2ACO,3MBT


Conserved Protein Domain Family
lipocalin_Blc-like

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cd19438: lipocalin_Blc-like 
bacterial lipocalin Blc, Arabidopsis thaliana temperature-induced lipocalin-1, and similar proteins
Escherichia coli bacterial lipocalin (Blc, also known as YjeL) is an outer membrane lipoprotein involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Blc has a binding preference for lysophospholipids. This group includes eukaryotic lipocalins such as Arabidopsis thaliana temperature-induced lipocalin-1 (TIL) which is involved in thermotolerance, oxidative, salt, drought and high light stress tolerance, and is needed for seed longevity by ensuring polyunsaturated lipids integrity. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.
Statistics
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PSSM-Id: 381213
Aligned: 94 rows
Threshold Bit Score: 98.0187
Created: 7-Feb-2006
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
ligand bindingdimer interface
Conserved site includes 10 residues -Click on image for an interactive view with Cn3D
Feature 1:ligand binding cavity [chemical binding site]
Evidence:
  • Comment:hydrophobic cavity binds different hydrophobic ligands; ligands are bound within the beta-barrel in a central internal water-filled cavity lined with polar and hydrophobic amino acids
  • Comment:based on Escherichia coli lipocalin Blc and on other lipocalin/cytosolic fatty-acid binding protein family members with structure
  • Structure:2ACO: Escherichia coli lipocalin Blc bound with vaccenic acid, contacts at 4A

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                               ##                          #                         
2ACO_B     27 VNNFDAKRYLGTWYEIARFDHr----FERGLE-KVTATYSLRd----dGGLNVINKGYNpd-rgMWQQSEGKAYFTGapt 96  Escherichia coli
CAK83008   20 VQTLNVTQYLGNWYEVASSPWvh-ltFEKDAF-CNRATYGLQq----dGNLSVLNMERYgspsgEIKQITGYAYIPNpel 93  Paramecium tetraur...
XP_782410  40 VNELDVQAYLGRWYQVYTDLVvn-vtFERNAK-CVTADYGLNa----dGTISVFNANTVgtpdgDFNTITGTATVPDasq 113 purple urchin
CAK85713   20 VDDYDVESYLGDWFEVASSPWvh-ttFEKNGF-CNRARYGVLg----sGDLSVYNVQRDgagdgAIKSIDGYARIPDltq 93  Paramecium tetraur...
CBN77358   20 VPDLDVAKYIGRWYQLYGNTFta--rITRDGT-CVAADYGLDqa---tGNITVINSERIgvptgRLQTIEGFAYGTGpsn 93  Ectocarpus silicul...
BAD57912   35 VTSVDLDRYVGRWHQLAAIPQp----FNLACArDTTAEYTPLp----tGDVGVHNRCTTwa--gGIDEIRGTARVNDpvt 104 Nocardia farcinica...
BAC17455   58 DQKVDLERYQGKWYQVAAIPQp----YTLQCSnDTTAEYEKId----eNTISVANSCGTp---fGPSVIQGKATVRSd-- 124 Corynebacterium ef...
GAB19654   42 ISKLDVPRYLGVWNQVAAVPQp----FNLDCLsSTQAKYSKId----dRNIRVENSCIRnn--gSRNRIVGNARVNDlkt 111 Gordonia effusa NB...
XP_794498  31 VYDIDVNKYVGVWYNMYTNFWadsftGTDGAE-CTTAEYGKIs----dTNVTVYNAYSVre--gRSDTIEGYAWIPFlve 103 purple urchin
NP_509849 392 TPTVDLSKFMGRWFEGINSPRa----TEQRCVvHHYGGLTRNdktatfTALKVYREGSEf---gPVKYSLGYAFRGGnk- 463 Caenorhabditis ele...
Feature 1            ##        ## ##                                #                         
2ACO_B     97 rAALKVSFFg-------PFYGGYNVIALDr---------eYRHALVCGPDRDYLWILSRTPti-----sDEVKQEMLAVA 155 Escherichia coli
CAK83008   94 pGQLKVHLEga-----pFEYADYWIVQLGpvk-----neqYQWAIVSEPSKFFMWVLARDPveynllyaTQVQNTVTNTL 163 Paramecium tetraur...
XP_782410 114 pGKLTVQFPg------vPVPGDYWILKLGpvv-----ggqYQYSVVSDSNKATLFVLARDAsaf---mgSDEKETVLEFL 179 purple urchin
CAK85713   94 kAKLKVFLNgg-----qVGGGDYWIIELGpvi-----nkkYQWVIVSEPEMLFMWVLSRNPqq----yrEEYEDYVRDRV 159 Paramecium tetraur...
CBN77358   94 pGQLKVHLGd------vPVDGDYWVVGLGpdtfg--pdslYQWALVSGPDAESLFVLVRDVre----feKTYARDVLEFV 161 Ectocarpus silicul...
BAD57912  105 nAQLHVSFPgvptqdrlDGPTNYIVTALGp---------dYSWAVVTDPNRLSGFVLAREPal-----dESGWAAVRSAI 170 Nocardia farcinica...
BAC17455  125 -ASLKVTFGgvpf-qteEGEPNYRVTYLEd---------dYSLAIVGSPNRLSGFVLSRTPdl-----sPEDWTKVRNIT 188 Corynebacterium ef...
GAB19654  112 lAQLHVSFPgvpfqsskSGPTNYVVTYIAp---------dYSWALVGDPNRLSGFVLKRTSdv-----sKKQWDSIKKVI 177 Gordonia effusa NB...
XP_794498 104 pGRLLVRLEg------vPLATPYFIIKLGpiv-----nnqYEYSIVSDPAAAALFVLARDPet----fdMMYDAEVREYL 168 purple urchin
NP_509849 464 dAMLQLHSSe------tSDAQPFWIYKLGpegknsfgdsqYEYAIISNWVKYPVTVLVRDPdt----fkTKYQKEVLRWL 533 Caenorhabditis ele...
Feature 1                       
2ACO_B    156 TREGFDv-----sKFIWV 168 Escherichia coli
CAK83008  164 QFDGRFn-----sYVVRP 176 Paramecium tetraurelia
XP_782410 180 RESGFKc------FWNRP 191 purple urchin
CAK85713  160 SALGFNgv---lnKYVPR 174 Paramecium tetraurelia
CBN77358  162 AELGFTgr---dkEPQRV 176 Ectocarpus siliculosus
BAD57912  171 VAAGQNpc----fYLTTP 184 Nocardia farcinica IFM 10152
BAC17455  189 EDRGWWs-----cAFVTV 201 Corynebacterium efficiens YS-314
GAB19654  178 SARGYNtc----fFLVTP 191 Gordonia effusa NBRC 100432
XP_794498 169 LVTGFTtp---ptQPVRV 183 purple urchin
NP_509849 534 EDQGFIngfirafNLLQP 551 Caenorhabditis elegans

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