQHV--GYKVEMMEqPL 316
Cdd:COG1473  249 DEAELEGTVRTFDPEVRELLEERIERIAEGIAAAYGATAEVEYLRGYPPTVNDPELTELAREAAREVlgEENVVDAE-PS 327
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 612671875 317 TIGEDFSGYSQHFPSVFALIGSHSE---YDLHHPQYKPDERILEKAPEYFVEFVKRLL 371
Cdd:COG1473  328 MGSEDFAYYLQKVPGAFFFLGAGNPgtvPPLHSPKFDFDEKALPIGAKALAALALDLL 385
carboxypep_CpsA NF040868
carboxypeptidase CpsA;
3-356 5.53e-85

carboxypeptidase CpsA;


Pssm-ID: 468805 [Multi-domain]  Cd Length: 391  Bit Score: 263.13  E-value: 5.53e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   3 LKDQAVAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILD-LPLTTGLVAEV--GQGPSCIAVRADIDALPIQEFVEQ 79
Cdd:NF040868  11 IEDKIIEIRRKIHENPELSYQEYRTAKLVAETLRSLGIEVREgVGLPTAVVGILrgKKKGKTVALRADMDALPVQEETDL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  80 DFKSENEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGY--GAFKIIETHALKDVQAVLGFHNDPSR 157
Cdd:NF040868  91 PFKSKVPGVMHACGHDAHVAMLLGAAYILSKHKDELSGEVRLIFQPAEEDGGrgGAKPMIEAGVMEGVDYVFGLHVSSSY 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 158 PIGTFAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVI 237
Cdd:NF040868 171 PSGVFATRKGPLMAAPDSFKVEVHGKGGHGSAPHETIDPIFISAQIVNALQGIRSRQIDPLQPFVLSVTSIHSGTKDNII 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 238 ADHAYVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAV-MNDEALTHKAIAVAQHVGYKVEMMEQPL 316
Cdd:NF040868 251 PDEAVMEGTIRTLDEDVREKALEYMRNIVESICEAYGAECKVEFKEDAYPVtVNDPETTKEVMDILSEIPGVKVVETDPV 330
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 612671875 317 TIGEDFSGYSQHFPSVFALIGSHSE-----YDLHHPQYKPDERIL 356
Cdd:NF040868 331 LGAEDFSRFLQKAPGTFIFLGTRNEkkgiiYPNHSSKFTVDEDVL 375
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
63-369 2.74e-76

Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.


Pssm-ID: 460247 [Multi-domain]  Cd Length: 315  Bit Score: 238.02  E-value: 2.74e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   63 AVRADIDALPIQEFVEQDFKSENEGVMHACGHDIHMASILATAVKLKEI--EGTLTGRVKFIFQPAEELGY-GAFKIIET 139
Cdd:pfam01546   1 LLRGHMDVVPDEETWGWPFKSTEDGKLYGRGHDDMKGGLLAALEALRALkeEGLKKGTVKLLFQPDEEGGMgGARALIED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  140 HALK--DVQAVLGFHN-DPSRPIGTFAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLS 216
Cdd:pfam01546  81 GLLEreKVDAVFGLHIgEPTLLEGGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSRNVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  217 AFDEAVVTIGQISC-GNTWNVIADHAYVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYT-HLPGAVMNDEAL 294
Cdd:pfam01546 161 PLDPAVVTVGNITGiPGGVNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEYVeGGAPPLVNDSPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  295 THKAIAVAQHV-GYKVEMMEQPLTIGEDFSGYSQHFPSVFALIG-----SHSeydlHHPQYkpDERILEKAPEYFVEFVK 368
Cdd:pfam01546 241 VAALREAAKELfGLKVELIVSGSMGGTDAAFFLLGVPPTVVFFGpgsglAHS----PNEYV--DLDDLEKGAKVLARLLL 314

                  .
gi 612671875  369 R 369
Cdd:pfam01546 315 K 315
PLN02693 PLN02693
IAA-amino acid hydrolase
5-362 5.79e-63

IAA-amino acid hydrolase


Pssm-ID: 178296 [Multi-domain]  Cd Length: 437  Bit Score: 207.60  E-value: 5.79e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   5 DQAVAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDLPLTTGLVAEVGQG-PSCIAVRADIDALPIQEFVEQDFKS 83
Cdd:PLN02693  47 DWMVRIRRKIHENPELGYEEFETSKLIRSELDLIGIKYRYPVAITGIIGYIGTGePPFVALRADMDALPIQEAVEWEHKS 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  84 ENEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGFHNDPSRPIGTFA 163
Cdd:PLN02693 127 KIPGKMHACGHDGHVAMLLGAAKILQEHRHHLQGTVVLIFQPAEEGLSGAKKMREEGALKNVEAIFGIHLSPRTPFGKAA 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 164 IKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIADHAYV 243
Cdd:PLN02693 207 SRAGSFMAGAGVFEAVITGKGGHAAIPQHTIDPVVAASSIVLSLQQLVSRETDPLDSKVVTVSKVNGGNAFNVIPDSITI 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 244 QGTVRSFDPVVRklVETRLQDIADGLAQAYNMKINLNYT-----HLPGAVMNDEALTHKAIAVAQHVGYKVEMMEQPLTI 318
Cdd:PLN02693 287 GGTLRAFTGFTQ--LQQRIKEIITKQAAVHRCNASVNLTpngrePMPPTVNNMDLYKQFKKVVRDLLGQEAFVEAAPEMG 364
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 612671875 319 GEDFSGYSQHFPSVFALIGSHSEYDLHHPQYKPDERILEKAPEY 362
Cdd:PLN02693 365 SEDFSYFAETIPGHFSLLGMQDETNGYASSHSPLYRINEDVLPY 408
 
Name Accession Description Interval E-value
M20_Acy1_YxeP-like cd05669
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ...
2-373 0e+00

M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.


Pssm-ID: 349919 [Multi-domain]  Cd Length: 371  Bit Score: 626.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   2 GLKDQAVAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDLPLTTGLVAEVGQGPSCIAVRADIDALPIQEFVEQDF 81
Cdd:cd05669    1 AFYQQLIEWRRYLHQHPELSNQEFETTKKIRRWLEEKGIRILDLPLKTGVVAEIGGGGPIIALRADIDALPIEEETGLPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  82 KSENEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGFHNDPSRPIGT 161
Cdd:cd05669   81 ASQNKGVMHACGHDFHTASLLGAAVLLKEREAELKGTVRLIFQPAEETGAGAKKVIEAGALDDVSAIFGFHNKPDLPVGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 162 FAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIADHA 241
Cdd:cd05669  161 IGLKSGALMAAVDRFEIEIAGKGAHAAKPENGVDPIVAASQIINALQTIVSRNISPLESAVVSVTRIHAGNTWNVIPDSA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 242 YVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAIAVAQHVGYKVEMMEQPLTiGED 321
Cdd:cd05669  241 ELEGTVRTFDAEVRQLVKERFEQIVEGIAAAFGAKIEFKWHSGPPAVINDEELTDLASEVAAQAGYEVVHAEPSLG-GED 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 612671875 322 FSGYSQHFPSVFALIGSHSEYDLHHPQYKPDERILEKAPEYFVEFVKRLLHE 373
Cdd:cd05669  320 FAFYQQKIPGVFAFIGSNGTYELHHPAFNPDEEALPVAADYFAELAERLLEH 371
amidohydrolases TIGR01891
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ...
8-359 3.19e-166

amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273857 [Multi-domain]  Cd Length: 363  Bit Score: 468.75  E-value: 3.19e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875    8 VAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILD-LPLTTGLVAEVGQGP--SCIAVRADIDALPIQEFVEQDFKSE 84
Cdd:TIGR01891   2 TDIRRHLHEHPELSFEEFKTSSLIAEALESLGIEVRRgVGGATGVVATIGGGKpgPVVALRADMDALPIQEQTDLPYKST 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   85 NEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGFHNDPSRPIGTFAI 164
Cdd:TIGR01891  82 NPGVMHACGHDLHTAILLGTAKLLKKLADLLEGTVRLIFQPAEEGGGGATKMIEDGVLDDVDAILGLHPDPSIPAGTVGL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  165 KTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIADHAYVQ 244
Cdd:TIGR01891 162 RPGTIMAAADKFEVTIHGKGAHAARPHLGRDALDAAAQLVVALQQIVSRNVDPSRPAVVSVGIIEAGGAPNVIPDKASMS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  245 GTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAIAVAQHVGYKVEMMEQPLTI--GEDF 322
Cdd:TIGR01891 242 GTVRSLDPEVRDQIIDRIERIVEGAAAMYGAKVELNYDRGLPAVTNDPALTQILKEVARHVVGPENVAEDPEVTmgSEDF 321
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 612671875  323 SGYSQHFPSVFALIGSHSE-----YDLHHPQYKPDERILEKA 359
Cdd:TIGR01891 322 AYYSQKVPGAFFFLGIGNEgtglsHPLHHPRFDIDEEALALG 363
AbgB COG1473
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ...
3-371 8.42e-159

Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441082 [Multi-domain]  Cd Length: 386  Bit Score: 450.72  E-value: 8.42e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   3 LKDQAVAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDLPLTTGLVAEVGQGPS--CIAVRADIDALPIQEFVEQD 80
Cdd:COG1473    9 LAPELIALRRDLHAHPELSFEEFRTAAYVAEELRELGIEVTTGVGGTGVVAVLKGGKPgpTIALRADMDALPIQEQTGLP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  81 FKSENEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETHALK--DVQAVLGFHNDPSRP 158
Cdd:COG1473   89 YASKNPGVMHACGHDGHTAMLLGAAKALAELRDELKGTVRLIFQPAEEGGGGAKAMIEDGLLDrpDVDAIFGLHVWPGLP 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 159 IGTFAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIA 238
Cdd:COG1473  169 VGTIGVRPGPIMAAADSFEITIKGKGGHAAAPHLGIDPIVAAAQIVTALQTIVSRNVDPLDPAVVTVGIIHGGTAPNVIP 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 239 DHAYVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAIAVAQHV--GYKVEMMEqPL 316
Cdd:COG1473  249 DEAELEGTVRTFDPEVRELLEERIERIAEGIAAAYGATAEVEYLRGYPPTVNDPELTELAREAAREVlgEENVVDAE-PS 327
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 612671875 317 TIGEDFSGYSQHFPSVFALIGSHSE---YDLHHPQYKPDERILEKAPEYFVEFVKRLL 371
Cdd:COG1473  328 MGSEDFAYYLQKVPGAFFFLGAGNPgtvPPLHSPKFDFDEKALPIGAKALAALALDLL 385
M20_Acy1 cd03886
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ...
8-367 3.48e-137

M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.


Pssm-ID: 349882 [Multi-domain]  Cd Length: 371  Bit Score: 395.43  E-value: 3.48e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   8 VAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDLPLTTGLVAEV-GQGPS-CIAVRADIDALPIQEFVEQDFKSEN 85
Cdd:cd03886    2 IALRRDLHQHPELSFEEFRTAARIAEELRELGLEVRTGVGGTGVVATLkGGGPGpTVALRADMDALPIQEETGLPFASKH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  86 EGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETHALK--DVQAVLGFHNDPSRPIGTFA 163
Cdd:cd03886   82 EGVMHACGHDGHTAMLLGAAKLLAERRDPLKGTVRFIFQPAEEGPGGAKAMIEEGVLEnpGVDAAFGLHVWPGLPVGTVG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 164 IKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIADHAYV 243
Cdd:cd03886  162 VRSGALMASADEFEITVKGKGGHGASPHLGVDPIVAAAQIVLALQTVVSRELDPLEPAVVTVGKFHAGTAFNVIPDTAVL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 244 QGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAIAVAQHV-GYKVEMMEQPLTIGEDF 322
Cdd:cd03886  242 EGTIRTFDPEVREALEARIKRLAEGIAAAYGATVELEYGYGYPAVINDPELTELVREAAKELlGEEAVVEPEPVMGSEDF 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 612671875 323 SGYSQHFPSVFALIGS----HSEYDLHHPQYKPDERILEKAPEYFVEFV 367
Cdd:cd03886  322 AYYLEKVPGAFFWLGAgepdGENPGLHSPTFDFDEDALPIGAALLAELA 370
M20_Acy1_YhaA-like cd08021
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ...
2-370 3.71e-124

M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.


Pssm-ID: 349941 [Multi-domain]  Cd Length: 384  Bit Score: 362.75  E-value: 3.71e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   2 GLKDQAVAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDL-PLTTGLVAEVGQGPS-CIAVRADIDALPIQEFVEQ 79
Cdd:cd08021    7 QLEDEMIQWRRHIHQYPELSFEEFETAAYIANELKKLGLEVETNvGGTGVVATLKGGKPGkTVALRADMDALPIEEETDL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  80 DFKSENEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFK-IIETHALKDVQAVLGFHNDPSRP 158
Cdd:cd08021   87 PFKSKNPGVMHACGHDGHTAMLLGAAKVLAENKDEIKGTVRFIFQPAEEVPPGGAKpMIEAGVLEGVDAVFGLHLWSTLP 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 159 IGTFAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIA 238
Cdd:cd08021  167 TGTIAVRPGAIMAAPDEFDITIKGKGGHGSMPHETVDPIVIAAQIVTALQTIVSRRVDPLDPAVVTIGTFQGGTSFNVIP 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 239 DHAYVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAIAVAQHVGYKVEMME-QPLT 317
Cdd:cd08021  247 DTVELKGTVRTFDEEVREQVPKRIERIVKGICEAYGASYELEYQPGYPVVYNDPEVTELVKKAAKEVLIGVENVEpQLMM 326
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 612671875 318 IGEDFSGYSQHFPSVFALIGSHSE-----YDLHHPQYKPDERILEKAPEYFVEFVKRL 370
Cdd:cd08021  327 GGEDFSYYLKEVPGCFFFLGAGNEekgciYPHHSPKFDIDESALKIGVKVHVGAVLEL 384
M20_Acy1-like cd05666
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ...
5-369 1.99e-120

M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).


Pssm-ID: 349916 [Multi-domain]  Cd Length: 373  Bit Score: 352.99  E-value: 1.99e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   5 DQAVAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDLPLTTGLVA--EVGQGPSCIAVRADIDALPIQEFVEQDFK 82
Cdd:cd05666    1 DELTAWRRDLHAHPELGFEEHRTSALVAEKLREWGIEVHRGIGGTGVVGvlRGGDGGRAIGLRADMDALPIQEATGLPYA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  83 SENEGVMHACGHDIHMASILATAVKLKEiEGTLTGRVKFIFQPAEELGYGAFKIIETHALK--DVQAVLGFHNDPSRPIG 160
Cdd:cd05666   81 STHPGKMHACGHDGHTTMLLGAARYLAE-TRNFDGTVHFIFQPAEEGGGGAKAMIEDGLFErfPCDAVYGLHNMPGLPAG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 161 TFAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIADH 240
Cdd:cd05666  160 KFAVRPGPMMASADTFEITIRGKGGHAAMPHLGVDPIVAAAQLVQALQTIVSRNVDPLDAAVVSVTQIHAGDAYNVIPDT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 241 AYVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAIAVAQHV--GYKVEMMEQPLTI 318
Cdd:cd05666  240 AELRGTVRAFDPEVRDLIEERIREIADGIAAAYGATAEVDYRRGYPVTVNDAEETAFAAEVAREVvgAENVDTDVRPSMG 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 612671875 319 GEDFSGYSQHFPSVFALIGSHSEYD---LHHPQYKPDERILEKAPEYFVEFVKR 369
Cdd:cd05666  320 SEDFAFMLEARPGAYVFLGNGDGEGgcpLHNPGYDFNDAILPIGASYWVRLVER 373
M20_Acy1-like cd08014
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ...
8-356 5.40e-109

M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of uncharacterized bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).


