NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1895569168|ref|WP_186281725|]
View 

MULTISPECIES: alpha/beta hydrolase [Bifidobacterium]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
BD-FAE super family cl48589
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 46-253 9.95e-67

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.


The actual alignment was detected with superfamily member pfam20434:

Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 207.42  E-value: 9.95e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  46 MPEGAmpEGGWPVIVFVRGSAFHEQNVTDYSNY----FVRIAEQGYVVAALKYRHSDIAPFPAQMQDCKTAVRFMRKNAE 121
Cdd:pfam20434   5 LPKNA--KGPYPVVIWIHGGGWNSGDKEADMGFmtntVKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRANAA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 122 RFHCNKDRIALWGDSSGGHTVLMAGFTGN-RAPDTD--AYAEESA----EVNAIVDWHGPTDFAKMnfyPSSQNHSDPQC 194
Cdd:pfam20434  83 KYGIDTNKIALMGFSAGGHLALLAGLSNNnKEFEGNvgDYTPESSkesfKVNAVVDFYGPTDLLDM---DSCGTHNDAKS 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1895569168 195 PEGVVIGGGdVLEHPDLSAQASPMTYLSADmpTPSTLIMHGGRDQLVPFNQSCRLYATL 253
Cdd:pfam20434 160 PETLLLGAP-PLENPDLAKSASPITYVDKN--DPPFLIIHGDKDPLVPYCQSVLLHEKL 215
 
Name Accession Description Interval E-value
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 46-253 9.95e-67

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: 207.42  E-value: 9.95e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  46 MPEGAmpEGGWPVIVFVRGSAFHEQNVTDYSNY----FVRIAEQGYVVAALKYRHSDIAPFPAQMQDCKTAVRFMRKNAE 121
Cdd:pfam20434   5 LPKNA--KGPYPVVIWIHGGGWNSGDKEADMGFmtntVKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRANAA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 122 RFHCNKDRIALWGDSSGGHTVLMAGFTGN-RAPDTD--AYAEESA----EVNAIVDWHGPTDFAKMnfyPSSQNHSDPQC 194
Cdd:pfam20434  83 KYGIDTNKIALMGFSAGGHLALLAGLSNNnKEFEGNvgDYTPESSkesfKVNAVVDFYGPTDLLDM---DSCGTHNDAKS 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1895569168 195 PEGVVIGGGdVLEHPDLSAQASPMTYLSADmpTPSTLIMHGGRDQLVPFNQSCRLYATL 253
Cdd:pfam20434 160 PETLLLGAP-PLENPDLAKSASPITYVDKN--DPPFLIIHGDKDPLVPYCQSVLLHEKL 215
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
36-292 1.43e-37

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 131.92  E-value: 1.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  36 MWVFTPgvdnmpegAMPEGGWPVIVFVRGSAFHEQNVTDYSNYFVRIAEQ-GYVVAALKYRHSDIAPFPAQMQDCKTAVR 114
Cdd:COG0657     1 MDVYRP--------AGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARaGAAVVSVDYRLAPEHPFPAALEDAYAALR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 115 FMRKNAERFHCNKDRIALWGDSSGGHTVLMAGFtgnRAPDTDAyaeesAEVNAIVDWHGPTDFAkmnfypssqnhsdpqc 194
Cdd:COG0657    73 WLRANAAELGIDPDRIAVAGDSAGGHLAAALAL---RARDRGG-----PRPAAQVLIYPVLDLT---------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 195 pegvvigggdvlehpdlsaqASPMTYLSADMPtPsTLIMHGGRDQLVPfnQSCRLYATLKALGKDVTFYKLDNACHACYG 274
Cdd:COG0657   129 --------------------ASPLRADLAGLP-P-TLIVTGEADPLVD--ESEALAAALRAAGVPVELHVYPGGGHGFGL 184

                         250       260
                  ....*....|....*....|..
gi 1895569168 275 F----RSARALRLVFDWLSDRL 292
Cdd:COG0657   185 LaglpEARAALAEIAAFLRRAL 206
PRK10162 PRK10162
acetyl esterase;
58-145 4.07e-06

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 47.41  E-value: 4.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  58 VIVFVRGSAFHEQNVtDYSNYFVRI--AEQGYVVAALKYRHSDIAPFPAQMQDCKTAVRFMRKNAERFHCNKDRIALWGD 135
Cdd:PRK10162   83 TLFYLHGGGFILGNL-DTHDRIMRLlaSYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIGFAGD 161

