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Conserved domains on  [gi|312032407|ref|NP_001185826|]
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aminoacylase-1 isoform c [Homo sapiens]

Protein Classification

aminoacylase-1 family protein( domain architecture ID 10145322)

peptidase M20 aminoacylase-1 family protein is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M20_AcylaseI_like cd05646
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ...
 9-334 0e+00

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


:

Pssm-ID: 349898 [Multi-domain]  Cd Length: 391  Bit Score: 626.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407   9 EHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVVPVFK 88
Cdd:cd05646    1 EDPAVTRFREYLRINTVHPNPDYDACVEFLKRQADELGLPVRVIEVVPGKPVVVLTWEGSNPELPSILLNSHTDVVPVFE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  89 EHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHALR 168
Cdd:cd05646   81 EKWTHDPFSAHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIGGHDGMEKFVKTEEFKKLN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 169 AGFALDEGIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKL----------------------------- 219
Cdd:cd05646  161 VGFALDEGLASPTEEYRVFYGERSPWWVVITAPGTPGHGSKLLENTAGEKLrkviesimefresqkqrlksnpnltlgdv 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 220 ------------------------------------AFEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDDSNPWWAAFS 263
Cdd:cd05646  241 ttvnltmlkggvqmnvvpseaeagfdlripptvdleEFEKQIDEWCAEAGRGVTYEFEQKSPEKDPTSLDDSNPWWAAFK 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312032407 264 RVCKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALA 334
Cdd:cd05646  321 KAVKEMGLKLKPEIFPAATDSRYIRALGIPALGFSPMNNTPILLHDHNEFLNEDVFLRGIEIYEKIIPALA 391
 
Name Accession Description Interval E-value
M20_AcylaseI_like cd05646
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ...
 9-334 0e+00

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


Pssm-ID: 349898 [Multi-domain]  Cd Length: 391  Bit Score: 626.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407   9 EHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVVPVFK 88
Cdd:cd05646    1 EDPAVTRFREYLRINTVHPNPDYDACVEFLKRQADELGLPVRVIEVVPGKPVVVLTWEGSNPELPSILLNSHTDVVPVFE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  89 EHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHALR 168
Cdd:cd05646   81 EKWTHDPFSAHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIGGHDGMEKFVKTEEFKKLN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 169 AGFALDEGIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKL----------------------------- 219
Cdd:cd05646  161 VGFALDEGLASPTEEYRVFYGERSPWWVVITAPGTPGHGSKLLENTAGEKLrkviesimefresqkqrlksnpnltlgdv 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 220 ------------------------------------AFEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDDSNPWWAAFS 263
Cdd:cd05646  241 ttvnltmlkggvqmnvvpseaeagfdlripptvdleEFEKQIDEWCAEAGRGVTYEFEQKSPEKDPTSLDDSNPWWAAFK 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312032407 264 RVCKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALA 334
Cdd:cd05646  321 KAVKEMGLKLKPEIFPAATDSRYIRALGIPALGFSPMNNTPILLHDHNEFLNEDVFLRGIEIYEKIIPALA 391
Ac-peptdase-euk TIGR01880
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ...
 1-336 0e+00

N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.


Pssm-ID: 273850 [Multi-domain]  Cd Length: 400  Bit Score: 607.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407    1 MTSKGpEEEHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSH 80
Cdd:TIGR01880   1 MSSSK-WEEDIAVTRFREYLRINTVQPNPDYAACVDFLIKQADELGLARKTIEFVPGKPVVVLTWPGSNPELPSILLNSH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407   81 TDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQ 160
Cdd:TIGR01880  80 TDVVPVFREHWTHPPFSAFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGMEKFAK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  161 RPEFHALRAGFALDEGIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKL--------------------- 219
Cdd:TIGR01880 160 TDEFKALNLGFALDEGLASPDDVYRVFYAERVPWWVVVTAPGNPGHGSKLMENTAMEKLeksvesirrfresqfqllqsn 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  220 --------------------------------------------AFEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDDS 255
Cdd:TIGR01880 240 pdlaigdvtsvnltklkggvqsnvipseaeagfdirlapsvdfeEMENRLDEWCADAGEGVTYEFSQHSGKPLVTPHDDS 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  256 NPWWAAFSRVCKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALAS 335
Cdd:TIGR01880 320 NPWWVAFKDAVKEMGCTFKPEILPGSTDSRYIRAAGVPALGFSPMNNTPVLLHDHNEFLNEAVFLRGIEIYQTLISALAS 399


                  .
gi 312032407  336 V 336
Cdd:TIGR01880 400 V 400
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
 13-334 6.89e-51

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: 173.53  E-value: 6.89e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  13 VTLFRQYLRIRTVQPkpDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTlSSILLNSHTDVVPV-FKEHW 91
Cdd:COG0624   15 LELLRELVRIPSVSG--EEAAAAELLAELLEALGFEVERLEVPPGRPNLVARRPGDGGG-PTLLLYGHLDVVPPgDLELW 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  92 SHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHqGMELFVQRpEFHALRAGF 171
Cdd:COG0624   92 TSDPFEP-TIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSP-GARALVEE-LAEGLKADA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 172 ALdegIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFME-DTAAEKLA------------------------------ 220
Cdd:COG0624  169 AI---VGEPTGVPTIVTGHKGSLRFELTVRGKAAHSSRPELgVNAIEALAralaalrdlefdgradplfgrttlnvtgie 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 221 ----------------------------FEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDDSNPWWAAFSRVCKD-MNL 271
Cdd:COG0624  246 ggtavnvipdeaeakvdirllpgedpeeVLAALRALLAAAAPGVEVEVEVLGDGRPPFETPPDSPLVAAARAAIREvTGK 325

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312032407 272 TLEPEIMPAATDNRYI-RAVGVPALGFSPMNRTpvLLHDHDERLHEAVFLRGVDIYTRLLPALA 334
Cdd:COG0624  326 EPVLSGVGGGTDARFFaEALGIPTVVFGPGDGA--GAHAPDEYVELDDLEKGARVLARLLERLA 387
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
 76-330 2.40e-39

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: 141.33  E-value: 2.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407   76 LLNSHTDVVPVfkEHWSHDPFEAFKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRfPRTIHMTFVPDEEvGGHQGM 155
Cdd:pfam01546   1 LLRGHMDVVPD--EETWGWPFKSTED--GKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEE-GGMGGA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  156 ELFVQRPEFHALRAGFALDEGIANPTD-----AFTVFYSERSPWWVRVTSTGRPGHASRF-MEDTAAEKLA--------- 220
Cdd:pfam01546  75 RALIEDGLLEREKVDAVFGLHIGEPTLleggiAIGVVTGHRGSLRFRVTVKGKGGHASTPhLGVNAIVAAArlilalqdi 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  221 ------------------------------------------------FEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPT 252
Cdd:pfam01546 155 vsrnvdpldpavvtvgnitgipggvnvipgeaelkgdirllpgedleeLEERIREILEAIAAAYGVKVEVEYVEGGAPPL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  253 DDSNPWWAAFSRVCKDM---NLTLEPEIMPAATDNRYIrAVGVPA--LGFSPMNRTpvlLHDHDERLHEAVFLRGVDIYT 327
Cdd:pfam01546 235 VNDSPLVAALREAAKELfglKVELIVSGSMGGTDAAFF-LLGVPPtvVFFGPGSGL---AHSPNEYVDLDDLEKGAKVLA 310


                  ...
gi 312032407  328 RLL 330
Cdd:pfam01546 311 RLL 313
PRK08262 PRK08262
M20 family peptidase;
20-220 2.40e-28

M20 family peptidase;


Pssm-ID: 236208 [Multi-domain]  Cd Length: 486  Bit Score: 114.66  E-value: 2.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  20 LRIRTV--QPKPDYGAA-----VAFFEETARQLGLGCQKVEVAPgyvVTVL-TWPGTNPTLSSILLNSHTDVVPV---FK 88
Cdd:PRK08262  54 IRFRTIsnRDRAEDDAAafdalHAHLEESYPAVHAALEREVVGG---HSLLyTWKGSDPSLKPIVLMAHQDVVPVapgTE 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  89 EHWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGH---QGMELFVQRpefh 165
Cdd:PRK08262 131 GDWTHPPFSGVIA-DGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVGGLgarAIAELLKER---- 205

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312032407 166 ALRAGFALDEGIANPTDAFTVF--------YSERSPWWVRVTSTGRPGHASRFMEDTAAEKLA 220
Cdd:PRK08262 206 GVRLAFVLDEGGAITEGVLPGVkkpvaligVAEKGYATLELTARATGGHSSMPPRQTAIGRLA 268
 
Name Accession Description Interval E-value
M20_AcylaseI_like cd05646
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ...
 9-334 0e+00

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


Pssm-ID: 349898 [Multi-domain]  Cd Length: 391  Bit Score: 626.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407   9 EHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVVPVFK 88
Cdd:cd05646    1 EDPAVTRFREYLRINTVHPNPDYDACVEFLKRQADELGLPVRVIEVVPGKPVVVLTWEGSNPELPSILLNSHTDVVPVFE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  89 EHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHALR 168
Cdd:cd05646   81 EKWTHDPFSAHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIGGHDGMEKFVKTEEFKKLN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 169 AGFALDEGIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKL----------------------------- 219
Cdd:cd05646  161 VGFALDEGLASPTEEYRVFYGERSPWWVVITAPGTPGHGSKLLENTAGEKLrkviesimefresqkqrlksnpnltlgdv 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 220 ------------------------------------AFEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDDSNPWWAAFS 263
Cdd:cd05646  241 ttvnltmlkggvqmnvvpseaeagfdlripptvdleEFEKQIDEWCAEAGRGVTYEFEQKSPEKDPTSLDDSNPWWAAFK 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312032407 264 RVCKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALA 334
Cdd:cd05646  321 KAVKEMGLKLKPEIFPAATDSRYIRALGIPALGFSPMNNTPILLHDHNEFLNEDVFLRGIEIYEKIIPALA 391
Ac-peptdase-euk TIGR01880
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ...
 1-336 0e+00

N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.


Pssm-ID: 273850 [Multi-domain]  Cd Length: 400  Bit Score: 607.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407    1 MTSKGpEEEHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSH 80
Cdd:TIGR01880   1 MSSSK-WEEDIAVTRFREYLRINTVQPNPDYAACVDFLIKQADELGLARKTIEFVPGKPVVVLTWPGSNPELPSILLNSH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407   81 TDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQ 160
Cdd:TIGR01880  80 TDVVPVFREHWTHPPFSAFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGMEKFAK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  161 RPEFHALRAGFALDEGIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKL--------------------- 219
Cdd:TIGR01880 160 TDEFKALNLGFALDEGLASPDDVYRVFYAERVPWWVVVTAPGNPGHGSKLMENTAMEKLeksvesirrfresqfqllqsn 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  220 --------------------------------------------AFEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDDS 255
Cdd:TIGR01880 240 pdlaigdvtsvnltklkggvqsnvipseaeagfdirlapsvdfeEMENRLDEWCADAGEGVTYEFSQHSGKPLVTPHDDS 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  256 NPWWAAFSRVCKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALAS 335
Cdd:TIGR01880 320 NPWWVAFKDAVKEMGCTFKPEILPGSTDSRYIRAAGVPALGFSPMNNTPVLLHDHNEFLNEAVFLRGIEIYQTLISALAS 399


                  .
gi 312032407  336 V 336
Cdd:TIGR01880 400 V 400
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
 13-334 6.89e-51

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: 173.53  E-value: 6.89e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  13 VTLFRQYLRIRTVQPkpDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTlSSILLNSHTDVVPV-FKEHW 91
Cdd:COG0624   15 LELLRELVRIPSVSG--EEAAAAELLAELLEALGFEVERLEVPPGRPNLVARRPGDGGG-PTLLLYGHLDVVPPgDLELW 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  92 SHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHqGMELFVQRpEFHALRAGF 171
Cdd:COG0624   92 TSDPFEP-TIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSP-GARALVEE-LAEGLKADA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 172 ALdegIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFME-DTAAEKLA------------------------------ 220
Cdd:COG0624  169 AI---VGEPTGVPTIVTGHKGSLRFELTVRGKAAHSSRPELgVNAIEALAralaalrdlefdgradplfgrttlnvtgie 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 221 ----------------------------FEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDDSNPWWAAFSRVCKD-MNL 271
Cdd:COG0624  246 ggtavnvipdeaeakvdirllpgedpeeVLAALRALLAAAAPGVEVEVEVLGDGRPPFETPPDSPLVAAARAAIREvTGK 325

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312032407 272 TLEPEIMPAATDNRYI-RAVGVPALGFSPMNRTpvLLHDHDERLHEAVFLRGVDIYTRLLPALA 334
Cdd:COG0624  326 EPVLSGVGGGTDARFFaEALGIPTVVFGPGDGA--GAHAPDEYVELDDLEKGARVLARLLERLA 387
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
 76-330 2.40e-39

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: 141.33  E-value: 2.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407   76 LLNSHTDVVPVfkEHWSHDPFEAFKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRfPRTIHMTFVPDEEvGGHQGM 155
Cdd:pfam01546   1 LLRGHMDVVPD--EETWGWPFKSTED--GKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEE-GGMGGA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  156 ELFVQRPEFHALRAGFALDEGIANPTD-----AFTVFYSERSPWWVRVTSTGRPGHASRF-MEDTAAEKLA--------- 220
Cdd:pfam01546  75 RALIEDGLLEREKVDAVFGLHIGEPTLleggiAIGVVTGHRGSLRFRVTVKGKGGHASTPhLGVNAIVAAArlilalqdi 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  221 ------------------------------------------------FEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPT 252
Cdd:pfam01546 155 vsrnvdpldpavvtvgnitgipggvnvipgeaelkgdirllpgedleeLEERIREILEAIAAAYGVKVEVEYVEGGAPPL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  253 DDSNPWWAAFSRVCKDM---NLTLEPEIMPAATDNRYIrAVGVPA--LGFSPMNRTpvlLHDHDERLHEAVFLRGVDIYT 327
Cdd:pfam01546 235 VNDSPLVAALREAAKELfglKVELIVSGSMGGTDAAFF-LLGVPPtvVFFGPGSGL---AHSPNEYVDLDDLEKGAKVLA 310


                  ...
gi 312032407  328 RLL 330
Cdd:pfam01546 311 RLL 313
M20_yscS_like cd05675
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ...
 13-330 1.11e-36

M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.


Pssm-ID: 349924 [Multi-domain]  Cd Length: 431  Bit Score: 136.72  E-value: 1.11e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  13 VTLFRQYLRIRTVQPKPDYG-------AAVAFFEETArqLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVVP 85
Cdd:cd05675    1 VDLLQELIRIDTTNSGDGTGsetraaeVLAARLAEAG--IQTEIFVVESHPGRANLVARIGGTDPSAGPLLLLGHIDVVP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  86 VFKEHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQ-RPEF 164
Cdd:cd05675   79 ADASDWSVDPFSG-EIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWLVDnHPEL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 165 HAlRAGFALDEG------IANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLA--------------FEEQ 224
Cdd:cd05675  158 FD-GATFALNEGgggslpVGKGRRLYPIQVAEKGIAWMKLTVRGRAGHGSRPTDDNAITRLAealrrlgahnfpvrLTDE 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 225 LQSWCQAA----GEGVTLEF------------------------------------------------------------ 240
Cdd:cd05675  237 TAYFAQMAelagGEGGALMLtavpvldpalaklgpsapllnamlrntasptmldagyatnvlpgrataevdcrilpgqse 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 241 ----------------AQKWMH---PQVTPTDdsNPWWAAFSRVCKDM--NLTLEPEIMPAATDNRYIRAVGVPALGFSP 299
Cdd:cd05675  317 eevldtldkllgdpdvSVEAVHlepATESPLD--SPLVDAMEAAVQAVdpGAPVVPYMSPGGTDAKYFRRLGIPGYGFAP 394

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 312032407 300 MNRTPVL-----LHDHDERLHEAVFLRGVDIYTRLL 330
Cdd:cd05675  395 LFLPPELdytglFHGVDERVPVESLYFGVRFLDRLV 430
Zinc_peptidase_like cd03873
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
 62-326 2.15e-35

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: 127.54  E-value: 2.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  62 VLTWPGTnPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHM 141
Cdd:cd03873    3 IARLGGG-EGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 142 TFVPDEEVGGHQGMELFVQRpefhALRAGFALDEgianptdaftVFYSERSPWWvrvtsTGRPGHASRfmedtaaeklaf 221
Cdd:cd03873   82 AFTADEEVGSGGGKGLLSKF----LLAEDLKVDA----------AFVIDATAGP-----ILQKGVVIR------------ 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 222 eeqlqswcqaagegvtlefaqkwmhpqvtptddsNPWWAAFSRVCKDMNLTLEPEIM-PAATDNRYIRAVGVPALGFSPM 300
Cdd:cd03873  131 ----------------------------------NPLVDALRKAAREVGGKPQRASViGGGTDGRLFAELGIPGVTLGPP 176

