NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16131974|ref|NP_418573|]
View 

outer membrane lipoprotein Blc [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

lipocalin family protein( domain architecture ID 10013536)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK10477 PRK10477
outer membrane lipoprotein Blc; Provisional
 1-177 2.25e-142

outer membrane lipoprotein Blc; Provisional


:

Pssm-ID: 182489  Cd Length: 177  Bit Score: 392.53  E-value: 2.25e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974    1 MRLLPLVAAATAAFLVVACSSPTPPRGVTVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYN 80
Cdd:PRK10477   1 MRLLPVVAAVTAAFLVVACSSPTPPKGVTVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974   81 PDRGMWQQSEGKAYFTGAPTRAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQEMLAVAT 160
Cdd:PRK10477  81 PDRGMWQESEGKAYFTGAPTRAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQQMLAVAT 160

                        170
                 ....*....|....*..
gi 16131974  161 REGFDVSKFIWVQQPGS 177
Cdd:PRK10477 161 REGFDVSKLIWVKQPGS 177
 
Name Accession Description Interval E-value
PRK10477 PRK10477
outer membrane lipoprotein Blc; Provisional
 1-177 2.25e-142

outer membrane lipoprotein Blc; Provisional


Pssm-ID: 182489  Cd Length: 177  Bit Score: 392.53  E-value: 2.25e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974    1 MRLLPLVAAATAAFLVVACSSPTPPRGVTVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYN 80
Cdd:PRK10477   1 MRLLPVVAAVTAAFLVVACSSPTPPKGVTVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974   81 PDRGMWQQSEGKAYFTGAPTRAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQEMLAVAT 160
Cdd:PRK10477  81 PDRGMWQESEGKAYFTGAPTRAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQQMLAVAT 160

                        170
                 ....*....|....*..
gi 16131974  161 REGFDVSKFIWVQQPGS 177
Cdd:PRK10477 161 REGFDVSKLIWVKQPGS 177
Blc COG3040
Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];
1-177 1.27e-103

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


Pssm-ID: 442274  Cd Length: 178  Bit Score: 294.83  E-value: 1.27e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974   1 MRLLPLVAAATAAFLVVACSSpTPPRGVTVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYN 80
Cdd:COG3040   1 MKRLRLLLALAAALLLAGCAS-APPPPVTPVPPVDLDRYLGTWYEIARLPHRFERGCVNVTAEYSLREDGTIKVINRGRK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974  81 PDRGMWQQSEGKAYFTGAPTRAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQEMLAVAT 160
Cdd:COG3040  80 GFDGEWKEAEGKARVVDDPTNAKLKVSFFGPFYGDYWILALDPDYQYALVGGPDRDYLWILSRTPTLPDAVYQELLARAR 159

                       170
                ....*....|....*..
gi 16131974 161 REGFDVSKFIWVQQPGS 177
Cdd:COG3040 160 ALGYDTSKLIRVPQTPP 176
lipocalin_Blc-like cd19438
bacterial lipocalin Blc, Arabidopsis thaliana temperature-induced lipocalin-1, and similar ...
 31-172 8.17e-76

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: 223.21  E-value: 8.17e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974  31 VNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYNPDRGMWQQSEGKAYFTGAPTRAALKVSFFG 110
Cdd:cd19438   1 VPNVDLDRYMGTWYEIARLPNRFEKGCVNVTATYTLNDDGTISVVNRCRDGDEGKWKEAEGKARVVDPSDNAKLKVSFFG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131974 111 -PFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQEMLAVATREGFDVSKFIWV 172
Cdd:cd19438  81 pPFYGDYWVLALDPDYQWALVGGPSRDYLWILSRTPQLSEETLQRLLEKARELGYDTDKLIRT 143
Lipocalin_2 pfam08212
Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as ...
 34-174 6.39e-58

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: 177.91  E-value: 6.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974    34 FDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYNPDrGMWQQSEGKAYFTGAPTRAALKVSFFG--- 110
Cdd:pfam08212   1 VDLSRYMGTWYEIARLPMRFQRGCVDVTATYTLRDDGTIAVTNRCRTFD-GKLKTAEGVAKVADPGSNAKLKVSFLGwff 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131974   111 PFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQEMLAVATREGFDVSKFIWVQQ 174
Cdd:pfam08212  80 PVKGDYWVLYIDPDYSWAIVGSPSRKYLWILSRTPQLSDAQYEQLLEKARDQGYDTSKLIRVPQ 143
 
Name Accession Description Interval E-value
PRK10477 PRK10477
outer membrane lipoprotein Blc; Provisional
 1-177 2.25e-142

outer membrane lipoprotein Blc; Provisional


Pssm-ID: 182489  Cd Length: 177  Bit Score: 392.53  E-value: 2.25e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974    1 MRLLPLVAAATAAFLVVACSSPTPPRGVTVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYN 80
Cdd:PRK10477   1 MRLLPVVAAVTAAFLVVACSSPTPPKGVTVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974   81 PDRGMWQQSEGKAYFTGAPTRAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQEMLAVAT 160
Cdd:PRK10477  81 PDRGMWQESEGKAYFTGAPTRAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQQMLAVAT 160