                          90
                  ....*....|
gi 1895569168 136 SSGGHTVLMA 145
Cdd:PRK10162  162 SAGAMLALAS 171
 
Name Accession Description Interval E-value
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 46-253 9.95e-67

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: 207.42  E-value: 9.95e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  46 MPEGAmpEGGWPVIVFVRGSAFHEQNVTDYSNY----FVRIAEQGYVVAALKYRHSDIAPFPAQMQDCKTAVRFMRKNAE 121
Cdd:pfam20434   5 LPKNA--KGPYPVVIWIHGGGWNSGDKEADMGFmtntVKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRANAA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 122 RFHCNKDRIALWGDSSGGHTVLMAGFTGN-RAPDTD--AYAEESA----EVNAIVDWHGPTDFAKMnfyPSSQNHSDPQC 194
Cdd:pfam20434  83 KYGIDTNKIALMGFSAGGHLALLAGLSNNnKEFEGNvgDYTPESSkesfKVNAVVDFYGPTDLLDM---DSCGTHNDAKS 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1895569168 195 PEGVVIGGGdVLEHPDLSAQASPMTYLSADmpTPSTLIMHGGRDQLVPFNQSCRLYATL 253
Cdd:pfam20434 160 PETLLLGAP-PLENPDLAKSASPITYVDKN--DPPFLIIHGDKDPLVPYCQSVLLHEKL 215
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
36-292 1.43e-37

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 131.92  E-value: 1.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  36 MWVFTPgvdnmpegAMPEGGWPVIVFVRGSAFHEQNVTDYSNYFVRIAEQ-GYVVAALKYRHSDIAPFPAQMQDCKTAVR 114
Cdd:COG0657     1 MDVYRP--------AGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARaGAAVVSVDYRLAPEHPFPAALEDAYAALR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 115 FMRKNAERFHCNKDRIALWGDSSGGHTVLMAGFtgnRAPDTDAyaeesAEVNAIVDWHGPTDFAkmnfypssqnhsdpqc 194
Cdd:COG0657    73 WLRANAAELGIDPDRIAVAGDSAGGHLAAALAL---RARDRGG-----PRPAAQVLIYPVLDLT---------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 195 pegvvigggdvlehpdlsaqASPMTYLSADMPtPsTLIMHGGRDQLVPfnQSCRLYATLKALGKDVTFYKLDNACHACYG 274
Cdd:COG0657   129 --------------------ASPLRADLAGLP-P-TLIVTGEADPLVD--ESEALAAALRAAGVPVELHVYPGGGHGFGL 184

                         250       260
                  ....*....|....*....|..
gi 1895569168 275 F----RSARALRLVFDWLSDRL 292
Cdd:COG0657   185 LaglpEARAALAEIAAFLRRAL 206
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
27-292 1.41e-30

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 114.73  E-value: 1.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  27 ADGssVDLPMWVFTPGvdnmpegamPEGGWPVIVFVRGSAFHEQNvtDYSNYFVRIAEQGYVVAALKYR---HSDIAPFP 103
Cdd:COG1506     5 ADG--TTLPGWLYLPA---------DGKKYPVVVYVHGGPGSRDD--SFLPLAQALASRGYAVLAPDYRgygESAGDWGG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 104 AQMQDCKTAVRFMRknaERFHCNKDRIALWGDSSGGHTVLMAGFTgnrapDTDAYAeesaevnAIVDWHGPTDFAkmNFY 183
Cdd:COG1506    72 DEVDDVLAAIDYLA---ARPYVDPDRIGIYGHSYGGYMALLAAAR-----HPDRFK-------AAVALAGVSDLR--SYY 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 184 PSSQNHSDPQCpegvviggGDVLEHPDLSAQASPMTYLsADMPTPsTLIMHGGRDQLVPFNQSCRLYATLKALGKDVTFY 263
Cdd:COG1506   135 GTTREYTERLM--------GGPWEDPEAYAARSPLAYA-DKLKTP-LLLIHGEADDRVPPEQAERLYEALKKAGKPVELL 204

                         250       260
                  ....*....|....*....|....*....
gi 1895569168 264 KLDNACHACYGFRSARALRLVFDWLSDRL 292
Cdd:COG1506   205 VYPGEGHGFSGAGAPDYLERILDFLDRHL 233
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
83-288 3.70e-15

