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Conserved domains on  [gi|916487145|ref|WP_051127647|]
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MULTISPECIES: lipocalin family protein [Variovorax]

Protein Classification

lipocalin family protein( domain architecture ID 10006876)

lipocalin/fatty-acid binding family protein similar to Vibrio cholerae outer membrane lipoprotein Blc, which is involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Blc COG3040
Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];
1-188 2.20e-74

Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442274  Cd Length: 178  Bit Score: 221.65  E-value: 2.20e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145   1 MKRHPKyplagpALVIAAgvatMLLVAGCAVSPP-TIPTAKQVDLQRFMGDWYVIGNIPTRPERDAFNAVESYTLQPDGR 79
Cdd:COG3040    1 MKRLRL------LLALAA----ALLLAGCASAPPpPVTPVPPVDLDRYLGTWYEIARLPHRFERGCVNVTAEYSLREDGT 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145  80 IDTRFRYREGgFDGPLKTMNPVGRVVPGTGNAVWGMQFVWPVKAEYVIVDVDKDYGLTIIGRSKRDYAWIMARTPSIPEP 159
Cdd:COG3040   71 IKVINRGRKG-FDGEWKEAEGKARVVDDPTNAKLKVSFFGPFYGDYWILALDPDYQYALVGGPDRDYLWILSRTPTLPDA 149
                        170       180
                 ....*....|....*....|....*....
gi 916487145 160 AYEAAVARLKGLGYSVENLRRVPQRWPEE 188
Cdd:COG3040  150 VYQELLARARALGYDTSKLIRVPQTPPQV 178
 
Name Accession Description Interval E-value
Blc COG3040
Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];
1-188 2.20e-74

Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442274  Cd Length: 178  Bit Score: 221.65  E-value: 2.20e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145   1 MKRHPKyplagpALVIAAgvatMLLVAGCAVSPP-TIPTAKQVDLQRFMGDWYVIGNIPTRPERDAFNAVESYTLQPDGR 79
Cdd:COG3040    1 MKRLRL------LLALAA----ALLLAGCASAPPpPVTPVPPVDLDRYLGTWYEIARLPHRFERGCVNVTAEYSLREDGT 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145  80 IDTRFRYREGgFDGPLKTMNPVGRVVPGTGNAVWGMQFVWPVKAEYVIVDVDKDYGLTIIGRSKRDYAWIMARTPSIPEP 159
Cdd:COG3040   71 IKVINRGRKG-FDGEWKEAEGKARVVDDPTNAKLKVSFFGPFYGDYWILALDPDYQYALVGGPDRDYLWILSRTPTLPDA 149
                        170       180
                 ....*....|....*....|....*....
gi 916487145 160 AYEAAVARLKGLGYSVENLRRVPQRWPEE 188
Cdd:COG3040  150 VYQELLARARALGYDTSKLIRVPQTPPQV 178
Lipocalin_2 pfam08212
Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as ...
42-183 4.33e-48

Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The structure is an eight-stranded beta barrel.


Pssm-ID: 400495  Cd Length: 143  Bit Score: 153.64  E-value: 4.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145   42 VDLQRFMGDWYVIGNIPTRPERDAFNAVESYTLQPDGRIDTRFRYREggFDGPLKTMNPVGRVVPGTGNAVWGMQFVW-- 119
Cdd:pfam08212   1 VDLSRYMGTWYEIARLPMRFQRGCVDVTATYTLRDDGTIAVTNRCRT--FDGKLKTAEGVAKVADPGSNAKLKVSFLGwf 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 916487145  120 -PVKAEYVIVDVDKDYGLTIIGRSKRDYAWIMARTPSIPEPAYEAAVARLKGLGYSVENLRRVPQ 183
Cdd:pfam08212  79 fPVKGDYWVLYIDPDYSWAIVGSPSRKYLWILSRTPQLSDAQYEQLLEKARDQGYDTSKLIRVPQ 143
lipocalin_Blc-like cd19438
bacterial lipocalin Blc, Arabidopsis thaliana temperature-induced lipocalin-1, and similar ...
39-181 1.15e-43

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.


Pssm-ID: 381213  Cd Length: 143  Bit Score: 142.32  E-value: 1.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145  39 AKQVDLQRFMGDWYVIGNIPTRPERDAFNAVESYTLQPDGRIDTRFRYREGGfDGPLKTMNPVGRVVPGTGNAVWGMQFV 118
Cdd:cd19438    1 VPNVDLDRYMGTWYEIARLPNRFEKGCVNVTATYTLNDDGTISVVNRCRDGD-EGKWKEAEGKARVVDPSDNAKLKVSFF 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 916487145 119 W-PVKAEYVIVDVDKDYGLTIIGRSKRDYAWIMARTPSIPEPAYEAAVARLKGLGYSVENLRRV 181
Cdd:cd19438   80 GpPFYGDYWVLALDPDYQWALVGGPSRDYLWILSRTPQLSEETLQRLLEKARELGYDTDKLIRT 143
PRK10477 PRK10477
outer membrane lipoprotein Blc; Provisional
15-184 6.04e-17

