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Conserved domains on  [gi|664527196|ref|WP_031043667|]
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MULTISPECIES: alpha/beta hydrolase [Streptomyces]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11429202)

alpha/beta hydrolase 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:  37582413|12369917|19508187

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
65-198 1.16e-16

Acetyl esterase/lipase [Lipid transport and metabolism];


:

Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 76.84  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196  65 LHGGSWRAPYDRRHISPFAGFLAQRGFAVASVEYRRgargpggedAGEpvaGRWPDTFDDVAAAVDALPELVRRHlpGAD 144
Cdd:COG0657   19 FHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRL---------APE---HPFPAALEDAYAALRWLRANAAEL--GID 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 664527196 145 VRRMVLTGHSAGGHLALWAASRHvlpadapwRTDRPAPLRGVVALAPIADFEVA 198
Cdd:COG0657   85 PDRIAVAGDSAGGHLAAALALRA--------RDRGGPRPAAQVLIYPVLDLTAS 130
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
65-198 1.16e-16

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 76.84  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196  65 LHGGSWRAPYDRRHISPFAGFLAQRGFAVASVEYRRgargpggedAGEpvaGRWPDTFDDVAAAVDALPELVRRHlpGAD 144
Cdd:COG0657   19 FHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRL---------APE---HPFPAALEDAYAALRWLRANAAEL--GID 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 664527196 145 VRRMVLTGHSAGGHLALWAASRHvlpadapwRTDRPAPLRGVVALAPIADFEVA 198
Cdd:COG0657   85 PDRIAVAGDSAGGHLAAALALRA--------RDRGGPRPAAQVLIYPVLDLTAS 130
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
85-194 1.57e-10

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 59.55  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196   85 FLAQRGFAVASVEYRrGarGPG-GEDAGEPVAGRWPD-TFDDVAAAVDALPELvrrhlPGADVRRMVLTGHSAGGHLALW 162
Cdd:pfam00326   9 LLADRGYVVAIANGR-G--SGGyGEAFHDAGKGDLGQnEFDDFIAAAEYLIEQ-----GYTDPDRLAIWGGSYGGYLTGA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 664527196  163 AAsrhvlpadapwrTDRPAPLRGVVALAPIAD 194
Cdd:pfam00326  81 AL------------NQRPDLFKAAVAHVPVVD 100
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
 129-193 2.94e-04

S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and human, with a conserved critical role in formaldehyde detoxification as S-formylglutathione hydrolase (EC 3.1.2.12). Members in eukaryotes such as the human protein are better known as esterase D (EC 3.1.1.1), an enzyme with broad specificity, although S-formylglutathione hydrolase has now been demonstrated as well. [Cellular processes, Detoxification]


Pssm-ID: 131868  Cd Length: 275  Bit Score: 41.69  E-value: 2.94e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664527196  129 VDALPELVRRHLPgADVRRMVLTGHSAGGHLALWAASRHvlpadapwrtdrPAPLRGVVALAPIA 193
Cdd:TIGR02821 122 VQELPALVAAQFP-LDGERQGITGHSMGGHGALVIALKN------------PDRFKSVSAFAPIV 173
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 118-191 5.45e-03

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 36.71  E-value: 5.45e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664527196 118 WPDTFDDVAAAVDALPELVRRHLPGADVrrmVLTGHSAGGHLALWAASRhvlpadapWRTDRPAPLRGVVALAP 191
Cdd:cd00741    3 FYKAARSLANLVLPLLKSALAQYPDYKI---HVTGHSLGGALAGLAGLD--------LRGRGLGRLVRVYTFGP 65
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
65-198 1.16e-16