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 72.65  E-value: 3.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  83 AEQGYVVAALKYR---------HSDIAPFPAQ--MQDCKTAVRFMrknAERFHCNKDRIALWGDSSGGHTVLMAGftgNR 151
Cdd:pfam00326  11 ADRGYVVAIANGRgsggygeafHDAGKGDLGQneFDDFIAAAEYL---IEQGYTDPDRLAIWGGSYGGYLTGAAL---NQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 152 APDTDAYAeesAEVNAIVDWhgptdfakMNFYpssqnhSDPQCPEGV-VIGGGDVLEHPDLSAQASPMTYLSADMPTPST 230
Cdd:pfam00326  85 RPDLFKAA---VAHVPVVDW--------LAYM------SDTSLPFTErYMEWGNPWDNEEGYDYLSPYSPADNVKVYPPL 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895569168 231 LIMHGGRDQLVPFNQSCRLYATLKALGKDVTFYKLDNACHacyGFRSARA----LRLVFDWL 288
Cdd:pfam00326 148 LLIHGLLDDRVPPWQSLKLVAALQRKGVPFLLLIFPDEGH---GIGKPRNkveeYARELAFL 206
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 59-273 4.83e-15

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 72.24  E-value: 4.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  59 IVFVRGSAFHEQNVTDYSNYFVRIAEQ-GYVVAALKYRHSDIAPFPAQMQDCKTAVRFMRKNAERFHCNKDRIALWGDSS 137
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEaGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 138 GGHtvlMAGFTGNRAPDtdayaEESAEVNAIVDWHGPTDFAKMNF-YPSSQNHSDPQCPEGVV-------IGGGDvLEHP 209
Cdd:pfam07859  81 GGN---LAAAVALRARD-----EGLPKPAGQVLIYPGTDLRTESPsYLAREFADGPLLTRAAMdwfwrlyLPGAD-RDDP 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1895569168 210 DLS-AQASPMTYLsadmptPSTLIMHGGRDQLVPfnQSCRLYATLKALGKDVTFYKLDNACHACY 273
Cdd:pfam07859 152 LASpLFASDLSGL------PPALVVVAEFDPLRD--EGEAYAERLRAAGVPVELIEYPGMPHGFH 208
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 12-292 8.05e-15

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 72.25  E-value: 8.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  12 YPVNIEQVTYVTRqlaDGssVDLPMWVFTPgvdnmpegAMPEGGWPVIVFVRGSAfheQNVTDYSNYFVRIAEQGYVVAA 91
Cdd:COG1073     6 DKVNKEDVTFKSR---DG--IKLAGDLYLP--------AGASKKYPAVVVAHGNG---GVKEQRALYAQRLAELGFNVLA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  92 LKYRH---SDIAP----FPAQmQDCKTAVRFMRKNAERfhcNKDRIALWGDSSGGHTVLMAGFTGNRApdtDAYAEESae 164
Cdd:COG1073    70 FDYRGygeSEGEPreegSPER-RDARAAVDYLRTLPGV---DPERIGLLGISLGGGYALNAAATDPRV---KAVILDS-- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 165 vnaivdwhGPTDFAKMNFYPSSQNhsdpqcpEGVVIGGGDVLEHPDL----SAQASPMTYLSA-DMPTpstLIMHGGRDQ 239
Cdd:COG1073   141 --------PFTSLEDLAAQRAKEA-------RGAYLPGVPYLPNVRLasllNDEFDPLAKIEKiSRPL---LFIHGEKDE 202

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1895569168 240 LVPFNQSCRLYatlKALGKDVTFYKLDNACHA-CYGFRSARALRLVFDWLSDRL 292
Cdd:COG1073   203 AVPFYMSEDLY---EAAAEPKELLIVPGAGHVdLYDRPEEEYFDKLAEFFKKNL 253
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
17-288 1.16e-12