                        250       260
                 ....*....|....*....|....*.
gi 312032407 301 nrTPVLLHDHDERLHEAVFLRGVDIY 326
Cdd:cd03873  177 --GDKGAHSPNEFLNLDDLEKATKVY 200
M20_18_42 cd18669
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ...
 62-326 4.51e-35

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: 126.78  E-value: 4.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  62 VLTWPGTnPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHM 141
Cdd:cd18669    3 IARYGGG-GGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 142 TFVPDEEVGGHQGMELFVQRPEFHALRAGFaldegianptdaftVFYSERSPWWVrvtstgrPGHASRfmedtaaeklaf 221
Cdd:cd18669   82 AFTPDEEVGSGAGKGLLSKDALEEDLKVDY--------------LFVGDATPAPQ-------KGVGIR------------ 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 222 eeqlqswcqaagegvtlefaqkwmhpqvtptddsNPWWAAFSRVCKDMNLTLEPEIM-PAATDNRYIRAVGVPALGFSPM 300
Cdd:cd18669  129 ----------------------------------TPLVDALSEAARKVFGKPQHAEGtGGGTDGRYLQELGIPGVTLGAG 174

                        250       260
                 ....*....|....*....|....*.
gi 312032407 301 nrTPVLLHDHDERLHEAVFLRGVDIY 326
Cdd:cd18669  175 --GGKGAHSPNERVNLEDLESALAVL 198
M20_ArgE_DapE-like cd08659
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ...
 15-330 1.06e-28

Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like; Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline.


Pssm-ID: 349944 [Multi-domain]  Cd Length: 361  Bit Score: 113.93  E-value: 1.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  15 LFRQYLRIRTVQPkpDYGAAVAFFEET--ARQLGLGCQKVEVAPGYVVTVLTwpGTNPTLssiLLNSHTDVVPVFKEH-W 91
Cdd:cd08659    2 LLQDLVQIPSVNP--PEAEVAEYLAELlaKRGYGIESTIVEGRGNLVATVGG--GDGPVL---LLNGHIDTVPPGDGDkW 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  92 SHDPFEAfKDSEGYIYARGAQDMK---CVSIQyleAVRRLKVEGHRFPRTIHMTFVPDEEVGGhQGMELFVQRPefHALR 168
Cdd:cd08659   75 SFPPFSG-RIRDGRLYGRGACDMKgglAAMVA---ALIELKEAGALLGGRVALLATVDEEVGS-DGARALLEAG--YADR 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 169 AGFALdegIANPTDaFTVFYSERSPWWVRVTSTGRPGHASR-FMEDTAAEKLA-----FEEQLQSW-------------- 228
Cdd:cd08659  148 LDALI---VGEPTG-LDVVYAHKGSLWLRVTVHGKAAHSSMpELGVNAIYALAdflaeLRTLFEELpahpllgpptlnvg 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 229 --------------CQA-------------------------AGEGVTLEFAQKWMHPQVTPTDdsNPWWAAFSRVCKDM 269
Cdd:cd08659  224 vinggtqvnsipdeATLrvdirlvpgetnegviarleaileeHEAKLTVEVSLDGDPPFFTDPD--HPLVQALQAAARAL 301

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312032407 270 NLTLEPEIMPAATDNRYI-RAVGVPALGFSPMNrtPVLLHDHDERLHEAVFLRGVDIYTRLL 330
Cdd:cd08659  302 GGDPVVRPFTGTTDASYFaKDLGFPVVVYGPGD--LALAHQPDEYVSLEDLLRAAEIYKEII 361
PRK08262 PRK08262
M20 family peptidase;
20-220 2.40e-28

M20 family peptidase;


Pssm-ID: 236208 [Multi-domain]  Cd Length: 486  Bit Score: 114.66  E-value: 2.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  20 LRIRTV--QPKPDYGAA-----VAFFEETARQLGLGCQKVEVAPgyvVTVL-TWPGTNPTLSSILLNSHTDVVPV---FK 88
Cdd:PRK08262  54 IRFRTIsnRDRAEDDAAafdalHAHLEESYPAVHAALEREVVGG---HSLLyTWKGSDPSLKPIVLMAHQDVVPVapgTE 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  89 EHWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGH---QGMELFVQRpefh 165
Cdd:PRK08262 131 GDWTHPPFSGVIA-DGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVGGLgarAIAELLKER---- 205

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312032407 166 ALRAGFALDEGIANPTDAFTVF--------YSERSPWWVRVTSTGRPGHASRFMEDTAAEKLA 220
Cdd:PRK08262 206 GVRLAFVLDEGGAITEGVLPGVkkpvaligVAEKGYATLELTARATGGHSSMPPRQTAIGRLA 268
PRK07906 PRK07906
hypothetical protein; Provisional
 13-220 4.78e-28

hypothetical protein; Provisional


Pssm-ID: 181163 [Multi-domain]  Cd Length: 426  Bit Score: 113.02  E-value: 4.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  13 VTLFRQYLRIRTVQP-----KPDYGAAvaffEETARQL---GLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVV 84
Cdd:PRK07906   2 VDLCSELIRIDTTNTgdgtgKGEREAA----EYVAEKLaevGLEPTYLESAPGRANVVARLPGADPSRPALLVHGHLDVV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  85 PVFKEHWSHDPFE-AFKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQ-RP 162
Cdd:PRK07906  78 PAEAADWSVHPFSgEIRD--GYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVADEEAGGTYGAHWLVDnHP 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312032407 163 EfhalragfaLDEGIanpTDA--------FTV-----FY----SERSPWWVRVTSTGRPGHASRFMEDTAAEKLA 220
Cdd:PRK07906 156 E---------LFEGV---TEAisevggfsLTVpgrdrLYlietAEKGLAWMRLTARGRAGHGSMVNDDNAVTRLA 218
M20_ArgE_DapE-like cd08011
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
 13-330 3.08e-27

M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 109.78  E-value: 3.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  13 VTLFRQYLRIRTVQPKPD-YGAAVAFFEETARQLGLGCQKVEVAPG--YVVTVLTWPGTNPTLssiLLNSHTDVVPVFKE 89
Cdd:cd08011    1 VKLLQELVQIPSPNPPGDnTSAIAAYIKLLLEDLGYPVELHEPPEEiyGVVSNIVGGRKGKRL---LFNGHYDVVPAGDG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  90 H-WSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHalr 168
Cdd:cd08011   78 EgWTVDPYSG-KIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTKYLLEKVRIK--- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 169 AGFALdegIANPTDAFTVFYSERSPWWVRVTSTGRPGHAS-------------RFMED--------------------TA 215
Cdd:cd08011  154 PNDVL---IGEPSGSDNIRIGEKGLVWVIIEITGKPAHGSlphrgesavkaamKLIERlyelektvnpgvikggvkvnLV 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 216 AEKLAFE------------EQLQSWCQ--AAGEGVTLEFAQKwmhPQVTPTDDSNPWWAAFSRVCKDM-NLTLEPEIMPA 280
Cdd:cd08011  231 PDYCEFSvdirlppgistdEVLSRIIDhlDSIEEVSFEIKSF---YSPTVSNPDSEIVKKTEEAITEVlGIRPKEVISVG 307

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 312032407 281 ATDNRYIRAVGVPALGFSPMNrtPVLLHDHDERLHEAVFLRGVDIYTRLL 330
Cdd:cd08011  308 ASDARFYRNAGIPAIVYGPGR--LGQMHAPNEYVEIDELIKVIKVHALVA 355
DapE-ArgE TIGR01910
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ...
 13-209 3.95e-25

acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273870 [Multi-domain]  Cd Length: 375  Bit Score: 104.40  E-value: 3.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407   13 VTLFRQYLRIRTVQP-KPDYGAAVAFFEETARQLGLGCQKVEVAPGYV----VTVLTWPGTNPTlSSILLNSHTDVVPV- 86
Cdd:TIGR01910   1 VELLKDLISIPSVNPpGGNEETIANYIKDLLREFGFSTDVIEITDDRLkvlgKVVVKEPGNGNE-KSLIFNGHYDVVPAg 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407   87 FKEHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGhQGMELFVQRpefha 166
Cdd:TIGR01910  80 DLELWKTDPFKP-VEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGE-AGTLYLLQR----- 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 312032407  167 lraGFALDEG---IANPTDAFTVFYSERSPWWVRVTSTGRPGHASR 209
Cdd:TIGR01910 153 ---GYFKDADgvlIPEPSGGDNIVIGHKGSIWFKLRVKGKQAHASF 195
PRK08651 PRK08651
succinyl-diaminopimelate desuccinylase; Reviewed
 12-208 6.27e-23

