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Conserved domains on  [gi|544827008|ref|WP_021242981|]
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MULTISPECIES: S9 family peptidase [Enterobacteriaceae]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 11445445)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
7-242 5.05e-33

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


:

Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 119.74  E-value: 5.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008   7 TFKNAAGEELAGLLELSENPKAF--ALLAHCFTCGKDlKGAARIARKLTENAIAVLRFDFTGLGNSEGDFSntnfSSNIS 84
Cdd:COG1506    1 TFKSADGTTLPGWLYLPADGKKYpvVVYVHGGPGSRD-DSFLPLAQALASRGYAVLAPDYRGYGESAGDWG----GDEVD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  85 DLLCAVDYLRRQYEAPS---LLIGHSLGGSAILSIAGEVPEA-KAVVTIGSPGELTHVKRLFKddveninqhgaypvELA 160
Cdd:COG1506   76 DVLAAIDYLAARPYVDPdriGIYGHSYGGYMALLAAARHPDRfKAAVALAGVSDLRSYYGTTR--------------EYT 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008 161 GRVFTLKKQMLDNIQEHKIAHKVFAMNKPLLIFHATEDDTVLIEQAEKIFKAAK---HPKSFISLGKADHLLTHAQDAEY 237
Cdd:COG1506  142 ERLMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKkagKPVELLVYPGEGHGFSGAGAPDY 221


                 ....*
gi 544827008 238 VADII 242
Cdd:COG1506  222 LERIL 226
 
Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
7-242 5.05e-33

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 119.74  E-value: 5.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008   7 TFKNAAGEELAGLLELSENPKAF--ALLAHCFTCGKDlKGAARIARKLTENAIAVLRFDFTGLGNSEGDFSntnfSSNIS 84
Cdd:COG1506    1 TFKSADGTTLPGWLYLPADGKKYpvVVYVHGGPGSRD-DSFLPLAQALASRGYAVLAPDYRGYGESAGDWG----GDEVD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  85 DLLCAVDYLRRQYEAPS---LLIGHSLGGSAILSIAGEVPEA-KAVVTIGSPGELTHVKRLFKddveninqhgaypvELA 160
Cdd:COG1506   76 DVLAAIDYLAARPYVDPdriGIYGHSYGGYMALLAAARHPDRfKAAVALAGVSDLRSYYGTTR--------------EYT 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008 161 GRVFTLKKQMLDNIQEHKIAHKVFAMNKPLLIFHATEDDTVLIEQAEKIFKAAK---HPKSFISLGKADHLLTHAQDAEY 237
Cdd:COG1506  142 ERLMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKkagKPVELLVYPGEGHGFSGAGAPDY 221


                 ....*
gi 544827008 238 VADII 242
Cdd:COG1506  222 LERIL 226
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 46-216 1.96e-07

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 50.29  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008   46 ARIARKLTENAIAVLRFDFTGLGNSEGDFSN-TNFSSNISDLLCAVDYLRRQY-EAPSLLIGHSLGGSAILSIAGEVPE- 122
Cdd:pfam12146  21 AHLADALAAQGFAVYAYDHRGHGRSDGKRGHvPSFDDYVDDLDTFVDKIREEHpGLPLFLLGHSMGGLIAALYALRYPDk 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  123 ---------------------AKAVVTIGS---PGELTHVKRLFK---DDVENINQHGAYPveLAGRVFTLK--KQMLD- 172
Cdd:pfam12146 101 vdglilsapalkikpylappiLKLLAKLLGklfPRLRVPNNLLPDslsRDPEVVAAYAADP--LVHGGISARtlYELLDa 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 544827008  173 --NIQEHkiAHKVFAmnkPLLIFHATEDDTVLIEQAEKIFKAAKHP 216
Cdd:pfam12146 179 geRLLRR--AAAITV---PLLLLHGGADRVVDPAGSREFYERAGST 219
hydr2_PEP TIGR03101
exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha ...
 45-141 8.13e-06

exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 1, TIGR03100) of the same superfamily.