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 65.76  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  17 EQVTYVTrqlADGssVDLPMWVFTPGVDnmpegampeGGWPVIVFV---RGSAFHEQNVTDysnyfvRIAEQGYVVAAL- 92
Cdd:COG0412     4 ETVTIPT---PDG--VTLPGYLARPAGG---------GPRPGVVVLheiFGLNPHIRDVAR------RLAAAGYVVLAPd 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  93 ------KYRHSDIA-------PFPAQMQDCKTAVRFMRKNAErfhCNKDRIALWGDSSGGHTVLMAgftgnrapdtdayA 159
Cdd:COG0412    64 lygrggPGDDPDEAralmgalDPELLAADLRAALDWLKAQPE---VDAGRVGVVGFCFGGGLALLA-------------A 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 160 EESAEVNAIVDWHGptdfakmnfypssqnhsdpqcpegvvigggdVLEHPDLSAQAspmtylsADMPTPsTLIMHGGRDQ 239
Cdd:COG0412   128 ARGPDLAAAVSFYG-------------------------------GLPADDLLDLA-------ARIKAP-VLLLYGEKDP 168

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1895569168 240 LVPFNQSCRLYATLKALGKDVTFYKLDNACHA-------CYGFRSA-RALRLVFDWL 288
Cdd:COG0412   169 LVPPEQVAALEAALAAAGVDVELHVYPGAGHGftnpgrpRYDPAAAeDAWQRTLAFL 225
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
57-290 1.28e-07

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 51.16  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  57 PVIVFVRGSafheqnvTDYSNYFVRIAE----QGYVVAALKYR--------HSDIAPFPAQMQDCKTAVRFMRKNAERfh 124
Cdd:COG2267    29 GTVVLVHGL-------GEHSGRYAELAEalaaAGYAVLAFDLRghgrsdgpRGHVDSFDDYVDDLRAALDALRARPGL-- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 125 cnkdRIALWGDSSGGHTVLmagftgnrapdtdAYAEEsaevnaivdwhgptdfakmnfypssqnhsDPQCPEGVVIGGGD 204
Cdd:COG2267   100 ----PVVLLGHSMGGLIAL-------------LYAAR-----------------------------YPDRVAGLVLLAPA 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 205 VLEHPDLSAQASPMTYLS-----ADMPTPsTLIMHGGRDQLVPFNQSCRLYAtlkALGKDVTFYKLDNACHACYGFR-SA 278
Cdd:COG2267   134 YRADPLLGPSARWLRALRlaealARIDVP-VLVLHGGADRVVPPEAARRLAA---RLSPDVELVLLPGARHELLNEPaRE 209

                         250
                  ....*....|..
gi 1895569168 279 RALRLVFDWLSD 290
Cdd:COG2267   210 EVLAAILAWLER 221
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
12-270 3.41e-06

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 47.79  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  12 YPVNIEQVTYVTRQladgSSVDLPMWVFTPGvdNMPEGAMPEGGWPVIVFVRGSAfheQNVTDYSNYFVRIAEQGYVVAA 91
Cdd:COG4188    24 FAVGVQTLTLRDPS----RDRPLPVDVWYPA--TAPADAPAGGPFPLVVLSHGLG---GSREGYAYLAEHLASHGYVVAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  92 LKYRHS---DIAPFPAQMQDCKTAVRF----------------MRKNAERF--HCNKDRIALWGDSSGGHTVLMAGftGN 150
Cdd:COG4188    95 PDHPGSnaaDLSAALDGLADALDPEELwerpldlsfvldqllaLNKSDPPLagRLDLDRIGVIGHSLGGYTALALA--GA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 151 RaPDTDAYAEESAEvnaivdwHGPTDFAKMNFYPSSQNHSDPQCPEGVVI--GGGDVLEHPDLSAqaspmtylsadMPTP 228
Cdd:COG4188   173 R-LDFAALRQYCGK-------NPDLQCRALDLPRLAYDLRDPRIKAVVALapGGSGLFGEEGLAA-----------ITIP 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1895569168 229 sTLIMHGGRDQLVPF-NQSCRLYATLKALGKD-VTfykLDNACH 270
Cdd:COG4188   234 -VLLVAGSADDVTPApDEQIRPFDLLPGADKYlLT---LEGATH 273
PRK10162 PRK10162
acetyl esterase;
58-145 4.07e-06

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 47.41  E-value: 4.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  58 VIVFVRGSAFHEQNVtDYSNYFVRI--AEQGYVVAALKYRHSDIAPFPAQMQDCKTAVRFMRKNAERFHCNKDRIALWGD 135
Cdd:PRK10162   83 TLFYLHGGGFILGNL-DTHDRIMRLlaSYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIGFAGD 161