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 76.84  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196  65 LHGGSWRAPYDRRHISPFAGFLAQRGFAVASVEYRRgargpggedAGEpvaGRWPDTFDDVAAAVDALPELVRRHlpGAD 144
Cdd:COG0657   19 FHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRL---------APE---HPFPAALEDAYAALRWLRANAAEL--GID 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 664527196 145 VRRMVLTGHSAGGHLALWAASRHvlpadapwRTDRPAPLRGVVALAPIADFEVA 198
Cdd:COG0657   85 PDRIAVAGDSAGGHLAAALALRA--------RDRGGPRPAAQVLIYPVLDLTAS 130
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
65-293 4.95e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 72.74  E-value: 4.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196  65 LHGGSWRAPYDRRhisPFAGFLAQRGFAVASVEYRrgarGPGGEdagepvAGRWP-DTFDDVAAAVDALpelvrRHLPGA 143
Cdd:COG1506   29 VHGGPGSRDDSFL---PLAQALASRGYAVLAPDYR----GYGES------AGDWGgDEVDDVLAAIDYL-----AARPYV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196 144 DVRRMVLTGHSAGGHLALWAASRHvlpadapwrtdrPAPLRGVVALAPIADFevADQLGVCGGAARQLLGSEKLFAERRP 223
Cdd:COG1506   91 DPDRIGIYGHSYGGYMALLAAARH------------PDRFKAAVALAGVSDL--RSYYGTTREYTERLMGGPWEDPEAYA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 664527196 224 YADPALLLPT-GIATTLVQGRADVDVPQAVADAYADAAAKAGEVVGVTLLEDVGHYPLIDPAADACAVVAE 293
Cdd:COG1506  157 ARSPLAYADKlKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFSGAGAPDYLERILD 227
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
85-194 1.57e-10

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 59.55  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196   85 FLAQRGFAVASVEYRrGarGPG-GEDAGEPVAGRWPD-TFDDVAAAVDALPELvrrhlPGADVRRMVLTGHSAGGHLALW 162
Cdd:pfam00326   9 LLADRGYVVAIANGR-G--SGGyGEAFHDAGKGDLGQnEFDDFIAAAEYLIEQ-----GYTDPDRLAIWGGSYGGYLTGA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 664527196  163 AAsrhvlpadapwrTDRPAPLRGVVALAPIAD 194
Cdd:pfam00326  81 AL------------NQRPDLFKAAVAHVPVVD 100
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
81-287 1.24e-08

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 54.24  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196  81 PFAGFLAQRGFAVASVEYRrgarGPGGEDAGEPVAGRWPDTFDDVAAAVDALpelvrRHLPGADVrrmVLTGHSAGGHLA 160
Cdd:COG2267   46 ELAEALAAAGYAVLAFDLR----GHGRSDGPRGHVDSFDDYVDDLRAALDAL-----RARPGLPV---VLLGHSMGGLIA 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196 161 LWAASRHvlpadapwrtdrPAPLRGVVALAPiaDFEVADQLGVCGGAARQLLGSEKLfaerrpyadPALLLPtgiaTTLV 240
Cdd:COG2267  114 LLYAARY------------PDRVAGLVLLAP--AYRADPLLGPSARWLRALRLAEAL---------ARIDVP----VLVL 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 664527196 241 QGRADVDVPQAVADAYADAAAKAGEVVgvtLLEDVGHYPLIDPAADA 287
Cdd:COG2267  167 HGGADRVVPPEAARRLAARLSPDVELV---LLPGARHELLNEPAREE 210
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 66-164 1.72e-08

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 53.72  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196   66 HGGSW-------RAPYDRRHISPFAgflaQRGFAVASVEYRRgargpggedAGEpvaGRWPDTFDDVAAAVdalpELVRR 138
Cdd:pfam20434  20 HGGGWnsgdkeaDMGFMTNTVKALL----KAGYAVASINYRL---------STD---AKFPAQIQDVKAAI----RFLRA 79

                          90       100
                  ....*....|....*....|....*...
gi 664527196  139 HLP--GADVRRMVLTGHSAGGHLALWAA 164
Cdd:pfam20434  80 NAAkyGIDTNKIALMGFSAGGHLALLAG 107
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
76-167 1.28e-07

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 51.51  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196  76 RRHISPFAGFLAQRGFAVASVE-YRRGARGPGGEDAGEPVAGRWPD-TFDDVAAAVDALpelvrRHLPGADVRRMVLTGH 153
Cdd:COG0412   42 NPHIRDVARRLAAAGYVVLAPDlYGRGGPGDDPDEARALMGALDPElLAADLRAALDWL-----KAQPEVDAGRVGVVGF 116