Pssm-ID: 274428  Cd Length: 266  Bit Score: 45.96  E-value: 8.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008   45 AARIARKLTENAIAVLRFDFTGLGNSEGDFSNTNFSSNISDLLCAVDYLRRQYEAPSLLIGHSLGGSAILSIAGEVPEAK 124
Cdd:TIGR03101  45 VALQARAFAAGGFGVLQIDLYGCGDSAGDFAAARWDVWKEDVAAAYRWLIEQGHPPVTLWGLRLGALLALDAANPLAAKC 124

                          90       100
                  ....*....|....*....|..
gi 544827008  125 AVVTIGSP-----GELTHVKRL 141
Cdd:TIGR03101 125 NRLVLWQPvvsgkQQLQQFLRL 146
PHA02857 PHA02857
monoglyceride lipase; Provisional
 26-132 1.88e-04

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 41.80  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  26 PKAFALLAHcfTCGKDLKGAARIARKLTENAIAVLRFDFTGLGNSEGD-FSNTNFSSNISDLLCAVDYLRRQY-EAPSLL 103
Cdd:PHA02857  24 PKALVFISH--GAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEkMMIDDFGVYVRDVVQHVVTIKSTYpGVPVFL 101

                         90       100
                 ....*....|....*....|....*....
gi 544827008 104 IGHSLGGSAILSIAGEVPEAKAVVTIGSP 132
Cdd:PHA02857 102 LGHSMGATISILAAYKNPNLFTAMILMSP 130
 
Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
7-242 5.05e-33

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 119.74  E-value: 5.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008   7 TFKNAAGEELAGLLELSENPKAF--ALLAHCFTCGKDlKGAARIARKLTENAIAVLRFDFTGLGNSEGDFSntnfSSNIS 84
Cdd:COG1506    1 TFKSADGTTLPGWLYLPADGKKYpvVVYVHGGPGSRD-DSFLPLAQALASRGYAVLAPDYRGYGESAGDWG----GDEVD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  85 DLLCAVDYLRRQYEAPS---LLIGHSLGGSAILSIAGEVPEA-KAVVTIGSPGELTHVKRLFKddveninqhgaypvELA 160
Cdd:COG1506   76 DVLAAIDYLAARPYVDPdriGIYGHSYGGYMALLAAARHPDRfKAAVALAGVSDLRSYYGTTR--------------EYT 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008 161 GRVFTLKKQMLDNIQEHKIAHKVFAMNKPLLIFHATEDDTVLIEQAEKIFKAAK---HPKSFISLGKADHLLTHAQDAEY 237
Cdd:COG1506  142 ERLMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKkagKPVELLVYPGEGHGFSGAGAPDY 221


                 ....*
gi 544827008 238 VADII 242
Cdd:COG1506  222 LERIL 226
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 1-241 1.68e-31

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 116.17  E-value: 1.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008   1 MKKLKFTFKNAAGEELAGLL---ELSENPKAFALLAHCFTCGKDlkGAARIARKLTENAIAVLRFDFTGLGNSEGDFSNT 77
Cdd:COG1073    8 VNKEDVTFKSRDGIKLAGDLylpAGASKKYPAVVVAHGNGGVKE--QRALYAQRLAELGFNVLAFDYRGYGESEGEPREE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  78 NfSSNISDLLCAVDYLRRQYEAPS---LLIGHSLGGSAILSIAGEVPEAKAVVTIGSPGELTHV-KRLFKDDveninQHG 153
Cdd:COG1073   86 G-SPERRDARAAVDYLRTLPGVDPeriGLLGISLGGGYALNAAATDPRVKAVILDSPFTSLEDLaAQRAKEA-----RGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008 154 AYPVELAGRVFTLKKQMLDniqEHKIAHKVFAMNKPLLIFHATEDDTVLIEQAEKIFKAAKHPKSFISLGKADHLLTHAQ 233
Cdd:COG1073  160 YLPGVPYLPNVRLASLLND---EFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDLYDR 236


                 ....*....
gi 544827008 234 -DAEYVADI 241
Cdd:COG1073  237 pEEEYFDKL 245
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
22-247 5.33e-27