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 236323 [Multi-domain]  Cd Length: 394  Bit Score: 98.14  E-value: 6.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  12 SVTLFRQYLRIRTVQPKP-DYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTW-----PGTNPTLSSILLNSHTDVVP 85
Cdd:PRK08651   8 IVEFLKDLIKIPTVNPPGeNYEEIAEFLRDTLEELGFSTEIIEVPNEYVKKHDGPrpnliARRGSGNPHLHFNGHYDVVP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  86 VfKEHW-SHDPFEAFKDsEGYIYARGAQDMK--CVSIqyLEAVRRLKVEGhrfPRTIHMTFVPDEEVGGHQGMELfvqrp 162
Cdd:PRK08651  88 P-GEGWsVNVPFEPKVK-DGKVYGRGASDMKggIAAL--LAAFERLDPAG---DGNIELAIVPDEETGGTGTGYL----- 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 312032407 163 efhALRAGFALDEGI-ANPTDAFTVFYSERSPWWVRVTSTGRPGHAS 208
Cdd:PRK08651 156 ---VEEGKVTPDYVIvGEPSGLDNICIGHRGLVWGVVKVYGKQAHAS 199
M20_yscS cd05674
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ...
 62-208 5.22e-22

M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.


Pssm-ID: 349923 [Multi-domain]  Cd Length: 471  Bit Score: 96.17  E-value: 5.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  62 VLTWPGTNPTLSSILLNSHTDVVPVFKEH---WSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRT 138
Cdd:cd05674   59 LYTWEGSDPSLKPLLLMAHQDVVPVNPETedqWTHPPFSGHYD-GGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRT 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 139 IHMTFVPDEEVGGHQGMELFVQRPEFhalRAG-----FALDEGIAN-PTDAFTVFY-----SERSPWWVRVTSTGRPGHA 207
Cdd:cd05674  138 IILAFGHDEEVGGERGAGAIAELLLE---RYGvdglaAILDEGGAVlEGVFLGVPFalpgvAEKGYMDVEITVHTPGGHS 214


                 .
gi 312032407 208 S 208
Cdd:cd05674  215 S 215
PRK09133 PRK09133
hypothetical protein; Provisional
 15-220 3.22e-19

hypothetical protein; Provisional


Pssm-ID: 236388 [Multi-domain]  Cd Length: 472  Bit Score: 88.13  E-value: 3.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  15 LFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVVT---VLTWPGTNPTlSSILLNSHTDVVPVFKEHW 91
Cdd:PRK09133  42 LYKELIEINTTASTGSTTPAAEAMAARLKAAGFADADIEVTGPYPRKgnlVARLRGTDPK-KPILLLAHMDVVEAKREDW 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  92 SHDPFEaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGME-LFVQRPEfhALRAG 170
Cdd:PRK09133 121 TRDPFK-LVEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKRDIILALTGDEEGTPMNGVAwLAENHRD--LIDAE 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 312032407 171 FALDEGIANPTD------AFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLA 220
Cdd:PRK09133 198 FALNEGGGGTLDedgkpvLLTVQAGEKTYADFRLEVTNPGGHSSRPTKDNAIYRLA 253
PRK13013 PRK13013
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
13-225 7.78e-16

acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;


Pssm-ID: 237268 [Multi-domain]  Cd Length: 427  Bit Score: 77.88  E-value: 7.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  13 VTLFRQYLRIRTVQPKPD-YGAAVAFFEETARQLGLGCQKVeVAPGYVVTVLTWPGTN--------PTLSSILLNSHTDV 83
Cdd:PRK13013  17 VALTQDLIRIPTLNPPGRaYREICEFLAARLAPRGFEVELI-RAEGAPGDSETYPRWNlvarrqgaRDGDCVHFNSHHDV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  84 VPVfKEHWSHDPFEAFKDsEGYIYARGAQDMK---CVSIQYLEAVRRLKVEghrFPRTIHMTFVPDEEVGGHQGMELFVQ 160
Cdd:PRK13013  96 VEV-GHGWTRDPFGGEVK-DGRIYGRGACDMKgglAASIIAAEAFLAVYPD---FAGSIEISGTADEESGGFGGVAYLAE 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312032407 161 RPEFHALRAGFALdegIANPTDAFTVFYSERSPWWVRVTSTGRPGHASR-FMEDTAAEKL-----AFEEQL 225
Cdd:PRK13013 171 QGRFSPDRVQHVI---IPEPLNKDRICLGHRGVWWAEVETRGRIAHGSMpFLGDSAIRHMgavlaEIEERL 238
M20_ArgE cd03894
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ...
 75-208 9.80e-16

M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16) subfamily. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.


Pssm-ID: 349889 [Multi-domain]  Cd Length: 367  Bit Score: 77.25  E-value: 9.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  75 ILLNSHTDVVPVFKEHWSHDPFEAfKDSEGYIYARGAQDMK----CVsiqyLEAVRRLKVEGHRFPrtIHMTFVPDEEVg 150
Cdd:cd03894   60 LLLSGHTDVVPVDGQKWSSDPFTL-TERDGRLYGRGTCDMKgflaAV----LAAVPRLLAAKLRKP--LHLAFSYDEEV- 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 312032407 151 GHQGMELFVQRPEFHALRAGFALdegIANPTD-AFTVFYSERSPWWVRVtsTGRPGHAS 208
Cdd:cd03894  132 GCLGVRHLIAALAARGGRPDAAI---VGEPTSlQPVVAHKGIASYRIRV--RGRAAHSS 185
M20_ArgE_DapE-like cd03895
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
 8-209 3.30e-15

M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE.


Pssm-ID: 349890 [Multi-domain]  Cd Length: 400  Bit Score: 75.81  E-value: 3.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407   8 EEHPSVTLFRQYLRIRtvqpkpdyGAAVAFFEETARQLG--LGCQKVEV----APGyVVTVLTwpGTNPTLSSILLNSHT 81
Cdd:cd03895   15 EEAAAQDLVAAALRSR--------GYTVDRWEIDVEKLKhhPGFSPVAVdyagAPN-VVGTHR--PRGETGRSLILNGHI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  82 DVVPVFK-EHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQ 160
Cdd:cd03895   84 DVVPEGPvELWTRPPFEA-TIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTGNGALAALMR 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 312032407 161 rpefhALRAGFALdegIANPTDAfTVFYSERSPWWVRVTSTGRPGHASR 209
Cdd:cd03895  163 -----GYRADAAL---IPEPTEL-KLVRAQVGVIWFRVKVRGTPAHVAE 202
M20_DapE_proteobac cd03891
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ...
 13-154 2.02e-13

M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE; aspartyl dipeptidase; succinyl-diaminopimelate desuccinylase) subfamily. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.


Pssm-ID: 349886 [Multi-domain]  Cd Length: 366  Bit Score: 70.23  E-value: 2.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  13 VTLFRQYLRIRTVQPKpDYGAaVAFFEETARQLGLGCQKVEVapGYVVTVLTWPGTNPTLssILLNSHTDVVPV-FKEHW 91
Cdd:cd03891    1 LELAKELIRRPSVTPD-DAGA-QDLIAERLKALGFTCERLEF--GGVKNLWARRGTGGPH--LCFAGHTDVVPPgDLEGW 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312032407  92 SHDPFEAfKDSEGYIYARGAQDMKCvSIQ-YLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQG 154
Cdd:cd03891   75 SSDPFSP-TIKDGMLYGRGAADMKG-GIAaFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDG 136
PRK06837 PRK06837
ArgE/DapE family deacylase;
62-233 7.36e-13

ArgE/DapE family deacylase;


Pssm-ID: 180721 [Multi-domain]  Cd Length: 427  Bit Score: 68.88  E-value: 7.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  62 VLTWPGTNPTLSSILLNSHTDVVPVFK-EHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIH 140
Cdd:PRK06837  87 VGTYRPAGKTGRSLILQGHIDVVPEGPlDLWSRPPFDP-VIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVH 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 141 MTFVPDEEVGGHqGMELFVQRpefhALRAGFALdegIANPTDAfTVFYSERSPWWVRVTSTGRPGHAsRFMED-----TA 215
Cdd:PRK06837 166 FQSVIEEESTGN-GALSTLQR----GYRADACL---IPEPTGE-KLVRAQVGVIWFRLRVRGAPVHV-REAGTganaiDA 235

                        170       180
                 ....*....|....*....|
gi 312032407 216 AEKL--AFEEQLQSWCQAAG 233
Cdd:PRK06837 236 AYHLiqALRELEAEWNARKA 255
M20_CPDG2 cd03885
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ...
 33-300 4.18e-12

M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.