                        170
                 ....*....|....*..
gi 16131974  161 REGFDVSKFIWVQQPGS 177
Cdd:PRK10477 161 REGFDVSKLIWVKQPGS 177
Blc COG3040
Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];
1-177 1.27e-103

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


Pssm-ID: 442274  Cd Length: 178  Bit Score: 294.83  E-value: 1.27e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974   1 MRLLPLVAAATAAFLVVACSSpTPPRGVTVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYN 80
Cdd:COG3040   1 MKRLRLLLALAAALLLAGCAS-APPPPVTPVPPVDLDRYLGTWYEIARLPHRFERGCVNVTAEYSLREDGTIKVINRGRK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974  81 PDRGMWQQSEGKAYFTGAPTRAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQEMLAVAT 160
Cdd:COG3040  80 GFDGEWKEAEGKARVVDDPTNAKLKVSFFGPFYGDYWILALDPDYQYALVGGPDRDYLWILSRTPTLPDAVYQELLARAR 159

                       170
                ....*....|....*..
gi 16131974 161 REGFDVSKFIWVQQPGS 177
Cdd:COG3040 160 ALGYDTSKLIRVPQTPP 176
lipocalin_Blc-like cd19438
bacterial lipocalin Blc, Arabidopsis thaliana temperature-induced lipocalin-1, and similar ...
 31-172 8.17e-76

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: 223.21  E-value: 8.17e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974  31 VNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYNPDRGMWQQSEGKAYFTGAPTRAALKVSFFG 110
Cdd:cd19438   1 VPNVDLDRYMGTWYEIARLPNRFEKGCVNVTATYTLNDDGTISVVNRCRDGDEGKWKEAEGKARVVDPSDNAKLKVSFFG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131974 111 -PFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQEMLAVATREGFDVSKFIWV 172
Cdd:cd19438  81 pPFYGDYWVLALDPDYQWALVGGPSRDYLWILSRTPQLSEETLQRLLEKARELGYDTDKLIRT 143
Lipocalin_2 pfam08212
Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as ...
 34-174 6.39e-58

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: 177.91  E-value: 6.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974    34 FDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYNPDrGMWQQSEGKAYFTGAPTRAALKVSFFG--- 110
Cdd:pfam08212   1 VDLSRYMGTWYEIARLPMRFQRGCVDVTATYTLRDDGTIAVTNRCRTFD-GKLKTAEGVAKVADPGSNAKLKVSFLGwff 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131974   111 PFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQEMLAVATREGFDVSKFIWVQQ 174
Cdd:pfam08212  80 PVKGDYWVLYIDPDYSWAIVGSPSRKYLWILSRTPQLSDAQYEQLLEKARDQGYDTSKLIRVPQ 143
lipocalin_apoD-like cd19437
apolipoprotein D and similar proteins; Human apolipoprotein D (ApoD) is a small glycoprotein ...
 22-174 2.26e-44

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: 143.93  E-value: 2.26e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974  22 PTPPrgvtVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYNPDRGMWQQSEGKAYFTGAPTR 101
Cdd:cd19437   5 PTVP----VQEDFDVDKYLGRWYEIERYPAPFEKGGDCVTANYSLNDDGTVRVVNSGINLTDGSINTIEGSARCPDPNEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974 102 AALKVSFFG-PFYGGYNVIALDREyRHALV--CGpDR------DYLWILSRTPTISDEVKQEMLAVATREGFDVSKFIWV 172
Cdd:cd19437  81 AKLGVSFPGfPPAGPYWVLDTDYD-NYAIVysCT-DVlglfkvEYAWILSRQRTLSAETLTKAKEILTSYGIDVSKLKKT 158


                ..
gi 16131974 173 QQ 174
Cdd:cd19437 159 DQ 160
lipocalin_FABP cd00301
lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low ...
 38-143 8.56e-15

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: 66.80  E-value: 8.56e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974  38 RYLGTWYEIARFDHRFERGLEK-VTATYSLRDDGGLNVINKGYNPdrGMWQQSEGKAYFTGAPtrAALKVSF-FGPFYGG 115
Cdd:cd00301   1 KFSGKWYEVASASNAPEEDEGKcTTAEYTLEGNGNLKVTNSFVRD--GVCKSITGTLKKTDGP--GKFTVTYpGYTGKNE 76