Pssm-ID: 349936 [Multi-domain]  Cd Length: 371  Bit Score: 323.84  E-value: 5.40e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   8 VAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDLPLTTGLVAEVG--QGPSCIAVRADIDALPIQEFVEQDFKSEN 85
Cdd:cd08014    2 VEWRRHLHAHPELSGQEYRTTAFVAERLRDLGLKPKEFPGGTGLVCDIGgkRDGRTVALRADMDALPIQEQTGLPYRSTV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  86 EGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELG-YGAFKIIETHALKDVQAVLGFHNDPSRPIGTFAI 164
Cdd:cd08014   82 PGVMHACGHDAHTAIALGAALVLAALEEELPGRVRLIFQPAEETMpGGALDMIRAGALDGVSAIFALHVDPRLPVGRVGV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 165 KTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIADHAYVQ 244
Cdd:cd08014  162 RYGPITAAADSLEIRIQGEGGHGARPHLTVDLVWAAAQVVTDLPQAISRRIDPRSPVVLTWGSIEGGRAPNVIPDSVELS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 245 GTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAIAVAQHVG---YKVEMMEQPLTiGED 321
Cdd:cd08014  242 GTVRTLDPDTWAQLPDLVEEIVAGICAPYGAKYELEYRRGVPPVINDPASTALLEAAVREILgedNVVALAEPSMG-GED 320
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 612671875 322 FSGYSQHFPSVFALIGSHS----EYDLHHPQYKPDERIL 356
Cdd:cd08014  321 FAWYLEHVPGAMARLGVWGgdgtSYPLHHPDFDVDERAI 359
M20_Acy1-like cd08019
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ...
7-367 5.46e-108

M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).


Pssm-ID: 349940 [Multi-domain]  Cd Length: 372  Bit Score: 321.21  E-value: 5.46e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   7 AVAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDlPLTTGLVAEV-GQGPS-CIAVRADIDALPIQEFVEQDFKSE 84
Cdd:cd08019    1 IIELRRYFHMHPELSLKEERTSKRIKEELDKLGIPYVE-TGGTGVIATIkGGKAGkTVALRADIDALPVEECTDLEYKSK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  85 NEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGFHNDPSRPIGTFAI 164
Cdd:cd08019   80 NPGLMHACGHDGHTAMLLGAAKILNEIKDTIKGTVKLIFQPAEEVGEGAKQMIEEGVLEDVDAVFGIHLWSDVPAGKISV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 165 KTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIADHAYVQ 244
Cdd:cd08019  160 EAGPRMASADIFKIEVKGKGGHGSMPHQGIDAVLAAASIVMNLQSIVSREIDPLEPVVVTVGKLNSGTRFNVIADEAKIE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 245 GTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAIAVAQHV--GYKVEMMEQPlTIGEDF 322
Cdd:cd08019  240 GTLRTFNPETREKTPEIIERIAKHTAASYGAEAELTYGAATPPVINDEKLSKIARQAAIKIfgEDSLTEFEKT-TGSEDF 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 612671875 323 SGYSQHFPSVFALIGSHSE-----YDLHHPQYKPDERILEKAPEYFVEFV 367
Cdd:cd08019  319 SYYLEEVPGVFAFVGSRNEekgatYPHHHEFFNIDEDALKLGAALYVQFA 368
M20_Acy1_YkuR-like cd05670
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ...
6-371 1.85e-104

M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.


Pssm-ID: 349920 [Multi-domain]  Cd Length: 367  Bit Score: 311.89  E-value: 1.85e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   6 QAVAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDL--PLTTGLVAEV-GQGPS-CIAVRADIDALPIQEFVEQDF 81
Cdd:cd05670    1 ELIKIRRDLHQIPELGLEEFKTQAYLLDVIAKLPQDNLEIktWCETGILVYVeGSNPErTIGYRADIDALPIEEETGLPF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  82 KSENEGVMHACGHDIHMASILATAVKLKEIEgtLTGRVKFIFQPAEELGYGAFKIIETHALKDVQA--VLGFHNDPSRPI 159
Cdd:cd05670   81 ASKHPGVMHACGHDGHMTIALGLLEYFAQHQ--PKDNLLFIFQPAEEGPGGAKRMYESGVFGKWRPdeIYGLHVNPDLPV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 160 GTFAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIAD 239
Cdd:cd05670  159 GTIATRSGTLFAGTSELHIDFIGKSGHAAYPHNANDMVVAAANFVTQLQTIVSRNVDPIDGAVVTIGKIHAGTARNVIAG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 240 HAYVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAI-AVAQHVGYKVEMMEqPLTI 318
Cdd:cd05670  239 TAHLEGTIRTLTQEMMELVKQRVRDIAEGIELAFDCEVKVDLGQGYYPVENDPDLTTEFIdFMKKADGVNFVEAE-PAMT 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 612671875 319 GEDFSGYSQHFPSVFALIGSHSEYDLHHPQYKPDERILEKApeyfVEFVKRLL 371
Cdd:cd05670  318 GEDFGYLLKKIPGTMFWLGVDSPYGLHSATLNPDEEAILFG----VNAYKGFL 366
M20_IAA_Hyd cd08017
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant ...
8-356 7.20e-97

M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.


Pssm-ID: 349938 [Multi-domain]  Cd Length: 376  Bit Score: 293.07  E-value: 7.20e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   8 VAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRiLDLPLT-TGLVAEVGQG-PSCIAVRADIDALPIQEFVEQDFKSEN 85
Cdd:cd08017    2 VRVRREIHENPELAFQEHETSALIRRELDALGIP-YRYPVAkTGIVATIGSGsPPVVALRADMDALPIQELVEWEHKSKV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  86 EGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGFHNDPSRPIGTFAIK 165
Cdd:cd08017   81 DGKMHACGHDAHVAMLLGAAKLLKARKHLLKGTVRLLFQPAEEGGAGAKEMIKEGALDDVEAIFGMHVSPALPTGTIASR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 166 TGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIADHAYVQG 245
Cdd:cd08017  161 PGPFLAGAGRFEVVIRGKGGHAAMPHHTVDPVVAASSAVLALQQLVSRETDPLDSQVVSVTRFNGGHAFNVIPDSVTFGG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 246 TVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYT--HLP--GAVMNDEALTHKAIAVAQHVG--YKVEMMEqPLTIG 319
Cdd:cd08017  241 TLRALTTEGFYRLRQRIEEVIEGQAAVHRCNATVDFSedERPpyPPTVNDERMYEHAKKVAADLLgpENVKIAP-PVMGA 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 612671875 320 EDFSGYSQHFPSVFALIGSHSE-----YDLHHPQYKPDERIL 356
Cdd:cd08017  320 EDFAFYAEKIPAAFFFLGIRNEtagsvHSLHSPYFFLDEEVL 361
M20_Acy1-like cd08660
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ...
11-365 3.08e-86

M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1L2 family contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay.