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 104.25  E-value: 5.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  22 LSENPKAFaLLAHCFTCGK-DLKgaaRIARKLTENAIAVLRFDFTGLGNSEGDFSNTNFSSNISDLLCAVDYLRRQYEAP 100
Cdd:COG1647   11 LEGGRKGV-LLLHGFTGSPaEMR---PLAEALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGYDKV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008 101 SLlIGHSLGGSAILSIAGEVPEAKAVVTIGSP-------GELTHVKRLFKDDVENIN--------QHGAYPVELAGRVFT 165
Cdd:COG1647   87 IV-IGLSMGGLLALLLAARYPDVAGLVLLSPAlkiddpsAPLLPLLKYLARSLRGIGsdiedpevAEYAYDRTPLRALAE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008 166 LKKqMLDNIQEHkiAHKVfamNKPLLIFHATEDDTVLIEQAEKIFKAAKHP-KSFISLGKADHLLTHAQDAEYVADIIIS 244
Cdd:COG1647  166 LQR-LIREVRRD--LPKI---TAPTLIIQSRKDEVVPPESARYIYERLGSPdKELVWLEDSGHVITLDKDREEVAEEILD 239


                 ...
gi 544827008 245 WSE 247
Cdd:COG1647  240 FLE 242
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
1-245 3.11e-23

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 93.91  E-value: 3.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008   1 MKKLKFTFKNAAGEELAGLLEL-SENPKAFALLAHCFTCGKDLkgAARIARKLTENAIAVLRFDFTGLGNSEGDFSN-TN 78
Cdd:COG2267    1 MTRRLVTLPTRDGLRLRGRRWRpAGSPRGTVVLVHGLGEHSGR--YAELAEALAAAGYAVLAFDLRGHGRSDGPRGHvDS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  79 FSSNISDLLCAVDYLRRQYEAPSLLIGHSLGGSAILSIAGEVPEA-KAVVTIGSpgelthvkRLFKDDVENINQHGAYPV 157
Cdd:COG2267   79 FDDYVDDLRAALDALRARPGLPVVLLGHSMGGLIALLYAARYPDRvAGLVLLAP--------AYRADPLLGPSARWLRAL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008 158 ELAGRvftlkkqmldniqehkiahkVFAMNKPLLIFHATEDDTVLIEQAEKIFKAAKHPKSFISLGKADHLLTHAQDAEY 237
Cdd:COG2267  151 RLAEA--------------------LARIDVPVLVLHGGADRVVPPEAARRLAARLSPDVELVLLPGARHELLNEPAREE 210


                 ....*...
gi 544827008 238 VADIIISW 245
Cdd:COG2267  211 VLAAILAW 218
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
5-228 2.80e-19

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 82.52  E-value: 2.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008   5 KFTFKNAAGEeLAGLLELSE-NPKAFALLAHC---FTCGKDLKGAARIARKLTENAIAVLRFDFTGLGNSEGDFSNTNfs 80
Cdd:COG2945    1 KVLINGPAGR-LEGRLDLPEgPPRGVALILHPhplFGGTMDNKVVYTLARALVAAGFAVLRFNFRGVGRSEGEFDEGR-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  81 SNISDLLCAVDYLRRQYEAPSLLIGHSLGGSAILSIAGEVPEAKAVVTIGSPgelthVKRLFKDDVEninqhgaypvela 160
Cdd:COG2945   78 GELDDAAAALDWLRAQNPLPLWLAGFSFGAYVALQLAMRLPEVEGLILVAPP-----VNRYDFSFLA------------- 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544827008 161 grvftlkkqmldniqehkiahkvfAMNKPLLIFHATEDDTVLIEQAEKIFKAAKHPKSFISLGKADHL 228
Cdd:COG2945  140 ------------------------PCPAPTLVIHGEQDEVVPPAEVLDWARPLSPPLPVVVVPGADHF 183
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
7-240 8.08e-11

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 59.98  E-value: 8.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008   7 TFKNAAGEELAGLLELSENPKAFA--LLAHcftcgkDLKG----AARIARKLTE---NAIAVLRFDFTGLGNSEGD---- 73
Cdd:COG0412    7 TIPTPDGVTLPGYLARPAGGGPRPgvVVLH------EIFGlnphIRDVARRLAAagyVVLAPDLYGRGGPGDDPDEaral 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  74 FSNTNFSSNISDLLCAVDYLRRQYEAPSL---LIGHSLGGSAILSIAGEVPEAKAVVTI-GSPGelthvkrlfkddveni 149
Cdd:COG0412   81 MGALDPELLAADLRAALDWLKAQPEVDAGrvgVVGFCFGGGLALLAAARGPDLAAAVSFyGGLP---------------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008 150 nqhGAYPVELAGRVftlkkqmldniqehkiahkvfamNKPLLIFHATEDDTVLIEQAEKIFKA---AKHPKSFISLGKAD 226
Cdd:COG0412  145 ---ADDLLDLAARI-----------------------KAPVLLLYGEKDPLVPPEQVAALEAAlaaAGVDVELHVYPGAG 198

                        250
                 ....*....|....
gi 544827008 227 HLLTHAQDAEYVAD 240
Cdd:COG0412  199 HGFTNPGRPRYDPA 212
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 59-245 9.13e-11

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 59.63  E-value: 9.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  59 VLRFDFTGLGNSEGDFSNTNFSSNISDLLCAVDYLRRQyeaPSLLIGHSLGGSAILSIAGEVPEA-KAVVTIGSpgelth 137
Cdd:COG0596   52 VIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALGLE---RVVLVGHSMGGMVALELAARHPERvAGLVLVDE------ 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008 138 vkrLFKDDVENINQHGAYPVELAgrvftlkkQMLDNIQEHKIAHKVFAMNKPLLIFHATEDDTVLIEQAEKIFKAAKHPK 217
Cdd:COG0596  123 ---VLAALAEPLRRPGLAPEALA--------ALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAE 191

                        170       180
                 ....*....|....*....|....*...
gi 544827008 218 sFISLGKADHLLtHAQDAEYVADIIISW 245
Cdd:COG0596  192 -LVVLPGAGHFP-PLEQPEAFAAALRDF 217
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
46-131 3.32e-08

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 52.96  E-value: 3.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  46 ARIARKLTENAIAVLRFDFTGLGNS-EGDFSNTNFSsnISDLLC-----AVDYLRRQY-EAPSLLIGHSLGGSAILSIAG 118
Cdd:COG4757   49 RPFARYLAERGFAVLTYDYRGIGLSrPGSLRGFDAG--YRDWGEldlpaVLDALRARFpGLPLLLVGHSLGGQLLGLAPN 126

                         90
                 ....*....|...
gi 544827008 119 eVPEAKAVVTIGS 131
Cdd:COG4757  127 -AERVDRLVTVAS 138
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 46-216 1.96e-07

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 50.29  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008   46 ARIARKLTENAIAVLRFDFTGLGNSEGDFSN-TNFSSNISDLLCAVDYLRRQY-EAPSLLIGHSLGGSAILSIAGEVPE- 122
Cdd:pfam12146  21 AHLADALAAQGFAVYAYDHRGHGRSDGKRGHvPSFDDYVDDLDTFVDKIREEHpGLPLFLLGHSMGGLIAALYALRYPDk 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  123 ---------------------AKAVVTIGS---PGELTHVKRLFK---DDVENINQHGAYPveLAGRVFTLK--KQMLD- 172
Cdd:pfam12146 101 vdglilsapalkikpylappiLKLLAKLLGklfPRLRVPNNLLPDslsRDPEVVAAYAADP--LVHGGISARtlYELLDa 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 544827008  173 --NIQEHkiAHKVFAmnkPLLIFHATEDDTVLIEQAEKIFKAAKHP 216
Cdd:pfam12146 179 geRLLRR--AAAITV---PLLLLHGGADRVVDPAGSREFYERAGST 219
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
45-132 1.70e-06

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 48.22  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  45 AARIARKLTENAIAVLRFDFTGLGNSEgdfsNTN---FSSN-ISDLLCAVDYLRRQY-EAPSLLIGHSLGGSAILSIAGE 119
Cdd:COG0429   79 ARGLARALYARGWDVVRLNFRGCGGEP----NLLprlYHSGdTEDLVWVLAHLRARYpYAPLYAVGFSLGGNLLLKYLGE 154

                         90
                 ....*....|....*..
gi 544827008 120 ----VPEAKAVVTIGSP 132
Cdd:COG0429  155 qgddAPPLKAAVAVSPP 171
hydr2_PEP TIGR03101
exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha ...
 45-141 8.13e-06

exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 1, TIGR03100) of the same superfamily.


Pssm-ID: 274428  Cd Length: 266  Bit Score: 45.96  E-value: 8.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008   45 AARIARKLTENAIAVLRFDFTGLGNSEGDFSNTNFSSNISDLLCAVDYLRRQYEAPSLLIGHSLGGSAILSIAGEVPEAK 124
Cdd:TIGR03101  45 VALQARAFAAGGFGVLQIDLYGCGDSAGDFAAARWDVWKEDVAAAYRWLIEQGHPPVTLWGLRLGALLALDAANPLAAKC 124

                          90       100
                  ....*....|....*....|..
gi 544827008  125 AVVTIGSP-----GELTHVKRL 141
Cdd:TIGR03101 125 NRLVLWQPvvsgkQQLQQFLRL 146
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 31-241 8.52e-05

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 42.46  E-value: 8.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008   31 LLAHCFTcgkdlKGAARIARKLTENaIAVLRFDFTGLGNSEGDFSNTNFSSNISDLLCAVDYLRrqyeaPSLLIGHSLGG 110
Cdd:pfam12697   2 VLVHGAG-----LSAAPLAALLAAG-VAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGAAR-----PVVLVGHSLGG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  111 SAILSIAGEVPEAKAVV--TIGSPGELTHVKRLFKDDVENINQHGAYPVELAGRVF----TLKKQMLDNIQEHKIAHKVF 184
Cdd:pfam12697  71 AVALAAAAAALVVGVLVapLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFlddlPADAEWAAALARLAALLAAL 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544827008  185 A-------MNKPLLIFHATEDDTVLIEQAEKIFkAAKHPKSFISLGKADHLLTHAQDAeyVADI 241
Cdd:pfam12697 151 AllplaawRDLPVPVLVLAEEDRLVPELAQRLL-AALAGARLVVLPGAGHLPLDDPEE--VAEA 211
PHA02857 PHA02857
monoglyceride lipase; Provisional
 26-132 1.88e-04

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 41.80  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008  26 PKAFALLAHcfTCGKDLKGAARIARKLTENAIAVLRFDFTGLGNSEGD-FSNTNFSSNISDLLCAVDYLRRQY-EAPSLL 103
Cdd:PHA02857  24 PKALVFISH--GAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEkMMIDDFGVYVRDVVQHVVTIKSTYpGVPVFL 101

                         90       100
                 ....*....|....*....|....*....
gi 544827008 104 IGHSLGGSAILSIAGEVPEAKAVVTIGSP 132
Cdd:PHA02857 102 LGHSMGATISILAAYKNPNLFTAMILMSP 130
fabD TIGR00128
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ...
 39-135 2.73e-03

malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 272922 [Multi-domain]  Cd Length: 290  Bit Score: 38.22  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544827008   39 GKDLKGAARIARKLTENAIAVLRFDFTGLgNSEGDFSNTNFSSNISDLLCAVDY-----LRRQYE-APSLLIGHSLGGSA 112
Cdd:TIGR00128  18 GKDLYEQYPIAKELFDQASEALGYDLKKL-CQEGPAEELNKTQYTQPALYVVSAilylkLKEQGGlKPDFAAGHSLGEYS 96

                          90       100
                  ....*....|....*....|...
gi 544827008  113 ILSIAGEVPEAKAVVTIGSPGEL 135
Cdd:TIGR00128  97 ALVAAGALDFETALKLVKKRGEL 119
 
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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