Pssm-ID: 349881 [Multi-domain]  Cd Length: 362  Bit Score: 66.46  E-value: 4.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  33 AAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPtlSSILLNSHTDVVpvfkehWSHD--PFEAFKDSEGYIYARG 110
Cdd:cd03885   23 RVAELLAEELEALGFTVERRPLGEFGDHLIATFKGTGG--KRVLLIGHMDTV------FPEGtlAFRPFTVDGDRAYGPG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 111 AQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFvqrpEFHALRAGFALDEGIANPTDAFTVFYSE 190
Cdd:cd03885   95 VADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSRELI----EEEAKGADYVLVFEPARADGNLVTARKG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 191 RSPWWVRVtsTGRPGHASRFMED------------------------------------------------------TAA 216
Cdd:cd03885  171 IGRFRLTV--KGRAAHAGNAPEKgrsaiyelahqvlalhaltdpekgttvnvgvisggtrvnvvpdhaeaqvdvrfaTAE 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 217 EKLAFEEQLQSWCQAA-GEGVTLEFAQKWMHPQVTPTDDSNPWWAAFSRVCKDMNLTLEPEIMPAATDNRYIRAVGVPAL 295
Cdd:cd03885  249 EADRVEEALRAIVATTlVPGTSVELTGGLNRPPMEETPASRRLLARAQEIAAELGLTLDWEATGGGSDANFTAALGVPTL 328


                 ....*.
gi 312032407 296 -GFSPM 300
Cdd:cd03885  329 dGLGPV 334
AcOrn-deacetyl TIGR01892
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ...
 75-209 4.52e-12

acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine deacetylases from proteobacteria. This enzyme is the final step of the "acetylated" ornithine biosynthesis pathway. The enzyme is closely related to dapE, succinyl-diaminopimelate desuccinylase, and outside of this clade annotation is very inaccurate as to which function should be ascribed to genes. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 130947 [Multi-domain]  Cd Length: 364  Bit Score: 66.38  E-value: 4.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407   75 ILLNSHTDVVPVFKEHWSHDPFEaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPrtIHMTFVPDEEVgGHQG 154
Cdd:TIGR01892  61 LALSGHTDVVPYDDAAWTRDPFR-LTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKP--LHLALTADEEV-GCTG 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 312032407  155 MELFVQRPefhALRAGFALdegIANPTDAFTVfYSERSPWWVRVTSTGRPGHASR 209
Cdd:TIGR01892 137 APKMIEAG---AGRPRHAI---IGEPTRLIPV-RAHKGYASAEVTVRGRSGHSSY 184
PRK08596 PRK08596
acetylornithine deacetylase; Validated
 37-150 4.88e-12

acetylornithine deacetylase; Validated


Pssm-ID: 181495 [Multi-domain]  Cd Length: 421  Bit Score: 66.60  E-value: 4.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  37 FFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPT-LSSILLNSHTDVVPVFK-EHWSHDPFEAFKDsEGYIYARGAQDM 114
Cdd:PRK08596  41 FIAEFLRKLGFSVDKWDVYPNDPNVVGVKKGTESDaYKSLIINGHMDVAEVSAdEAWETNPFEPTIK-DGWLYGRGAADM 119

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 312032407 115 KCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVG 150
Cdd:PRK08596 120 KGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEVG 155
M20_ArgE_DapE-like_fungal cd05652
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
 33-158 3.49e-11

M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal, and have been inferred by similarity as being related to both ArgE and DapE.


Pssm-ID: 349903 [Multi-domain]  Cd Length: 340  Bit Score: 63.45  E-value: 3.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  33 AAVA-FFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTlSSILLNSHTDVVPvfkehwSHDPFEAfKDSEGYIYARGA 111
Cdd:cd05652   19 AAVGdFLAEYLESLGFTVEKQPVENKDRFNVYAYPGSSRQ-PRVLLTSHIDTVP------PFIPYSI-SDGGDTIYGRGS 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 312032407 112 QDMK-CVSIQYLeAVRRLKVEGHRFPRTIHMTFVPDEEVGGHqGMELF 158
Cdd:cd05652   91 VDAKgSVAAQII-AVEELLAEGEVPEGDLGLLFVVGEETGGD-GMKAF 136
PRK13009 PRK13009
succinyl-diaminopimelate desuccinylase; Reviewed
 10-115 4.71e-11

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 237265 [Multi-domain]  Cd Length: 375  Bit Score: 63.18  E-value: 4.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  10 HPSVTLFRQYLRIRTVQPKpDYGAaVAFFEETARQLGLGCQKVEVAPgyvVTVL--TWPGTNPTLssiLLNSHTDVVPV- 86
Cdd:PRK13009   2 SDVLELAQDLIRRPSVTPD-DAGC-QDLLAERLEALGFTCERMDFGD---VKNLwaRRGTEGPHL---CFAGHTDVVPPg 73

                         90       100
                 ....*....|....*....|....*....
gi 312032407  87 FKEHWSHDPFEAfKDSEGYIYARGAQDMK 115
Cdd:PRK13009  74 DLEAWTSPPFEP-TIRDGMLYGRGAADMK 101
PRK13983 PRK13983
M20 family metallo-hydrolase;
79-209 5.53e-11

M20 family metallo-hydrolase;


Pssm-ID: 237578 [Multi-domain]  Cd Length: 400  Bit Score: 62.94  E-value: 5.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  79 SHTDVVPVFKEH-WSHDPFEA-FKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGME 156
Cdd:PRK13983  83 SHMDVVPPGDLSlWETDPFKPvVKD--GKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETGSKYGIQ 160

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 312032407 157 -LFVQRPEfhalraGFALDEGI-----ANPTDAFtVFYSERSPWWVRVTSTGRPGHASR 209
Cdd:PRK13983 161 yLLKKHPE------LFKKDDLIlvpdaGNPDGSF-IEIAEKSILWLKFTVKGKQCHAST 212
dipeptidaselike TIGR01887
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ...
 20-150 9.53e-11

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


Pssm-ID: 273854 [Multi-domain]  Cd Length: 447  Bit Score: 62.40  E-value: 9.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407   20 LRIRTVQ----PKPDY------GAAVAFFEETARQLGLGCQKVEVAPGYVVTvltwpGTNPTLSSILlnSHTDVVPVfKE 89
Cdd:TIGR01887  12 IAIDSVEdlekAKEGApfgegpRKALDKFLEIAKRDGFTTENVDNYAGYIEY-----GQGEEVLGIL--GHLDVVPA-GD 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312032407   90 HWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVG 150
Cdd:TIGR01887  84 GWTSPPFEPTIK-DGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEESG 143
PRK07522 PRK07522
acetylornithine deacetylase; Provisional
 75-150 2.07e-10

acetylornithine deacetylase; Provisional


Pssm-ID: 236039 [Multi-domain]  Cd Length: 385  Bit Score: 61.36  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  75 ILLNSHTDVVPVFKEHWSHDPFEAFKDsEGYIYARGAQDMK----CVsiqyLEAVRRLKVEGHRFPrtIHMTFVPDEEVG 150
Cdd:PRK07522  67 IVLSGHTDVVPVDGQAWTSDPFRLTER-DGRLYGRGTCDMKgfiaAA----LAAVPELAAAPLRRP--LHLAFSYDEEVG 139
PRK13004 PRK13004
YgeY family selenium metabolism-linked hydrolase;
47-208 2.90e-10

YgeY family selenium metabolism-linked hydrolase;


Pssm-ID: 183836 [Multi-domain]  Cd Length: 399  Bit Score: 61.11  E-value: 2.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  47 LGCQKVEVAP-----GYVvtvltwpGTNPTLssILLNSHTDVVPVF-KEHWSHDPFEAFKDsEGYIYARGAQDMK--CVS 118
Cdd:PRK13004  48 VGFDKVEIDPmgnvlGYI-------GHGKKL--IAFDAHIDTVGIGdIKNWDFDPFEGEED-DGRIYGRGTSDQKggMAS 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 119 IQYleAVRRLKVEGHRFPRTIHMT-FVPDEEVGGHQGMELFVQ---RPEFHAlragfaldegIANPTDaFTVFYSERSPW 194
Cdd:PRK13004 118 MVY--AAKIIKDLGLDDEYTLYVTgTVQEEDCDGLCWRYIIEEdkiKPDFVV----------ITEPTD-LNIYRGQRGRM 184

                        170
                 ....*....|....
gi 312032407 195 WVRVTSTGRPGHAS 208
Cdd:PRK13004 185 EIRVETKGVSCHGS 198
M20_PepV cd03888
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ...
 17-205 3.91e-10

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


Pssm-ID: 349884 [Multi-domain]  Cd Length: 449  Bit Score: 60.72  E-value: 3.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  17 RQYLRIRTV--QPKPDY--G----AAVAFFEETARQLGLgcqKVEVAPGYVVTVLTwpGTNPTLSSILlnSHTDVVPVfK 88
Cdd:cd03888   15 KELVAIPSVrdEATEGApfGegprKALDKFLDLAKRLGF---KTKNIDNYAGYAEY--GEGEEVLGIL--GHLDVVPA-G 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  89 EHWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGhQGMELFVQR---PEFh 165
Cdd:cd03888   87 EGWTTDPFKPVIK-DGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGTDEETGW-KCIEHYFEHeeyPDF- 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 312032407 166 alraGFALDegiANptdaFTVFYSERSPWWVRVTSTGRPG 205
Cdd:cd03888  164 ----GFTPD---AE----FPVINGEKGIVTVDLTFKIDDD 192
dapE_proteo TIGR01246
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ...
 12-148 1.87e-09

succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 162269 [Multi-domain]  Cd Length: 370  Bit Score: 58.19  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407   12 SVTLFRQYLRIRTVQPKpDYGAaVAFFEETARQLGLGCQKVEVapGYVVTVLTWPGTNPTLssILLNSHTDVVPV-FKEH 90
Cdd:TIGR01246   1 VTELAKELISRPSVTPN-DAGC-QDIIAERLEKLGFEIEWMHF--GDTKNLWATRGTGEPV--LAFAGHTDVVPAgPEEQ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 312032407   91 WSHDPFEaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEE 148
Cdd:TIGR01246  75 WSSPPFE-PVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEE 131
PRK06915 PRK06915
peptidase;
74-218 2.56e-09

peptidase;


Pssm-ID: 180745 [Multi-domain]  Cd Length: 422  Bit Score: 58.16  E-value: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  74 SILLNSHTDVVPVFK-EHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGH 152
Cdd:PRK06915  95 SMILNGHIDVVPEGDvNQWDHHPYSG-EVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEESGGA 173

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312032407 153 QGMElfvqrpefhALRAGFALDEG-IANPTDaFTVFYSERSPWWVRVTSTGRPGH-ASRFMEDTAAEK 218
Cdd:PRK06915 174 GTLA---------AILRGYKADGAiIPEPTN-MKFFPKQQGSMWFRLHVKGKAAHgGTRYEGVSAIEK 231
M20_ArgE_DapE-like cd05649
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
 13-208 4.06e-09

M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.


Pssm-ID: 349900 [Multi-domain]  Cd Length: 381  Bit Score: 57.43  E-value: 4.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  13 VTLFRQYLRIRTvqPKPDYGAAVAFFEETARQLGLgcQKVEVAPgyVVTVLTWPGTNPTLssILLNSHTDVVPVF-KEHW 91
Cdd:cd05649    1 TRFLRDLIQIPS--ESGEEKGVVERIEEEMEKLGF--DEVEIDP--MGNVIGYIGGGKKK--ILFDGHIDTVGIGnIDNW 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  92 SHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHR-FPRTIHMTFVPDEEV-GGHQGMELFVQ---RPEFHA 166
Cdd:cd05649   73 KFDPYEG-YETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGLRdFAYTILVAGTVQEEDcDGVCWQYISKAdkiKPDFVV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 312032407 167 lragfaldegIANPTDAfTVFYSERSPWWVRVTSTGRPGHAS 208
Cdd:cd05649  152 ----------SGEPTDG-NIYRGQRGRMEIRVDTKGVSCHGS 182
PRK07205 PRK07205
hypothetical protein; Provisional
 80-148 8.47e-09

hypothetical protein; Provisional


Pssm-ID: 235965 [Multi-domain]  Cd Length: 444  Bit Score: 56.63  E-value: 8.47e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312032407  80 HTDVVPVFKEH-WSHDPFEA-FKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEE 148
Cdd:PRK07205  83 HLDVVPEGDLSdWQTPPFEAvEKD--GCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGTDEE 151
M20_dipept_Sso-CP2 cd05681
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ...
 17-176 1.94e-08

uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.


Pssm-ID: 349930 [Multi-domain]  Cd Length: 429  Bit Score: 55.42  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  17 RQYLRIRTVQPKPDYGAAVA-FFEETARQLGLGCQKVEvAPGYVVTVLTWP-GTNPTLssiLLNSHTDVVPVFK-EHWSH 93
Cdd:cd05681    6 RDLLKIPSVSAQGRGIPETAdFLKEFLRRLGAEVEIFE-TDGNPIVYAEFNsGDAKTL---LFYNHYDVQPAEPlELWTS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  94 DPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGhQGMELFVQRpefHA--LRAGF 171
Cdd:cd05681   82 DPFEL-TIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGS-PNLEKFVAE---HAdlLKADG 156


                 ....*
gi 312032407 172 ALDEG 176
Cdd:cd05681  157 CIWEG 161
M20_ArgE_DapE-like cd05650
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
 79-209 2.53e-08

M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.


Pssm-ID: 349901 [Multi-domain]  Cd Length: 389  Bit Score: 54.77  E-value: 2.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  79 SHTDVVPVFK-EHWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMEL 157
Cdd:cd05650   76 SHLDTVPPGDlSLWETDPWEPVVK-DGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSEYGIQY 154

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 312032407 158 FVQRPEFhalragFALDEGIANP----TDAFTVFYSERSPWWVRVTSTGRPGHASR 209
Cdd:cd05650  155 LLNKFDL------FKKDDLIIVPdfgtEDGEFIEIAEKSILWIKVNVKGKQCHAST 204
M20_ArgE_DapE-like cd05651
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
 74-215 3.14e-07

M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are bacterial, and have been inferred by homology as being related to both ArgE and DapE.


Pssm-ID: 349902 [Multi-domain]  Cd Length: 341  Bit Score: 51.54  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  74 SILLNSHTDVVPVFKEhWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGhrfPRTIHMTFV--PDEEVGG 151
Cdd:cd05651   57 TLLLNSHHDTVKPNAG-WTKDPFEP-VEKGGKLYGLGSNDAGASVVSLLATFLHLYSEG---PLNYNLIYAasAEEEISG 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312032407 152 HQGME-LFVQRPEfhalragfaLDEGI-ANPTDaFTVFYSERSPWWVRVTSTGRPGHASRFMEDTA 215
Cdd:cd05651  132 KNGIEsLLPHLPP---------LDLAIvGEPTE-MQPAIAEKGLLVLDCTARGKAGHAARNEGDNA 187
PRK08588 PRK08588
succinyl-diaminopimelate desuccinylase; Reviewed
 80-208 3.34e-07

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 181490 [Multi-domain]  Cd Length: 377  Bit Score: 51.42  E-value: 3.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  80 HTDVVPVFKEH-WSHDPFEAfKDSEGYIYARGAQDMK----CVSIqyleAVRRLKVEGHRFPRTIHMTFVPDEEVGGHqG 154
Cdd:PRK08588  67 HMDVVAAGDVDkWTYDPFEL-TEKDGKLYGRGATDMKsglaALVI----AMIELKEQGQLLNGTIRLLATAGEEVGEL-G 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 312032407 155 MELFVQrpefhalrAGFALD-EG--IANPTDAFtVFYSERSPWWVRVTSTGRPGHAS 208
Cdd:PRK08588 141 AKQLTE--------KGYADDlDAliIGEPSGHG-IVYAHKGSMDYKVTSTGKAAHSS 188
M20_ArgE_LysK cd05653
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ...
 13-252 3.51e-07

M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.


Pssm-ID: 349904 [Multi-domain]  Cd Length: 343  Bit Score: 51.20  E-value: 3.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  13 VTLFRQYLRIRTvqPKPDYGAAVAFFEETARQLGLGCQKVEVapGYVVTVLtwpGTNPTLssILLNSHTDVVPVFKEhws 92
Cdd:cd05653    4 VELLLDLLSIYS--PSGEEARAAKFLEEIMKELGLEAWVDEA--GNAVGGA---GSGPPD--VLLLGHIDTVPGEIP--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  93 hdpfeaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHrfpRTIHMTFVPDEEVGGHQGMELFVQRPEFHALRAGfa 172
Cdd:cd05653   72 ------VRVEGGVLYGRGAVDAKGPLAAMILAASALNEELG---ARVVVAGLVDEEGSSKGARELVRRGPRPDYIIIG-- 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 173 ldegiaNPTDAFTVFYSERSPWWVRVTSTGRPGHASRfMEDTAAEKLA-FEEQLQSWCQAAGEGVTLEFaqkwmhpQVTP 251
Cdd:cd05653  141 ------EPSGWDGITLGYRGSLLVKIRCEGRSGHSSS-PERNAAEDLIkKWLEVKKWAEGYNVGGRDFD-------SVVP 206


                 .
gi 312032407 252 T 252
Cdd:cd05653  207 T 207
M20_dipept_like cd05680
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ...
 20-150 4.13e-07

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


Pssm-ID: 349929 [Multi-domain]  Cd Length: 437  Bit Score: 51.16  E-value: 4.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  20 LRIRTVQPKPDYGAAVAFFEE-TARQL-GLGCQKVEV--APGYVVTVLTWPGTnPTLSSILLNSHTDVVPVFKEH-WSHD 94
Cdd:cd05680    8 LRIPSVSADPAHKGDVRRAAEwLADKLtEAGFEHTEVlpTGGHPLVYAEWLGA-PGAPTVLVYGHYDVQPPDPLElWTSP 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 312032407  95 PFE-AFKDseGYIYARGAQDMKCVSIQYLEAVRR-LKVEGhRFPRTIHMTFVPDEEVG 150
Cdd:cd05680   87 PFEpVVRD--GRLYARGASDDKGQVFIHIKAVEAwLAVEG-ALPVNVKFLIEGEEEIG 141
M20_ArgE_DapE-like cd08013
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
 46-209 4.76e-07

M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal and bacterial, and have been inferred by homology as being related to both ArgE and DapE.


Pssm-ID: 349935 [Multi-domain]  Cd Length: 379  Bit Score: 50.94  E-value: 4.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  46 GLGCQKVEVAPG--YVVTVLTWPGTNPTLssiLLNSHTDVVPVfkEHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLE 123
Cdd:cd08013   43 GIEAHRIEGTPGrpSVVGVVRGTGGGKSL---MLNGHIDTVTL--DGYDGDPLSG-EIADGRVYGRGTLDMKGGLAACMA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 124 AVRRLKVEGHRfpRTIHMTFVPDEEVGGhQGMElfvqrpefHALRAGFALDEGI-ANPTDaFTVFYSERSPWWVRVTSTG 202
Cdd:cd08013  117 ALADAKEAGLR--GDVILAAVADEEDAS-LGTQ--------EVLAAGWRADAAIvTEPTN-LQIIHAHKGFVWFEVDIHG 184


                 ....*..
gi 312032407 203 RPGHASR 209
Cdd:cd08013  185 RAAHGSR 191
PRK07907 PRK07907
hypothetical protein; Provisional
 21-166 8.15e-07

hypothetical protein; Provisional


Pssm-ID: 236127 [Multi-domain]  Cd Length: 449  Bit Score: 50.29  E-value: 8.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  21 RIRTVQPKP----DYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTN--PTlssILLNSHTDVVPVFKE-HWSH 93
Cdd:PRK07907  29 RIPSVAADPfrreEVARSAEWVADLLREAGFDDVRVVSADGAPAVIGTRPAPPgaPT---VLLYAHHDVQPPGDPdAWDS 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312032407  94 DPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLkveGHRFPRTIHMtFVPDEEVGGHQGMELFV--QRPEFHA 166
Cdd:PRK07907 106 PPFEL-TERDGRLYGRGAADDKGGIAMHLAALRAL---GGDLPVGVTV-FVEGEEEMGSPSLERLLaeHPDLLAA 175
M20_dipept_like_CNDP cd05676
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ...
 67-150 9.27e-07

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


Pssm-ID: 349925 [Multi-domain]  Cd Length: 467  Bit Score: 50.29  E-value: 9.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  67 GTNPTLSSILLNSHTDVVPVFKE-HWSHDPFEaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVP 145
Cdd:cd05676   80 GSDPSKKTVLIYGHLDVQPAKLEdGWDTDPFE-LTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEG 158


                 ....*
gi 312032407 146 DEEVG 150
Cdd:cd05676  159 MEESG 163
M20_like cd02697
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ...
 74-172 1.20e-06

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


Pssm-ID: 349869 [Multi-domain]  Cd Length: 394  Bit Score: 49.86  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  74 SILLNSHTDVVPVfKEHWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQ 153
Cdd:cd02697   75 TVALNAHGDVVPP-GDGWTRDPYGAVVE-DGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGEL 152

                         90       100
                 ....*....|....*....|...
gi 312032407 154 GMELFVQ----RPEFhALRAGFA 172
Cdd:cd02697  153 GPGWLLRqgltKPDL-LIAAGFS 174
PRK08554 PRK08554
peptidase; Reviewed
 75-157 3.43e-06

peptidase; Reviewed


Pssm-ID: 236285 [Multi-domain]  Cd Length: 438  Bit Score: 48.62  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  75 ILLNSHTDVVPVFKEHWSHDPFEaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRfpRTIHMTFVPDEEVGGHQG 154
Cdd:PRK08554  66 LLFMAHFDVVPVNPEEWNTEPFK-LTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLN--GKVIFAFTGDEEIGGAMA 142


                 ...
gi 312032407 155 MEL 157
Cdd:PRK08554 143 MHI 145
PRK08201 PRK08201
dipeptidase;
17-161 4.35e-06

dipeptidase;


Pssm-ID: 169276 [Multi-domain]  Cd Length: 456  Bit Score: 48.20  E-value: 4.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  17 RQYLRIRTV----QPKPDYGAAVAFFEETARQLGLgcQKVEV--APGYVVTVLTW---PGtNPTlssILLNSHTDVVPVF 87
Cdd:PRK08201  21 KEFLRIPSIsalsEHKEDVRKAAEWLAGALEKAGL--EHVEImeTAGHPIVYADWlhaPG-KPT---VLIYGHYDVQPVD 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312032407  88 KEH-WSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRR-LKVEGhRFPRTIHMTFVPDEEVGGhQGMELFVQR 161
Cdd:PRK08201  95 PLNlWETPPFEP-TIRDGKLYARGASDDKGQVFMHLKAVEAlLKVEG-TLPVNVKFCIEGEEEIGS-PNLDSFVEE 167
PRK06446 PRK06446
hypothetical protein; Provisional
 74-176 5.75e-06

hypothetical protein; Provisional


Pssm-ID: 235802 [Multi-domain]  Cd Length: 436  Bit Score: 47.83  E-value: 5.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  74 SILLNSHTDVVPVFK-EHWSHDPFEA-FKDseGYIYARGAQDMKCVSIQYLEAVRRLkVEGHRFPRTIHMTFVPDEEVGG 151
Cdd:PRK06446  64 TLLIYNHYDVQPVDPlSEWKRDPFSAtIEN--GRIYARGASDNKGTLMARLFAIKHL-IDKHKLNVNVKFLYEGEEEIGS 140

                         90       100
                 ....*....|....*....|....*
gi 312032407 152 hQGMELFVQRPEfHALRAGFALDEG 176
Cdd:PRK06446 141 -PNLEDFIEKNK-NKLKADSVIMEG 163
PRK09104 PRK09104
hypothetical protein; Validated
 15-186 8.31e-06

hypothetical protein; Validated


Pssm-ID: 236379 [Multi-domain]  Cd Length: 464  Bit Score: 47.20  E-value: 8.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  15 LFrQYLRIRTVQPKPDYGA----AVAFFEETARQLGLGCQKVEvAPGYVVTVLTWPGTNPTLSSILLNSHTDVVPVFK-E 89
Cdd:PRK09104  23 LF-ALLRIPSISTDPAYAAdcrkAADWLVADLASLGFEASVRD-TPGHPMVVAHHEGPTGDAPHVLFYGHYDVQPVDPlD 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  90 HWSHDPFE-AFKDSEG---YIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGhQGMELFVQRpefH 165
Cdd:PRK09104 101 LWESPPFEpRIKETPDgrkVIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEESGS-PSLVPFLEA---N 176

                        170       180
                 ....*....|....*....|....*.
gi 312032407 166 A--LRAGFAL--DEGIANP-TDAFTV 186
Cdd:PRK09104 177 AeeLKADVALvcDTGMWDReTPAITT 202
M20_ArgE_RocB cd05654
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ...
 67-155 9.34e-06

M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.