Pssm-ID: 349945 [Multi-domain]  Cd Length: 366  Bit Score: 265.64  E-value: 3.08e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  11 RRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDLP-LTTGLVAEVGQG--PSCIAVRADIDALPIQEFVEQDFKSENEG 87
Cdd:cd08660    5 RRDIHEHPELGFEEVETSKKIRRWLEEEQIEILDVPqLKTGVIAEIKGGedGPVIAIRADIDALPIQEQTNLPFASKVDG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  88 VMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGFHNDPSRPIGTFAIKTG 167
Cdd:cd08660   85 T*HACGHDFHTTSIIGTA*LLNQRRAELKGTVVFIFQPAEEGAAGARKVLEAGVLNGVSAIFGIHNKPDLPVGTIGVKEG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 168 AITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIADHAYVQGTV 247
Cdd:cd08660  165 PL*ASVDVFEIVIKGKGGHASIPNNSIDPIAAAGQIISGLQSVVSRNISSLQNAVVSITRVQGGTAWNVIPDQAE*EGTV 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 248 RSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYT-HLPGAVMNDEALTHKAIAVAQHVGYKVeMMEQPLTIGEDFSGYS 326
Cdd:cd08660  245 RAFTKEARQAVPEH*RRVAEGIAAGYGCQAEFKWFpNGPSEVQNDGTLLNAFSKAAARLGYAT-VHAEQSPGSEDFALYQ 323
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 612671875 327 QHFPSVFALIGSHSEYDL-HHPQYKPDERILEKAPEYFVE 365
Cdd:cd08660  324 EKIPGFFVW*GTNGRTEEwHHPAFRLDEEALTVGAQIFAE 363
M20_Acy1-like cd05667
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ...
3-367 2.44e-85

M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins that have been predicted as N-acyl-L-amino acid amidohydrolase (amaA), thermostable carboxypeptidase (cpsA-1, cpsA-2 in Sulfolobus solfataricus) and abgB (aminobenzoyl-glutamate utilization protein B), and generally are involved in the urea cycle and metabolism of amino groups. Aminoacylases 1 (ACY1s) comprise a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and is a highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).


Pssm-ID: 349917 [Multi-domain]  Cd Length: 403  Bit Score: 264.29  E-value: 2.44e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   3 LKDQAVAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDLPLTTGLVA--EVGQGPSCIAVRADIDALPIQEFVEQD 80
Cdd:cd05667    8 VEPKVIEWRRDFHQNPELSNREFRTAALIAKELKSLGIEVRTGIAKTGVVGilKGGKPGPVIALRADMDALPVEEKTGLP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  81 FKSENE--------GVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELG-----YGAFKIIETHALKD--V 145
Cdd:cd05667   88 FASKVKttylgqtvGVMHACGHDAHVAILLGAAEVLAANKDKIKGTVMFIFQPAEEGPpegeeGGAKLMLKEGAFKDykP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 146 QAVLGFHNDPSRPIGTFAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDE-AVVT 224
Cdd:cd05667  168 EAIFGLHVGSGLPSGQLGYRSGPIMASADRFRITVKGKQTHGSRPWDGIDPIMASAQIIQGLQTIISRRIDLTKEpAVIS 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 225 IGQISCGNTWNVIADHAYVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAIAVAQH 304
Cdd:cd05667  248 IGKINGGTRGNIIPEDAEMVGTIRTFDPEMREDIFARLKTIAEHIAKAYGATAEVEFANGYPVTYNDPALTAKMLPTLQK 327
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612671875 305 VGYKVEMMEQP--LTIGEDFSGYSQHFPSVFALIGSHSE-YDL------HHPQYKPDERILEKAPEYFVEFV 367
Cdd:cd05667  328 AVGKADLVVLPptQTGAEDFSFYAEQVPGMFFFLGGTPAgQEPatappnHSPYFIVDESALKTGVKAHIQLV 399
carboxypep_CpsA NF040868
carboxypeptidase CpsA;
3-356 5.53e-85

carboxypeptidase CpsA;


Pssm-ID: 468805 [Multi-domain]  Cd Length: 391  Bit Score: 263.13  E-value: 5.53e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   3 LKDQAVAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILD-LPLTTGLVAEV--GQGPSCIAVRADIDALPIQEFVEQ 79
Cdd:NF040868  11 IEDKIIEIRRKIHENPELSYQEYRTAKLVAETLRSLGIEVREgVGLPTAVVGILrgKKKGKTVALRADMDALPVQEETDL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  80 DFKSENEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGY--GAFKIIETHALKDVQAVLGFHNDPSR 157
Cdd:NF040868  91 PFKSKVPGVMHACGHDAHVAMLLGAAYILSKHKDELSGEVRLIFQPAEEDGGrgGAKPMIEAGVMEGVDYVFGLHVSSSY 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 158 PIGTFAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVI 237
Cdd:NF040868 171 PSGVFATRKGPLMAAPDSFKVEVHGKGGHGSAPHETIDPIFISAQIVNALQGIRSRQIDPLQPFVLSVTSIHSGTKDNII 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 238 ADHAYVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAV-MNDEALTHKAIAVAQHVGYKVEMMEQPL 316
Cdd:NF040868 251 PDEAVMEGTIRTLDEDVREKALEYMRNIVESICEAYGAECKVEFKEDAYPVtVNDPETTKEVMDILSEIPGVKVVETDPV 330
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 612671875 317 TIGEDFSGYSQHFPSVFALIGSHSE-----YDLHHPQYKPDERIL 356
Cdd:NF040868 331 LGAEDFSRFLQKAPGTFIFLGTRNEkkgiiYPNHSSKFTVDEDVL 375
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
63-369 2.74e-76

Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.


Pssm-ID: 460247 [Multi-domain]  Cd Length: 315  Bit Score: 238.02  E-value: 2.74e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   63 AVRADIDALPIQEFVEQDFKSENEGVMHACGHDIHMASILATAVKLKEI--EGTLTGRVKFIFQPAEELGY-GAFKIIET 139
Cdd:pfam01546   1 LLRGHMDVVPDEETWGWPFKSTEDGKLYGRGHDDMKGGLLAALEALRALkeEGLKKGTVKLLFQPDEEGGMgGARALIED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  140 HALK--DVQAVLGFHN-DPSRPIGTFAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLS 216
Cdd:pfam01546  81 GLLEreKVDAVFGLHIgEPTLLEGGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSRNVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  217 AFDEAVVTIGQISC-GNTWNVIADHAYVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYT-HLPGAVMNDEAL 294
Cdd:pfam01546 161 PLDPAVVTVGNITGiPGGVNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEYVeGGAPPLVNDSPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  295 THKAIAVAQHV-GYKVEMMEQPLTIGEDFSGYSQHFPSVFALIG-----SHSeydlHHPQYkpDERILEKAPEYFVEFVK 368
Cdd:pfam01546 241 VAALREAAKELfGLKVELIVSGSMGGTDAAFFLLGVPPTVVFFGpgsglAHS----PNEYV--DLDDLEKGAKVLARLLL 314

                  .
gi 612671875  369 R 369
Cdd:pfam01546 315 K 315
M20_Acy1-like cd05664
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ...
12-337 6.53e-72

M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).