                        90       100       110
                ....*....|....*....|....*....|....
gi 16131974 116 YNVIALDREyRHALVC------GPDRDYLWILSR 143
Cdd:cd00301  77 LYVLSTDYD-NYAIVYscknldGGHTVVAWLLSR 109
lipocalin_Bla_g_4_Per_a_4 cd19440
major allergens Bla g 4 and Per a 4; Inhalant allergens from cockroaches are an important ...
 25-155 9.63e-12

major allergens Bla g 4 and Per a 4; Inhalant allergens from cockroaches are an important cause of asthma. Bla g 4 and Per a 4 are male pheromone transport lipocalins, and both are major allergens. Bla g 4 is produced by Blattella germanica (German cockroach) and has been shown to bind two biogenic amines, tyramine and octopamine which may be its physiological ligands. Per a 4 is produced by Periplaneta americana (American cockroach) and may bind different ligands from Bla g 4 or have different modes for tyramine/octopamine binding. 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: 381215  Cd Length: 148  Bit Score: 59.81  E-value: 9.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974  25 PRGVTVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYNpdrgmwqqSEGKAYFTgapTRAAL 104
Cdd:cd19440   2 QRGDSLFTGFDYTKYLGVWYEAFRTPNAHEEQYKCWIDRFSLDPEGPIAVTSVAYD--------SRGKNRVT---LTGTV 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131974 105 KVSFFGPFYGGYN----------VIALDREyRHALVCG-PDRDY----LWILSRTPTISDEVKQEM 155
Cdd:cd19440  71 PVSTGNKFDIDYGddeawssqywVLGTDYE-TYAILAGcPAQDSnkhlIWVQSRDTSFDNATKKAV 135
lipocalin_crustacyanin cd19436
crustacyanin Type I CRTC and Type II CRTA subunits; Alpha crustacyanin bound with the ...
 32-177 1.90e-11

crustacyanin Type I CRTC and Type II CRTA subunits; Alpha crustacyanin bound with the carotenoid astaxanthisn (AXT) is the predominant cartenoprotein generating the slate-grey/blue color of the lobster carapace. Crustacyanin forms heterodimers (beta-crustacyanin) or complexes of 16 subunits (alpha-crustacyanin) assembled from beta-crustacyanin. Beta-crustacyanin is formed from one type I CRTC lipocalin subunit, and one type II CRTA lipocalin subunit (and two bound astaxanthin molecules). Homarus gammarus (European lobster) crustacyanin has of five distinct subunits evident on 6 M urea-PAGE gels: type I CRTC ( A1, C1, C2) and type II CRTA ( A2, A3). Homarus americanus crustacyanin consists of only two major subunits, namely type I CRTC (H1) and type II CRTA (H2), both of which behave like Ax subunits on a 6 M urea-PAGE gel. This family includes both type I CRTC subunit and type II CRTA subunits and 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: 381211  Cd Length: 169  Bit Score: 59.41  E-value: 1.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974  32 NNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRD-DGGLNVINKGYNPDrGMWQQSEGKAYFTGAPTRAALKVSFFG 110
Cdd:cd19436  17 DNFDLRRYAGRWYQTHLINNPYQPVTRCVHSNYSYSGsDYGFKVTSAGFNPD-NNYLKRNGKVYPTKEFPAAHMLIDYPS 95

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131974 111 PFYGGYNVIALDRE-YRHALVC----GPDRDYLWILSRTPTISDEVKQEMLAVATREGFDVSKFIWVQQPGS 177
Cdd:cd19436  96 VFAAPYEVIETDYEnYSCVYSCidtdGYKSEFGFVFSRSPQLAGPAVEKCAAVFKKNGVDFSRFVPVVHTSD 167
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
 40-170 2.54e-08

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: 50.52  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131974    40 LGTWYEIAR-FDHRFERGLEKV---TATYSLRDDGGLNVINKGYNPDRgMWQQSeGKAYFTGAPTRaaLKVSFFGpFYGG 115
Cdd:pfam00061   1 SGKWYLIASaNFNELEEEMKALgvgFATIKVLENGNLPVTEITKEGGK-CKTVS-VTFKKTEEPGK--LGVEFDE-YAGG 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131974   116 YNVIALDREYRHALVC-------GPDRDYLWILSRTPTISDEVKQEMLAVATREGFDVSKFI 170
Cdd:pfam00061  76 RKVKVLTTDYDNYLIFyqkgdkdGKTTIVRELYGRDPELSPELLEKFKKFLKELGIDEENIV 137
lipocalin_RBP_like cd00743
retinol-binding protein 4 and similar proteins; Retinol-Binding Protein 4 (RBP4) is a plasma ...
 29-78 9.13e-05

retinol-binding protein 4 and similar proteins; Retinol-Binding Protein 4 (RBP4) is a plasma protein that transports retinol (vitamin A) from the liver stores to the peripheral tissues. The RBP4-retinol complex interacts with transthyretin (TTR - transports thyroxine and retinol) which protects it from renal excretion. In addition to retinol, other endogenous and synthetic retinoids bind RBP4, including all-trans and 13-cis retinoic acid, retinyl acetate, N-(ethyl)retinamide, and fenretinide. This group also includes purpurin, a retinol-specific protein that plays a role in neural retina cell adhesion during development of the chicken retina; it also binds retinol and may participate in retinol transporter in the retina. 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: 381184  Cd Length: 171  Bit Score: 40.89  E-value: 9.13e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 16131974  29 TVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKG 78
Cdd:cd00743   7 RVKENFDKARYAGTWYAMAKKDPEGLFLQDNIVAEFSVDENGTMTATAKG 56
 
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