                         90
                 ....*....|....
gi 664527196 154 SAGGHLALWAASRH 167
Cdd:COG0412  117 CFGGGLALLAAARG 130
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
65-196 7.21e-07

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 49.17  E-value: 7.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196  65 LHG--GSwraPYDrrhISPFAGFLAQRGFAVASVEYrrgargPG-GEDAGEPVAGRWPDTFDDVAAAVDALpelvrrhlp 141
Cdd:COG1647   21 LHGftGS---PAE---MRPLAEALAKAGYTVYAPRL------PGhGTSPEDLLKTTWEDWLEDVEEAYEIL--------- 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 664527196 142 GADVRRMVLTGHSAGGHLALWAASRHvlpadapwrtdrpAPLRGVVALAPIADFE 196
Cdd:COG1647   80 KAGYDKVIVIGLSMGGLLALLLAARY-------------PDVAGLVLLSPALKID 121
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
76-190 2.11e-06

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


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 48.34  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196  76 RRHISPFAGFLAQRGFAVASVEYR-RGARGPGgedAGEPVAGRWPDTFD-DVAAAVDALpelvRRHLPGadvRRMVLTGH 153
Cdd:COG4757   45 QRFYRPFARYLAERGFAVLTYDYRgIGLSRPG---SLRGFDAGYRDWGElDLPAVLDAL----RARFPG---LPLLLVGH 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 664527196 154 SAGGHLALWAASRH------VLPADAPWRTDRPAPLRGVVALA 190
Cdd:COG4757  115 SLGGQLLGLAPNAErvdrlvTVASGSGYWRDYPPRRRLKVLLF 157
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 78-167 2.40e-06

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 47.99  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196  78 HISPFAGFLAQRGFAVASVEYRRGargpgGEDAGEPVAGRWPDTFDdVAAAVDALpelvrRHLPGADVRRMVLTGHSAGG 157
Cdd:COG1073   52 QRALYAQRLAELGFNVLAFDYRGY-----GESEGEPREEGSPERRD-ARAAVDYL-----RTLPGVDPERIGLLGISLGG 120

                         90
                 ....*....|
gi 664527196 158 HLALWAASRH 167
Cdd:COG1073  121 GYALNAAATD 130
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 65-298 8.11e-05

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: 43.07  E-value: 8.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196  65 LHGGswraPYDRRHISPFAGFLAQRgFAVASVEyRRGArgpgGEDAGEPVAGRWPDTFDDVAAAVDALpelvrrhlpgaD 144
Cdd:COG0596   29 LHGL----PGSSYEWRPLIPALAAG-YRVIAPD-LRGH----GRSDKPAGGYTLDDLADDLAALLDAL-----------G 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196 145 VRRMVLTGHSAGGHLALWAASRHvlpadapwrtdrPAPLRGVVALAPIADfEVADQLGVCGGAARQLLGsekLFAERRPY 224
Cdd:COG0596   88 LERVVLVGHSMGGMVALELAARH------------PERVAGLVLVDEVLA-ALAEPLRRPGLAPEALAA---LLRALART 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664527196 225 ADPALLLPTGIATTLVQGRADVDVPQAVADAYADAAAKagevVGVTLLEDVGHYPLIDPAADACAVVAEEIAQL 298
Cdd:COG0596  152 DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPN----AELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 65-191 9.56e-05

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: 42.97  E-value: 9.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196   65 LHGG---SWRapYDRrhispFAGFLAQRGFAVasveYRRGARGPGGEDaGEPvaGRWPDtFDDVAAAVDALPELVRRHLP 141
Cdd:pfam12146  10 VHGLgehSGR--YAH-----LADALAAQGFAV----YAYDHRGHGRSD-GKR--GHVPS-FDDYVDDLDTFVDKIREEHP 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 664527196  142 GadvRRMVLTGHSAGGHLALWAASRHvlpadapwrtdrPAPLRGVVALAP 191
Cdd:pfam12146  75 G---LPLFLLGHSMGGLIAALYALRY------------PDKVDGLILSAP 109
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
 129-193 2.94e-04

S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and human, with a conserved critical role in formaldehyde detoxification as S-formylglutathione hydrolase (EC 3.1.2.12). Members in eukaryotes such as the human protein are better known as esterase D (EC 3.1.1.1), an enzyme with broad specificity, although S-formylglutathione hydrolase has now been demonstrated as well. [Cellular processes, Detoxification]


Pssm-ID: 131868  Cd Length: 275  Bit Score: 41.69  E-value: 2.94e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664527196  129 VDALPELVRRHLPgADVRRMVLTGHSAGGHLALWAASRHvlpadapwrtdrPAPLRGVVALAPIA 193
Cdd:TIGR02821 122 VQELPALVAAQFP-LDGERQGITGHSMGGHGALVIALKN------------PDRFKSVSAFAPIV 173
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
75-200 4.02e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 41.25  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196  75 DRRHISPFAGFLAQRGFAVASVEY----RRGARGPGGEDAGEPVAGRWPDTFDDVAAAVDALPELVRRHLPGA---DVRR 147
Cdd:COG4188   74 SREGYAYLAEHLASHGYVVAAPDHpgsnAADLSAALDGLADALDPEELWERPLDLSFVLDQLLALNKSDPPLAgrlDLDR 153

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 664527196 148 MVLTGHSAGGHLALWAASRHVLPADAPWRTDRPAPLRGVVALAPIADFEVADQ 200
Cdd:COG4188  154 IGVIGHSLGGYTALALAGARLDFAALRQYCGKNPDLQCRALDLPRLAYDLRDP 206
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
132-245 3.94e-03

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 37.89  E-value: 3.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196 132 LPELVRRHLPGADVR-RMVLTGHSAGGHLALWAASRHvlpadapwrtdrPAPLRGVVALAPIADFevaDQLGVCGGAARQ 210
Cdd:COG0627   98 LPPLIEANFPVSADReRRAIAGLSMGGHGALTLALRH------------PDLFRAVAAFSGILDP---SQPPWGEKAFDA 162

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 664527196 211 LLGSEKLFAERRpyADPALL---LPTGIATTLVQGRAD 245
Cdd:COG0627  163 YFGPPDRAAWAA--NDPLALaekLRAGLPLYIDCGTAD 198
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 81-191 4.21e-03

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 36.35  E-value: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196  81 PFAGFLAQRGFAVASVEYrrgargpggedagepvagrwPDTFDDVAAAVDALPELVRRHLPGADVRRMVLTGHSAGGHLA 160
Cdd:COG1075   23 PLAPRLRAAGYPVYALNY--------------------PSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGHSMGGLVA 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 664527196 161 LWAASRHvlpadapwrtDRPAPLRGVVALAP 191
Cdd:COG1075   83 RYYLKRL----------GGAAKVARVVTLGT 103
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 132-186 4.77e-03

Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 37.83  E-value: 4.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664527196  132 LPELVRRHLPGADVRRmVLTGHSAGGHLALWAASRH-------------VLPADAPW-RTDRPAPLRGV 186
Cdd:pfam00756  97 LPPLLDANFPTAPDGR-ALAGQSMGGLGALYLALKYpdlfgsvssfspiLNPSNSMWgPEDDPAWQEGD 164
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 118-191 5.45e-03

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 36.71  E-value: 5.45e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664527196 118 WPDTFDDVAAAVDALPELVRRHLPGADVrrmVLTGHSAGGHLALWAASRhvlpadapWRTDRPAPLRGVVALAP 191
Cdd:cd00741    3 FYKAARSLANLVLPLLKSALAQYPDYKI---HVTGHSLGGALAGLAGLD--------LRGRGLGRLVRVYTFGP 65
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
 85-164 7.90e-03

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 37.48  E-value: 7.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664527196  85 FLAQRGFAVASVEYR-----RGARGPGGEDAGEPVAGRW------PDT------FDDVAAAVDALpelvrRHLPGADVRR 147
Cdd:COG3458  103 DWAAAGYAVLVMDTRgqgssWGDTPDPGGYSGGALPGYMtrgiddPDTyyyrrvYLDAVRAVDAL-----RSLPEVDGKR 177

                         90
                 ....*....|....*..
gi 664527196 148 MVLTGHSAGGHLALWAA 164
Cdd:COG3458  178 IGVTGGSQGGGLALAAA 194
 
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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