Pssm-ID: 349914 [Multi-domain]  Cd Length: 399  Bit Score: 229.53  E-value: 6.53e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  12 RYFHQFPELSDKEFKTTQKIKDilteyHIRILDLPLT-----TGLVAEV--GQGPScIAVRADIDALPIQEFVEQDFKSE 84
Cdd:cd05664    8 KDFHAHPELSFQEHRTAAKIAE-----ELRKLGFEVTtgiggTGVVAVLrnGEGPT-VLLRADMDALPVEENTGLPYAST 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  85 NE---------GVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETH-----ALKDVqaVLG 150
Cdd:cd05664   82 VRmkdwdgkevPVMHACGHDMHVAALLGAARLLVEAKDAWSGTLIAVFQPAEETGGGAQAMVDDGlydkiPKPDV--VLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 151 FHNDPSrPIGTFAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISC 230
Cdd:cd05664  160 QHVMPG-PAGTVGTRPGRFLSAADSLDITIFGRGGHGSMPHLTIDPVVMAASIVTRLQTIVSREVDPQEFAVVTVGSIQA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 231 GNTWNVIADHAYVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPG--AVMNDEALTHK-AIAVAQHVGY 307
Cdd:cd05664  239 GSAENIIPDEAELKLNVRTFDPEVREKVLNAIKRIVRAECAASGAPKPPEFTYTDSfpATVNDEDATARlAAAFREYFGE 318
                        330       340       350
                 ....*....|....*....|....*....|..
gi 612671875 308 KVEMMEQPLTIGEDFS--GYSQHFPSVFALIG 337
Cdd:cd05664  319 DRVVEVPPVSASEDFSilATAFGVPSVFWFIG 350
PLN02693 PLN02693
IAA-amino acid hydrolase
5-362 5.79e-63

IAA-amino acid hydrolase


Pssm-ID: 178296 [Multi-domain]  Cd Length: 437  Bit Score: 207.60  E-value: 5.79e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   5 DQAVAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDLPLTTGLVAEVGQG-PSCIAVRADIDALPIQEFVEQDFKS 83
Cdd:PLN02693  47 DWMVRIRRKIHENPELGYEEFETSKLIRSELDLIGIKYRYPVAITGIIGYIGTGePPFVALRADMDALPIQEAVEWEHKS 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  84 ENEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGFHNDPSRPIGTFA 163
Cdd:PLN02693 127 KIPGKMHACGHDGHVAMLLGAAKILQEHRHHLQGTVVLIFQPAEEGLSGAKKMREEGALKNVEAIFGIHLSPRTPFGKAA 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 164 IKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIADHAYV 243
Cdd:PLN02693 207 SRAGSFMAGAGVFEAVITGKGGHAAIPQHTIDPVVAASSIVLSLQQLVSRETDPLDSKVVTVSKVNGGNAFNVIPDSITI 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 244 QGTVRSFDPVVRklVETRLQDIADGLAQAYNMKINLNYT-----HLPGAVMNDEALTHKAIAVAQHVGYKVEMMEQPLTI 318
Cdd:PLN02693 287 GGTLRAFTGFTQ--LQQRIKEIITKQAAVHRCNASVNLTpngrePMPPTVNNMDLYKQFKKVVRDLLGQEAFVEAAPEMG 364
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 612671875 319 GEDFSGYSQHFPSVFALIGSHSEYDLHHPQYKPDERILEKAPEY 362
Cdd:PLN02693 365 SEDFSYFAETIPGHFSLLGMQDETNGYASSHSPLYRINEDVLPY 408
M20_Acy1_amhX-like cd08018
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ...
3-367 2.23e-59

M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).


Pssm-ID: 349939 [Multi-domain]  Cd Length: 365  Bit Score: 195.96  E-value: 2.23e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   3 LKDQAVAWRRYFHQFPELSDKEFKTTQKIKDILTEYHIRILDLPLTTGLVAEVGQGPS--CIAVRADIDALPiQEfVEQD 80
Cdd:cd08018    2 LKERIVEVFTHLHQIPEISWEEYKTTEYLAKKLEEMGFRVTTFEGGTGVVAEIGSGKPgpVVALRADMDALW-QE-VDGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  81 FKSenegvMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGFHNDPSR--P 158
Cdd:cd08018   80 FKA-----NHSCGHDAHMTMVLGAAELLKKIGLVKKGKLKFLFQPAEEKGTGALKMIEDGVLDDVDYLFGVHLRPIQelP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 159 IGTF--AIKTGAITSavdrFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSI-VSRNLSafdeAVVTIGQISCG-NTW 234
Cdd:cd08018  155 FGTAapAIYHGASTF----LEGTIKGKQAHGARPHLGINAIEAASAIVNAVNAIhLDPNIP----WSVKMTKLQAGgEAT 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 235 NVIADHAYVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLN-YTHLPGAVMNDEALTHKAIAVAQHVGyKVEMME 313
Cdd:cd08018  227 NIIPDKAKFALDLRAQSNEAMEELKEKVEHAIEAAAALYGASIEITeKGGMPAAEYDEEAVELMEEAITEVLG-EEKLAG 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 612671875 314 QPLTIG-EDFSGYSQHFPSVFAL---IGSHSEYDLHHPQYKPDERILEKAPEYFVEFV 367
Cdd:cd08018  306 PCVTPGgEDFHFYTKKKPELKATmigLGCGLTPGLHHPNMTFDRDALENGVKILARAV 363
PLN02280 PLN02280
IAA-amino acid hydrolase
8-356 5.29e-57

IAA-amino acid hydrolase


Pssm-ID: 215158 [Multi-domain]  Cd Length: 478  Bit Score: 192.87  E-value: 5.29e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   8 VAW----RRYFHQFPELSDKEFKTTQKIKDILTEYHIRiLDLPLT-TGLVAEVGQG-PSCIAVRADIDALPIQEFVEQDF 81
Cdd:PLN02280  96 VAWlksvRRKIHENPELAFEEYKTSELVRSELDRMGIM-YRYPLAkTGIRAWIGTGgPPFVAVRADMDALPIQEAVEWEH 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  82 KSENEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGFHNDPSRPIGT 161
Cdd:PLN02280 175 KSKVAGKMHACGHDAHVAMLLGAAKILKSREHLLKGTVVLLFQPAEEAGNGAKRMIGDGALDDVEAIFAVHVSHEHPTAV 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 162 FAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIADHA 241
Cdd:PLN02280 255 IGSRPGPLLAGCGFFRAVISGKKGRAGSPHHSVDLILAASAAVISLQGIVSREANPLDSQVVSVTTMDGGNNLDMIPDTV 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 242 YVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLN-----YTHLPGAVMNDEALTHKAIAVAQHVGYKVEMMEQPL 316
Cdd:PLN02280 335 VLGGTFRAFSNTSFYQLLKRIQEVIVEQAGVFRCSATVDffekqNTIYPPTVNNDAMYEHVRKVAIDLLGPANFTVVPPM 414
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 612671875 317 TIGEDFSGYSQHFPSVFALIGSHSE-----YDLHHPQYKPDERIL 356
Cdd:PLN02280 415 MGAEDFSFYSQVVPAAFYYIGIRNEtlgstHTGHSPYFMIDEDVL 459
M20_Acy1-like cd05668
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ...
8-355 1.91e-42

M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial uncharacterized proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).


Pssm-ID: 349918 [Multi-domain]  Cd Length: 371  Bit Score: 151.91  E-value: 1.91e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   8 VAWRRYFHQFPELSDKEFKTTQKIKDILTEYHirildlP--LTTGL----VAEVGQ----GPSCIaVRADIDALPIQEFV 77
Cdd:cd05668    5 STFRHTLHRYPELSGQEKETAKRILAFFEPLS------PdeVLTGLgghgVAFIFEgkaeGPTVL-FRCELDALPIEEEN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  78 EQDFKSENEGVMHACGHDIHMASILATAVKLKEIEGTlTGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGF--HNDP 155
Cdd:cd05668   78 DFAHRSKIQGKSHLCGHDGHMAIVSGLGMELSQNRPQ-KGKVILLFQPAEETGEGAAAVIADPKFKEIQPDFAFalHNLP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 156 SRPIGTFAIKTGAITSAVDRFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSrnlSAFDEAVVTIGQISCGN-TW 234
Cdd:cd05668  157 GLELGQIAVKKGPFNCASRGMIIRLKGRTSHAAHPEAGVSPAEAMAKLIVALPALPD---AMPKFTLVTVIHAKLGEaAF 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 235 NVIADHAYVQGTVRSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAIAVAQHVGYKVEMMEQ 314
Cdd:cd05668  234 GTAPGEATVMATLRAHTNETMEQLVAEAEKLVQQIADAYGLGVSLEYTEVFAATHNHPEAWALGNQAAKNLGLPTKHIRI 313
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 612671875 315 PLTIGEDFSGYSQHFPSVFALIGSHSEY-DLHHPQYK-PDERI 355
Cdd:cd05668  314 PFRWSEDFGQFGSVAKTALFVLGSGEDQpQLHNPDFDfPDELI 356
M20_Acy1_IAAspH cd05665
M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, ...
5-274 1.53e-39

M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, bacterial and archaeal aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.