Pssm-ID: 349905  Cd Length: 534  Bit Score: 47.34  E-value: 9.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  67 GTNPTLSSILLNSHTDVVPV-------------------FKEHWSHDPFEAFKD--SEGYIYARGAQDMKCVSIQYLEAV 125
Cdd:cd05654   66 GKKPSKRTIILISHFDTVGIedygelkdiafdpdeltkaFSEYVEELDEEVREDllSGEWLFGRGTMDMKSGLAVHLALL 145

                         90       100       110
                 ....*....|....*....|....*....|
gi 312032407 126 RRLKVEGHrFPRTIHMTFVPDEEVgGHQGM 155
Cdd:cd05654  146 EQASEDED-FDGNLLLMAVPDEEV-NSRGM 173
M20_ArgE-related cd08012
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ...
 46-181 1.11e-05

M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.


Pssm-ID: 349934 [Multi-domain]  Cd Length: 423  Bit Score: 46.68  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  46 GLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGyIYARGAQDmkCVSIQYL--E 123
Cdd:cd08012   52 PLVIDHVSYVKGRGNIIVEYPGTVDGKTVSFVGSHMDVVTANPETWEFDPFSLSIDGDK-LYGRGTTD--CLGHVALvtE 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312032407 124 AVRRLKVEGHRFPRTIHMTFVPDEEVGG--HQGMELFVQRPEFHALRAG--FALDEGIANPT 181
Cdd:cd08012  129 LFRQLATEKPALKRTVVAVFIANEENSEipGVGVDALVKSGLLDNLKSGplYWVDSADSQPC 190
PRK07318 PRK07318
dipeptidase PepV; Reviewed
 80-150 1.52e-05

dipeptidase PepV; Reviewed


Pssm-ID: 235988 [Multi-domain]  Cd Length: 466  Bit Score: 46.37  E-value: 1.52e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312032407  80 HTDVVPVfKEHWSHDPFEA-FKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVG 150
Cdd:PRK07318  87 HLDVVPA-GDGWDTDPYEPvIKD--GKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVRFIVGTDEESG 155
PRK08652 PRK08652
acetylornithine deacetylase; Provisional
 75-182 1.82e-05

acetylornithine deacetylase; Provisional


Pssm-ID: 236324 [Multi-domain]  Cd Length: 347  Bit Score: 45.91  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  75 ILLNS--------HTDVVPVFKEhwshdPFEafkdSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIhmTFVPD 146
Cdd:PRK08652  50 IVVNSkaelfvevHYDTVPVRAE-----FFV----DGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGI--AFVSD 118

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 312032407 147 EEVGGhQGMELFVQRpefhaLRAGFALdegIANPTD 182
Cdd:PRK08652 119 EEEGG-RGSALFAER-----YRPKMAI---VLEPTD 145
M20_Dipept_like cd03893
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ...
 17-151 6.34e-05

M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a large variety of enzymes, including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase), canosinase, DUG2 type proteins, as well as many proteins inferred by homology to be dipeptidases. These enzymes have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Substrates of CNDP are varied and not limited to Xaa-His dipeptides. DUG2 proteins contain a metallopeptidase domain and a large N-terminal WD40 repeat region, and are involved in the alternative pathway of glutathione degradation.


Pssm-ID: 349888 [Multi-domain]  Cd Length: 426  Bit Score: 44.63  E-value: 6.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  17 RQYLRIRTVQPKPD----YGAAVAFFEETARQLGLGCQKVEVAPG--YVVTVLTWPGTNPTlssILLNSHTDVVPVFKEH 90
Cdd:cd03893    5 AELVAIPSVSAQPDrreeLRRAAEWLADLLRRLGFTVEIVDTSNGapVVFAEFPGAPGAPT---VLLYGHYDVQPAGDED 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312032407  91 -WSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPrtIHMTFVPD--EEVGG 151
Cdd:cd03893   82 gWDSDPFEL-TERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLP--VNVKFIIEgeEESGS 142
PRK05111 PRK05111
acetylornithine deacetylase; Provisional
 75-208 2.92e-04

acetylornithine deacetylase; Provisional


Pssm-ID: 235346 [Multi-domain]  Cd Length: 383  Bit Score: 42.12  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  75 ILLNSHTDVVPvFKEH-WSHDPFeAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVegHRFPRTIHMTFVPDEEVGGHq 153
Cdd:PRK05111  74 LLLAGHTDTVP-FDEGrWTRDPF-TLTEHDGKLYGLGTADMKGFFAFILEALRDIDL--TKLKKPLYILATADEETSMA- 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 154 GMELFVQRpefHALRAGFALdegIANPTDAFTVF-----YSERspwwVRVtsTGRPGHAS 208
Cdd:PRK05111 149 GARAFAEA---TAIRPDCAI---IGEPTSLKPVRahkghMSEA----IRI--TGQSGHSS 196
PRK07473 PRK07473
M20/M25/M40 family metallo-hydrolase;
42-207 4.54e-04

M20/M25/M40 family metallo-hydrolase;


Pssm-ID: 168961 [Multi-domain]  Cd Length: 376  Bit Score: 41.69  E-value: 4.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  42 ARQLGLGCQKVEVAPGYV----VTVLTWPGTNPTLSSILLNSHTDVV-PVfkehwshDPFE--AFKDSEGYIYARGAQDM 114
Cdd:PRK07473  41 ARDMAIMGATIERIPGRQgfgdCVRARFPHPRQGEPGILIAGHMDTVhPV-------GTLEklPWRREGNKCYGPGILDM 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407 115 KCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFvqrpEFHALRAGFAL-------DEGIANPTDAFTVF 187
Cdd:PRK07473 114 KGGNYLALEAIRQLARAGITTPLPITVLFTPDEEVGTPSTRDLI----EAEAARNKYVLvpepgrpDNGVVTGRYAIARF 189

                        170       180
                 ....*....|....*....|
gi 312032407 188 yserspwwvRVTSTGRPGHA 207
Cdd:PRK07473 190 ---------NLEATGRPSHA 200
PRK00466 PRK00466
acetyl-lysine deacetylase; Validated
 15-208 9.08e-04

acetyl-lysine deacetylase; Validated


Pssm-ID: 166979 [Multi-domain]  Cd Length: 346  Bit Score: 40.54  E-value: 9.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  15 LFRQYLRIRTvqPKPDYGAAVAFFEETARQLGLGCQkvevapgyvvtvlTWPGTNPTLSS---ILLNSHTDVVPVFKEhw 91
Cdd:PRK00466  15 LLLDLLSIYT--PSGNETNATKFFEKISNELNLKLE-------------ILPDSNSFILGegdILLASHVDTVPGYIE-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  92 shdPFEafkdsEGY-IYARGAQDMKCVSIQYLEAVRRLKVEGHRfprtIHMTFVPDEEVGGHQGMELfvqrpefhaLRAG 170
Cdd:PRK00466  78 ---PKI-----EGEvIYGRGAVDAKGPLISMIIAAWLLNEKGIK----VMVSGLADEESTSIGAKEL---------VSKG 136

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 312032407 171 FALDEGI-ANPTDAFTVFYSERSPWWVRVTSTGRPGHAS 208
Cdd:PRK00466 137 FNFKHIIvGEPSNGTDIVVEYRGSIQLDIMCEGTPEHSS 175
PRK06156 PRK06156
dipeptidase;
17-161 1.10e-03

dipeptidase;


Pssm-ID: 235720 [Multi-domain]  Cd Length: 520  Bit Score: 40.72  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032407  17 RQYLRIRTV----QPKPDYGAAVAF---FEETARQLGLGCQKVevapGYVVTVLTWPGTNPTLSSILlnSHTDVVPVFKE 89
Cdd:PRK06156  53 RELVAFPTVrvegVPQHENPEFIGFkklLKSLARDFGLDYRNV----DNRVLEIGLGGSGSDKVGIL--THADVVPANPE 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312032407  90 HW-----SHDPFEAFKDSEgYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGhQGMELFVQR 161
Cdd:PRK06156 127 LWvldgtRLDPFKVTLVGD-RLYGRGTEDDKGAIVTALYAMKAIKDSGLPLARRIELLVYTTEETDG-DPLKYYLER 201
 
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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