outer membrane lipoprotein Blc; Provisional


Pssm-ID: 182489  Cd Length: 177  Bit Score: 74.36  E-value: 6.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145  15 VIAAGVATMLLVAgCavSPPTIPTAKQV----DLQRFMGDWYVIGNIPTRPERDAFNAVESYTLQPDGRIDTRFRyregG 90
Cdd:PRK10477   6 VVAAVTAAFLVVA-C--SSPTPPKGVTVvnnfDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINK----G 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145  91 FDgPLKTM--NPVGRVVpGTGN---AVWGMQFVWPVKAEYVIVDVDKDYGLTIIGRSKRDYAWIMARTPSIPEPAYEAAV 165
Cdd:PRK10477  79 YN-PDRGMwqESEGKAY-FTGAptrAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQQML 156
                        170
                 ....*....|....*....
gi 916487145 166 ARLKGLGYSVENLRRVPQR 184
Cdd:PRK10477 157 AVATREGFDVSKLIWVKQP 175
 
Name Accession Description Interval E-value
Blc COG3040
Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];
1-188 2.20e-74

Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442274  Cd Length: 178  Bit Score: 221.65  E-value: 2.20e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145   1 MKRHPKyplagpALVIAAgvatMLLVAGCAVSPP-TIPTAKQVDLQRFMGDWYVIGNIPTRPERDAFNAVESYTLQPDGR 79
Cdd:COG3040    1 MKRLRL------LLALAA----ALLLAGCASAPPpPVTPVPPVDLDRYLGTWYEIARLPHRFERGCVNVTAEYSLREDGT 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145  80 IDTRFRYREGgFDGPLKTMNPVGRVVPGTGNAVWGMQFVWPVKAEYVIVDVDKDYGLTIIGRSKRDYAWIMARTPSIPEP 159
Cdd:COG3040   71 IKVINRGRKG-FDGEWKEAEGKARVVDDPTNAKLKVSFFGPFYGDYWILALDPDYQYALVGGPDRDYLWILSRTPTLPDA 149
                        170       180
                 ....*....|....*....|....*....
gi 916487145 160 AYEAAVARLKGLGYSVENLRRVPQRWPEE 188
Cdd:COG3040  150 VYQELLARARALGYDTSKLIRVPQTPPQV 178
Lipocalin_2 pfam08212
Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as ...
42-183 4.33e-48

Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The structure is an eight-stranded beta barrel.


Pssm-ID: 400495  Cd Length: 143  Bit Score: 153.64  E-value: 4.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145   42 VDLQRFMGDWYVIGNIPTRPERDAFNAVESYTLQPDGRIDTRFRYREggFDGPLKTMNPVGRVVPGTGNAVWGMQFVW-- 119
Cdd:pfam08212   1 VDLSRYMGTWYEIARLPMRFQRGCVDVTATYTLRDDGTIAVTNRCRT--FDGKLKTAEGVAKVADPGSNAKLKVSFLGwf 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 916487145  120 -PVKAEYVIVDVDKDYGLTIIGRSKRDYAWIMARTPSIPEPAYEAAVARLKGLGYSVENLRRVPQ 183
Cdd:pfam08212  79 fPVKGDYWVLYIDPDYSWAIVGSPSRKYLWILSRTPQLSDAQYEQLLEKARDQGYDTSKLIRVPQ 143
lipocalin_Blc-like cd19438
bacterial lipocalin Blc, Arabidopsis thaliana temperature-induced lipocalin-1, and similar ...
39-181 1.15e-43

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.


Pssm-ID: 381213  Cd Length: 143  Bit Score: 142.32  E-value: 1.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145  39 AKQVDLQRFMGDWYVIGNIPTRPERDAFNAVESYTLQPDGRIDTRFRYREGGfDGPLKTMNPVGRVVPGTGNAVWGMQFV 118
Cdd:cd19438    1 VPNVDLDRYMGTWYEIARLPNRFEKGCVNVTATYTLNDDGTISVVNRCRDGD-EGKWKEAEGKARVVDPSDNAKLKVSFF 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 916487145 119 W-PVKAEYVIVDVDKDYGLTIIGRSKRDYAWIMARTPSIPEPAYEAAVARLKGLGYSVENLRRV 181
Cdd:cd19438   80 GpPFYGDYWVLALDPDYQWALVGGPSRDYLWILSRTPQLSEETLQRLLEKARELGYDTDKLIRT 143
PRK10477 PRK10477
outer membrane lipoprotein Blc; Provisional
15-184 6.04e-17

outer membrane lipoprotein Blc; Provisional


Pssm-ID: 182489  Cd Length: 177  Bit Score: 74.36  E-value: 6.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145  15 VIAAGVATMLLVAgCavSPPTIPTAKQV----DLQRFMGDWYVIGNIPTRPERDAFNAVESYTLQPDGRIDTRFRyregG 90
Cdd:PRK10477   6 VVAAVTAAFLVVA-C--SSPTPPKGVTVvnnfDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINK----G 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145  91 FDgPLKTM--NPVGRVVpGTGN---AVWGMQFVWPVKAEYVIVDVDKDYGLTIIGRSKRDYAWIMARTPSIPEPAYEAAV 165
Cdd:PRK10477  79 YN-PDRGMwqESEGKAY-FTGAptrAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQQML 156
                        170
                 ....*....|....*....
gi 916487145 166 ARLKGLGYSVENLRRVPQR 184
Cdd:PRK10477 157 AVATREGFDVSKLIWVKQP 175
lipocalin_apoD-like cd19437
apolipoprotein D and similar proteins; Human apolipoprotein D (ApoD) is a small glycoprotein ...
34-183 5.18e-13

apolipoprotein D and similar proteins; Human apolipoprotein D (ApoD) is a small glycoprotein associated with high density lipoproteins (HDL) in plasma. It appears promiscuous since it can bind hydrophobic ligands belonging to different lipid groups, with different shapes and biochemical properties; however, it exhibits specificity between very similar lipidic species. Some ligands, such as progesterone and arachidonic acid, bind to the ligand-binding pocket with high affinity, while others may interact with ApoD via its region of surface hydrophobicity. This hydrophobic surface cluster may facilitate its association with HDL particles and facilitate its insertion into cellular lipid membranes. Drosophila NLaz and Schistocerca Laz belong to this group, and share functional properties with human ApoD, including regulation of lifespan, lipid and carbohydrate metabolism control, and protection against oxidative stress or starvation. This group also includes Sandercyanin, a blue protein secreted in the skin mucus of blue forms of walleye, Sander vitreus. Walleye is an important golden yellow commercial and sport fish; the findings of blue walleye are recent. 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.


Pssm-ID: 381212 [Multi-domain]  Cd Length: 160  Bit Score: 63.80  E-value: 5.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145  34 PTIPTAKQVDLQRFMGDWYVIGNIPTRPERDAFNAVESYTLQPDG--RIDTRFRYReggFDGPLKTMNPVGRVVPGTGNA 111
Cdd:cd19437    5 PTVPVQEDFDVDKYLGRWYEIERYPAPFEKGGDCVTANYSLNDDGtvRVVNSGINL---TDGSINTIEGSARCPDPNEPA 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 916487145 112 VWGMQFVW-PVKAEYVIVDVDKD-YGL-----TIIGRSKRDYAWIMARTPSIPEPAYEAAVARLKGLGYSVENLRRVPQ 183
Cdd:cd19437   82 KLGVSFPGfPPAGPYWVLDTDYDnYAIvysctDVLGLFKVEYAWILSRQRTLSAETLTKAKEILTSYGIDVSKLKKTDQ 160
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
48-184 1.73e-06

Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The family also encompasses the enzyme prostaglandin D synthase (EC:5.3.99.2). Alignment subsumes both the lipocalin and fatty acid binding protein signatures from PROSITE. This is supported on structural and functional grounds. The structure is an eight-stranded beta barrel.


Pssm-ID: 395015  Cd Length: 143  Bit Score: 45.51  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145   48 MGDWYVIGNIPTRpERDAFNA-----VESYTLQPDGRIDTRFRYREGGfdgPLKTMNPVGRVVpgTGNAVWGMQFVWPVK 122
Cdd:pfam00061   1 SGKWYLIASANFN-ELEEEMKalgvgFATIKVLENGNLPVTEITKEGG---KCKTVSVTFKKT--EEPGKLGVEFDEYAG 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 916487145  123 AEYVIVdVDKDYGLTIIGRSKRD-------YAWIMARTPSIPEPAYEAAVARLKGLGYSVENLRRVPQR 184
Cdd:pfam00061  75 GRKVKV-LTTDYDNYLIFYQKGDkdgkttiVRELYGRDPELSPELLEKFKKFLKELGIDEENIVRLYQK 142
lipocalin_FABP cd00301
lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low ...
46-152 1.85e-06

lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, 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 have a large beta-barrel ligand-binding cavity. Members include retinol-binding protein, retinoic acid-binding protein, complement protein C8 gamma, Can f 2, apolipoprotein D, extracellular fatty acid-binding protein, beta-lactoglobulin, oderant-binding protein, and bacterial lipocalin Blc. Lipocalins are involved in many important 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 are involved in protection and shuttling of fatty acids within the cell, and in acquisition and removal of fatty acids from intracellular sites.


Pssm-ID: 381182  Cd Length: 109  Bit Score: 44.84  E-value: 1.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916487145  46 RFMGDWYVIGNIPTRPERDAFNAVES-YTLQPDG--RIDTRFRyreggFDGPLKTMNpvGRVVPGTGNAVWGMQF-VWPV 121
Cdd:cd00301    1 KFSGKWYEVASASNAPEEDEGKCTTAeYTLEGNGnlKVTNSFV-----RDGVCKSIT--GTLKKTDGPGKFTVTYpGYTG 73
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 916487145 122 KAEYVIVDVD-KDYGL----TIIGRSKRDYAWIMAR 152
Cdd:cd00301   74 KNELYVLSTDyDNYAIvyscKNLDGGHTVVAWLLSR 109
 
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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