Pssm-ID: 349915 [Multi-domain]  Cd Length: 415  Bit Score: 145.15  E-value: 1.53e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   5 DQAVAWRRYFHQFPELSDKEFKTTQKIKDILTE--YHIRI----------LDLPLT------------------------ 48
Cdd:cd05665    1 EQLVRWRRDFHRYPESGWTEFRTASLIADYLEElgYELKLgrevinadfrMGLPDDetlaaaferareqgadeellekme 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  49 ---TGLVA--EVGQ-GPScIAVRADIDALPIQEF-------VEQDFKSENEGVMHACGHDIHMASILATAVKLKEIEGTL 115
Cdd:cd05665   81 ggfTGVVAtlDTGRpGPT-IALRFDIDAVDVTESeddshrpFKEGFASRNDGCMHACGHDGHTAIGLGLAHALAQLKDSL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 116 TGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGFHNDPSRPIGTFAIKTGAITsAVDRFEFHIKGVGGHA-AKPEQCN 194
Cdd:cd05665  160 SGTIKLIFQPAEEGVRGARAMAEAGVVDDVDYFLASHIGFGVPSGEVVCGPDNFL-ATTKLDARFTGVSAHAgAAPEDGR 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 195 DPVIVLVQLINSIQSIVSRNLSAfdeAVVTIGQISCGNTWNVIADHAYVQGTVRSFDPVVRKLVETRLQDIADGLAQAYN 274
Cdd:cd05665  239 NALLAAATAALNLHAIPRHGEGA---TRINVGVLGAGEGRNVIPASAELQVETRGETTAINEYMFEQAQRVIKGAATMYG 315
M20_Acy1L2 cd03887
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ...
12-272 1.07e-23

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


Pssm-ID: 349883 [Multi-domain]  Cd Length: 360  Bit Score: 100.73  E-value: 1.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  12 RYFHQFPELSDKEFKTTQKIKDIL------TEYHIRILDlpltTGLVAEVG---QGPsCIAVRADIDALPiqefveqdfk 82
Cdd:cd03887   12 RDIHDNPELGYEEYKAHDLLTDFLeelgfdVTRGAYGLE----TAFRAEYGsgkGGP-TVAFLAEYDALP---------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  83 seneGVMHACGHDIHMASILATAVKLKEI--EGTLTGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGFHndPSrPIG 160
Cdd:cd03887   77 ----GIGHACGHNLIATASVAAALALKAAlkALGLPGTVVVLGTPAEEGGGGKIDLIKAGAFDDVDIALMVH--PG-PKD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 161 TfaikTGAITSAVDRFEFHIKGVGGHAA-KPEQ---CNDPVIVLVQLIN----------SIQSIVSrnlsafdEAvvtiG 226
Cdd:cd03887  150 V----AGPKSLAVSKLRVEFHGKAAHAAaAPWEginALDAAVLAYNNISalrqqlkptvRVHGIIT-------EG----G 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 612671875 227 QIScgntwNVIADHAYVQGTVRSFD-PVVRKLVEtRLQDIADGLAQA 272
Cdd:cd03887  215 KAP-----NIIPDYAEAEFYVRAPTlKELEELTE-RVIACFEGAALA 255
M20_ACY1L2-like cd05672
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 ...
12-272 3.07e-20

M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 family, aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase)-like subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. This subfamily includes Staphylococcus aureus antibiotic resistance factor HmrA that has been shown to participate in methicillin resistance mechanisms in vivo in the presence of beta-lactams. Aminoacylase 1 (ACY1) proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).


Pssm-ID: 349921 [Multi-domain]  Cd Length: 360  Bit Score: 90.70  E-value: 3.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  12 RYFHQFPELSDKEFKTTQKIKDIL------TEYHIRILDlpltTGLVAEVG--QGPsCIAVRADIDALPiqefveqdfks 83
Cdd:cd05672   13 RDIHDNPELGFEEYKAHDLLTDFLeehgftVTRGAYGLE----TAFRAEYGssGGP-TVGFLAEYDALP----------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  84 eneGVMHACGHDIHMASILATAVKLKEI--EGTLTGRVKFIFQPAEELGYGAFKIIETHALKDVQAVLGFHndPSrPIGT 161
Cdd:cd05672   77 ---GIGHACGHNLIATASVAAALALKEAlkALGLPGKVVVLGTPAEEGGGGKIDLIKAGAFDDVDAALMVH--PG-PRDV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 162 faikTGAITSAVDRFEFHIKGVGGHAA-KPEQ---CNDPVIVLVQLIN----------SIQSIVSrnlsafdEAvvtiGQ 227
Cdd:cd05672  151 ----AGVPSLAVDKLTVEFHGKSAHAAaAPWEginALDAAVLAYNAISalrqqlkptwRIHGIIT-------EG----GK 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 612671875 228 IScgntwNVIADHAYVQGTVRSFDPVVRKLVETRLQDIADGLAQA 272
Cdd:cd05672  216 AP-----NIIPDYAEARFYVRAPTRKELEELRERVIACFEGAALA 255
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
98-371 1.42e-18

Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440389 [Multi-domain]  Cd Length: 388  Bit Score: 86.09  E-value: 1.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  98 MASILATAVKLKEIEGTLTGRVKFIFQPAEELG-YGAFKIIETHA-LKDVQAVLGFhnDPSrpiGTFAIKTGAITSAvdR 175
Cdd:COG0624  117 LAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGsPGARALVEELAeGLKADAAIVG--EPT---GVPTIVTGHKGSL--R 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 176 FEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLS--AFDEAVVTIGQISCGNTWNVIADHAYVQGTVRSFDPV 253
Cdd:COG0624  190 FELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDGRAdpLFGRTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGE 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 254 VRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMN-DEALTHKAIAVAQHV-GYKVEMMEQPLTIgeDFSGYSQHF-- 329
Cdd:COG0624  270 DPEEVLAALRALLAAAAPGVEVEVEVLGDGRPPFETPpDSPLVAAARAAIREVtGKEPVLSGVGGGT--DARFFAEALgi 347
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 612671875 330 PSVfaLIGsHSEYDLHHpqyKPDERI----LEKAPEYFVEFVKRLL 371
Cdd:COG0624  348 PTV--VFG-PGDGAGAH---APDEYVelddLEKGARVLARLLERLA 387
M20_Acy1L2_AbgB cd05673
M20 Peptidase Aminoacylase 1-like protein 2 aminobenzoyl-glutamate utilization protein B ...
17-188 5.02e-16

M20 Peptidase Aminoacylase 1-like protein 2 aminobenzoyl-glutamate utilization protein B subfamily; Peptidase M20 family, ACY1L2 aminobenzoyl-glutamate utilization protein B (AbgB) subfamily. This group contains mostly bacterial amidohydrolases, including gene products of abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate is a natural end product of folate catabolism, and its utilization is initiated by the abg region gene product, AbgT, by enabling uptake of its into the cell in a concentration-dependent, saturable manner. It is subsequently cleaved by AbgA and AbgB (sometimes referred to as AbgAB).


Pssm-ID: 349922 [Multi-domain]  Cd Length: 437  Bit Score: 78.88  E-value: 5.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  17 FPELSDKEFKTTQKIKDILTEYHIRILDLP--LTTGLVAEVGQGPSCIAVRADIDALP--IQEFVEQDFKSENEGVM-HA 91
Cdd:cd05673   18 FPELSFEEFRSAALLKEALEEEGFTVERGVagIPTAFVASYGSGGPVIAILGEYDALPglSQEAGVAERKPVEPGANgHG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  92 CGHD-IHMASILA-TAVKlKEIEGT-LTGRVKFIFQPAEELGYG-AFKIIEThALKDVQAVLGFHndPSRPIGTFAIKTG 167
Cdd:cd05673   98 CGHNlLGTGSLGAaIAVK-DYMEENnLAGTVRFYGCPAEEGGSGkTFMVRDG-VFDDVDAAISWH--PASFNGVWSTSSL 173
                        170       180
                 ....*....|....*....|.
gi 612671875 168 AITSAVdrfeFHIKGVGGHAA 188
Cdd:cd05673  174 ANISVK----FKFKGISAHAA 190
M20_Acy1L2-like cd09849
M20 Peptidase aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ...
4-128 4.35e-15

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


Pssm-ID: 349947 [Multi-domain]  Cd Length: 389  Bit Score: 75.98  E-value: 4.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875   4 KDQAVAWRRYFHQFPELSDKEFKTTQKIKDIL-TEYHIRILDLPLTTGLVA---EVGQGPScIAVRADIDALPIQEFVEQ 79
Cdd:cd09849    4 KEKIIAIGQTIYDNPELGYKEFKTTETVADFFkNLLNLDVEKNIASTGCRAtlnGDKKGPN-IAVLGELDAISCPEHPDA 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 612671875  80 DfksENEGVMHACGHDIHMASILATAVKLKE--IEGTLTGRVKFIFQPAEE 128
Cdd:cd09849   83 N---EATGAAHACGHNIQIAGMLGAAVALFKsgVYEELDGKLTFIATPAEE 130
M20_ArgE_DapE-like cd08659
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ...
98-306 6.56e-13

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: 69.25  E-value: 6.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  98 MASILATAVKLKEIEGTLTGRVKFIFQPAEELG-YGAFKIIETHALKDVQAVL-GfhnDPSRPIGTFAIKtGAITsavdr 175
Cdd:cd08659  100 LAAMVAALIELKEAGALLGGRVALLATVDEEVGsDGARALLEAGYADRLDALIvG---EPTGLDVVYAHK-GSLW----- 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 176 FEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRnLSAFDE---AVVTIGQISCGNTWNVIADHAYVQGTVRSFDP 252
Cdd:cd08659  171 LRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEE-LPAHPLlgpPTLNVGVINGGTQVNSIPDEATLRVDIRLVPG 249
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 612671875 253 VVRKLVETRLQDIADGLAQAYNMKINLNYTHlPGAVMNDEALTHKAIAVAQHVG 306
Cdd:cd08659  250 ETNEGVIARLEAILEEHEAKLTVEVSLDGDP-PFFTDPDHPLVQALQAAARALG 302
M20_18_42 cd18669
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ...
56-193 1.78e-10

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: 59.75  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  56 GQGPSCIAVRADIDALPIQE-------FVEQDFKSENEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVKFIFQPAEE 128
Cdd:cd18669    9 GGGGKRVLLGAHIDVVPAGEgdprdppFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEE 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612671875 129 LG--YGAFKIIETHALKD--VQAVLGFHNDPsRPIGTFAIKTGaitsAVDRFEFHIKGVGGHAAKPEQC 193
Cdd:cd18669   89 VGsgAGKGLLSKDALEEDlkVDYLFVGDATP-APQKGVGIRTP----LVDALSEAARKVFGKPQHAEGT 152
PRK08588 PRK08588
succinyl-diaminopimelate desuccinylase; Reviewed
31-304 1.87e-09

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 181490 [Multi-domain]  Cd Length: 377  Bit Score: 58.74  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  31 IKDILTEYHIRILDLPLTTG---LVAEVGQGPSCIAVRA--DIDALPIQEFVEQD-FK-SENEGVMHacGHDI-HMASIL 102
Cdd:PRK08588  28 LQDLFAKHGIESKIVKVNDGranLVAEIGSGSPVLALSGhmDVVAAGDVDKWTYDpFElTEKDGKLY--GRGAtDMKSGL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 103 ATAV----KLKEIEGTLTGRVKFIFQPAEELG-YGAFKIIETHALKDVQA-VLGfhnDPSRPIGTFAIKtGAITsavdrf 176
Cdd:PRK08588 106 AALViamiELKEQGQLLNGTIRLLATAGEEVGeLGAKQLTEKGYADDLDAlIIG---EPSGHGIVYAHK-GSMD------ 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 177 eFHIK--GVGGHAAKPEQCNDPVIVLVQLINSIQSIVSrNLSAFDE------AVVTIgqISCGNTWNVIADHAYVQGTVR 248
Cdd:PRK08588 176 -YKVTstGKAAHSSMPELGVNAIDPLLEFYNEQKEYFD-SIKKHNPylggltHVVTI--INGGEQVNSVPDEAELEFNIR 251
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 612671875 249 SFDPVVRKLVETRLQDIADGLAQAYNMKINLN--YTHLPGAVMNDEALTHKAIAVAQH 304
Cdd:PRK08588 252 TIPEYDNDQVISLLQEIINEVNQNGAAQLSLDiySNHRPVASDKDSKLVQLAKDVAKS 309
Zinc_peptidase_like cd03873
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
50-193 2.66e-09

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: 56.28  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  50 GLVAE--VGQGPSCIAVRADIDALPIQE-------FVEQDFKSENEGVMHACGHDIHMASILATAVKLKEIEGTLTGRVK 120
Cdd:cd03873    1 NLIARlgGGEGGKSVALGAHLDVVPAGEgdnrdppFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612671875 121 FIFQPAEE----LGYGAFKIIETHALKDVQAVLGFHNDP-SRPIGTFAIKtgaiTSAVDRFEFHIKGVGGHAAKPEQC 193
Cdd:cd03873   81 VAFTADEEvgsgGGKGLLSKFLLAEDLKVDAAFVIDATAgPILQKGVVIR----NPLVDALRKAAREVGGKPQRASVI 154
M20_CPDG2 cd03885
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ...
98-266 3.79e-09

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: 57.60  E-value: 3.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  98 MASILATAVKLKEIEGTLTGRVKFIFQPAEELGY-GAFKIIETHAlKDVQAVLGFhnDPSRPIGtfAIKTGaiTSAVDRF 176
Cdd:cd03885  102 LVVILHALKALKAAGGRDYLPITVLLNSDEEIGSpGSRELIEEEA-KGADYVLVF--EPARADG--NLVTA--RKGIGRF 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 177 EFHIKGVGGHAAK-PEQCNDPVIVLVQLINSIQSivsrnLSAFDEAV-VTIGQISCGNTWNVIADHAYVQGTVRSFDPVV 254
Cdd:cd03885  175 RLTVKGRAAHAGNaPEKGRSAIYELAHQVLALHA-----LTDPEKGTtVNVGVISGGTRVNVVPDHAEAQVDVRFATAEE 249
                        170
                 ....*....|..
gi 612671875 255 RKLVETRLQDIA 266
Cdd:cd03885  250 ADRVEEALRAIV 261
PepD2 COG2195
Di- or tripeptidase [Amino acid transport and metabolism];
98-273 6.37e-09

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


Pssm-ID: 441798 [Multi-domain]  Cd Length: 364  Bit Score: 56.98  E-value: 6.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  98 MASILATAVKLK--EIEgtlTGRVKFIFQPAEELG-YGAFKIiethALKDVQAVLGFHNDpSRPIGTFAIKT-GAitsav 173
Cdd:COG2195  105 VAAILAALEYLKepEIP---HGPIEVLFTPDEEIGlRGAKAL----DVSKLGADFAYTLD-GGEEGELEYECaGA----- 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 174 DRFEFHIKGVGGHA-AKPEqcndpvivlvQLINSIQsIVSRNLSAFDEAVVT------IGQISCGNTWNVIADHAYVQGT 246
Cdd:COG2195  172 ADAKITIKGKGGHSgDAKE----------KMINAIK-LAARFLAALPLGRIPeetegnEGFIHGGSATNAIPREAEAVYI 240
                        170       180
                 ....*....|....*....|....*..
gi 612671875 247 VRSFDpvvRKLVETRLQDIADGLAQAY 273
Cdd:COG2195  241 IRDHD---REKLEARKAELEEAFEEEN 264
M20_dimer pfam07687
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ...
176-267 1.36e-08

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: 52.35  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  176 FEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVSRNLSAFDEAVVTIGQISCGNTWNVIADHAYVQGTVRSFDPVVR 255
Cdd:pfam07687   9 GHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGFDFPRTTLNITGIEGGTATNVIPAEAEAKFDIRLLPGEDL 88
                          90
                  ....*....|..
gi 612671875  256 KLVETRLQDIAD 267
Cdd:pfam07687  89 EELLEEIEAILE 100
M20_bAS cd03884
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ...
175-312 4.31e-06

M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.


Pssm-ID: 349880 [Multi-domain]  Cd Length: 398  Bit Score: 48.29  E-value: 4.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 175 RFEFHIKGVGGHA-AKP-EQCNDPVIVLVQLINSIQSIVSRNLsafDEAVVTIGQISCG-NTWNVIADhaYVQGTV--RS 249
Cdd:cd03884  208 WLEVTVTGEAGHAgTTPmALRRDALLAAAELILAVEEIALEHG---DDLVATVGRIEVKpNAVNVIPG--EVEFTLdlRH 282
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612671875 250 FDPVVRKLVETRLQDIADGLAQAYNMKINLNYTHLPGAVMNDEALTHKAIAVAQHVGYKVEMM 312
Cdd:cd03884  283 PDDAVLDAMVERIRAEAEAIAAERGVEVEVERLWDSPPVPFDPELVAALEAAAEALGLSYRRM 345
M20_peptT_like cd05683
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ...
116-308 7.76e-05

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


Pssm-ID: 349932 [Multi-domain]  Cd Length: 368  Bit Score: 44.36  E-value: 7.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 116 TGRVKFIFQPAEELGYGAFKIIETHALKdvqAVLGFHNDPSRPIGTFAIktGAITSavDRFEFHIKGVGGHAA-KPEQCn 194
Cdd:cd05683  128 HGQIQFVITVGEESGLVGAKALDPELID---ADYGYALDSEGDVGTIIV--GAPTQ--DKINAKIYGKTAHAGtSPEKG- 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 195 dpvivlvqlINSI----QSIVSRNLSAFD-EAVVTIGQISCGNTWNVIADHAYVQGTVRSFDP-----VVRKLVETrLQD 264
Cdd:cd05683  200 ---------ISAIniaaKAISNMKLGRIDeETTANIGKFQGGTATNIVTDEVNIEAEARSLDEekldaQVKHMKET-FET 269
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 612671875 265 IADGLAQAYNMKINLNYThlPGAVMNDEALTHKAIAVAQHVGYK 308
Cdd:cd05683  270 TAKEKGAHAEVEVETSYP--GFKINEDEEVVKLAKRAANNLGLE 311
PRK12893 PRK12893
Zn-dependent hydrolase;
157-312 3.24e-04

Zn-dependent hydrolase;


Pssm-ID: 237250 [Multi-domain]  Cd Length: 412  Bit Score: 42.56  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 157 RPIGtfaIKTGAitSAVDRFEFHIKGVGGHA---AKPEQcNDPVIVLVQLINSIQSIVSRnlsAFDEAVVTIGQISCG-N 232
Cdd:PRK12893 203 LPIG---VVTGI--QGIRWLEVTVEGQAAHAgttPMAMR-RDALVAAARIILAVERIAAA---LAPDGVATVGRLRVEpN 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 233 TWNVIADhaYVQGTV--RSFDPVVRKLVETRLQDIADGLAQAYNMKINLNYT-HLPGAVMnDEALTHKAIAVAQHVGYKV 309
Cdd:PRK12893 274 SRNVIPG--KVVFTVdiRHPDDARLDAMEAALRAACAKIAAARGVQVTVETVwDFPPVPF-DPALVALVEAAAEALGLSH 350

                 ...
gi 612671875 310 EMM 312
Cdd:PRK12893 351 MRM 353
M20_PAAh_like cd03896
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ...
98-306 1.33e-03

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: 40.54  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  98 MASILATAVKLKEIEGTLTGRVKFIFQPAEE-LG--YGAFKIIETHalkdvQAVLGFH--NDPSrpigTFAIKTGAITSA 172
Cdd:cd03896   94 LACLLAMARAMKEAGAALKGDVVFAANVGEEgLGdlRGARYLLSAH-----GARLDYFvvAEGT----DGVPHTGAVGSK 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 173 VDRFEFhiKGVGGHAAKPEQCNDPVIVLVQLINSIQSIVsrnLSAFDEAVVTIGQISCGNTWNVIADHAYVQGTVRSFDP 252
Cdd:cd03896  165 RFRITT--VGPGGHSYGAFGSPSAIVAMAKLVEALYEWA---APYVPKTTFAAIRGGGGTSVNRIANLCSMYLDIRSNPD 239
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 612671875 253 VVRKLVETRLQDIADGLAQAY-NMKINLN-YTHLPGA-VMNDEALTHKAIAVAQHVG 306
Cdd:cd03896  240 AELADVQREVEAVVSKLAAKHlRVKARVKpVGDRPGGeAQGTEPLVNAAVAAHREVG 296
PRK06133 PRK06133
glutamate carboxypeptidase; Reviewed
99-265 1.93e-03

glutamate carboxypeptidase; Reviewed


Pssm-ID: 235710 [Multi-domain]  Cd Length: 410  Bit Score: 40.00  E-value: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  99 ASILATAVKLKEIEGTLTGRVKFIFQPAEELGY-GAFKIIETHAlKDVQAVLGFhnDPSRPIGTFAIKTGAITSAVdrfe 177
Cdd:PRK06133 142 AVILHALKILQQLGFKDYGTLTVLFNPDEETGSpGSRELIAELA-AQHDVVFSC--EPGRAKDALTLATSGIATAL---- 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875 178 FHIKGVGGHA-AKPEQCNDPVIVLvqlinSIQSIVSRNLSAFDEAV-VTIGQISCGNTWNVIADHAYVQGTVRSFDPVVR 255
Cdd:PRK06133 215 LEVKGKASHAgAAPELGRNALYEL-----AHQLLQLRDLGDPAKGTtLNWTVAKAGTNRNVIPASASAQADVRYLDPAEF 289
                        170
                 ....*....|
gi 612671875 256 KLVETRLQDI 265
Cdd:PRK06133 290 DRLEADLQEK 299
M20_ArgE_DapE-like cd08011
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
99-241 2.65e-03

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: 39.29  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612671875  99 ASILAtAVKLKEIEGTLTGRVKFIFQPAEELG--YGafkiieTHALkdVQAVLGFHNDP--SRPIGTFAIKTGAitSAVD 174
Cdd:cd08011  108 ASIIA-VARLADAKAPWDLPVVLTFVPDEETGgrAG------TKYL--LEKVRIKPNDVliGEPSGSDNIRIGE--KGLV 176
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612671875 175 RFEFHIKGVGGHAAKPEQCNDPVIVLVQLINSIQSIvsrnlsafdEAVVTIGQISCGNTWNVIADHA 241
Cdd:cd08011  177 WVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYEL---------EKTVNPGVIKGGVKVNLVPDYC 234
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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