                          90
                  ....*....|
gi 1895569168 136 SSGGHTVLMA 145
Cdd:PRK10162  162 SAGAMLALAS 171
YpfH COG0400
Predicted esterase [General function prediction only];
205-292 8.04e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 39.89  E-value: 8.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168 205 VLEHPDLSAQA---SPM-------TYLSADMPTPSTLIMHGGRDQLVPFNQSCRLYATLKALGKDVTFYKLDNAcHACyg 274
Cdd:COG0400   107 ALRRPELLAGVvalSGYlpgeealPAPEAALAGTPVFLAHGTQDPVIPVERAREAAEALEAAGADVTYREYPGG-HEI-- 183

                          90
                  ....*....|....*...
gi 1895569168 275 frSARALRLVFDWLSDRL 292
Cdd:COG0400   184 --SPEELADARAWLAERL 199
PLN00021 PLN00021
chlorophyllase
 34-142 2.19e-03

chlorophyllase


Pssm-ID: 177659  Cd Length: 313  Bit Score: 38.88  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  34 LPMWVFTPGVdnmpegampEGGWPVIVFVRGsaFHEQNvTDYSNYFVRIAEQGYVVAALkyRHSDIAPfPAQMQDCKTAV 113
Cdd:PLN00021   39 KPLLVATPSE---------AGTYPVLLFLHG--YLLYN-SFYSQLLQHIASHGFIVVAP--QLYTLAG-PDGTDEIKDAA 103

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1895569168 114 RFMRKNAERFHC--------NKDRIALWGDSSGGHTV 142
Cdd:PLN00021  104 AVINWLSSGLAAvlpegvrpDLSKLALAGHSRGGKTA 140
PAF-AH_p_II pfam03403
Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor ...
 52-130 3.47e-03

Platelet-activating factor acetylhydrolase, isoform II; Platelet-activating factor acetylhydrolase (PAF-AH) is a subfamily of phospholipases A2, responsible for inactivation of platelet-activating factor through cleavage of an acetyl group. Three known PAF-AHs are the brain heterotrimeric PAF-AH Ib, whose catalytic beta and gamma subunits are aligned in pfam02266, the extracellular, plasma PAF-AH (pPAF-AH), and the intracellular PAF-AH isoform II (PAF-AH II). This family aligns pPAF-AH and PAF-AH II, whose similarity was previously noted.


Pssm-ID: 397462 [Multi-domain]  Cd Length: 372  Bit Score: 38.58  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  52 PEGGWPVIVFVRG-SAFHeqnvTDYSNYFVRIAEQGYVVAALKYR-HSDIAPF-----PAQMQDCKTAVRFMRKNAER-F 123
Cdd:pfam03403  96 TGEKYPLIVFSHGlGAFR----TIYSAICIELASHGFVVAAVEHRdRSASATYffkdkPAAEEEQKSWIYLRKVKEEEeF 171


                  ....*..
gi 1895569168 124 HCNKDRI 130
Cdd:pfam03403 172 HLRNEQV 178
COesterase pfam00135
Carboxylesterase family;
38-139 3.54e-03

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 38.83  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  38 VFTPgvDNMPEgamPEGGWPVIVFVRGSAFHEQNVTDYSNYFVrIAEQGYVVAALKYR---------HSDIAPFPAQMQD 108
Cdd:pfam00135  90 VYTP--KELKE---NKNKLPVMVWIHGGGFMFGSGSLYDGSYL-AAEGDVIVVTINYRlgplgflstGDDEAPGNYGLLD 163

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1895569168 109 CKTAVRFMRKNAERFHCNKDRIALWGDSSGG 139
Cdd:pfam00135 164 QVLALRWVQENIASFGGDPNRVTLFGESAGA 194
Chlorophyllase pfam07224
Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1. ...
 53-141 4.87e-03

Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1.1.14). Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of ester bond to yield chlorophyllide and phytol.


Pssm-ID: 254111  Cd Length: 307  Bit Score: 37.90  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895569168  53 EGGWPVIVFVRGSAFHEQnvtDYSNYFVRIAEQGYVVAALK-YRhsdIAPFPAQMQDCKTA---VRFMRKNAERF----- 123
Cdd:pfam07224  43 AGTYPVVLFLHGTMLSNE---FYSLFFNHIASHGFIVVAPQlYR---LFPPPSQQDEIDSAaevANWLPLGLQVVlptgv 116

                          90
                  ....*....|....*...
gi 1895569168 124 HCNKDRIALWGDSSGGHT 141
Cdd:pfam07224 117 EANLSKLALSGHSRGGKT 134
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH