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Conserved domains on  [gi|554702983|gb|ESK08493|]
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hypothetical protein G723_02759 [Escherichia coli HVH 50 (4-2593475)]

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

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List of domain hits

 Name Accession Description Interval E-value
PRK10477 PRK10477
outer membrane lipoprotein Blc; Provisional
 1-174 3.35e-124

outer membrane lipoprotein Blc; Provisional


:

Pssm-ID: 182489  Cd Length: 177  Bit Score: 346.69  E-value: 3.35e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983   1 MKLWPVLTGIALSFTLIACKAPTPPKGVQPITNFDANRYLGKWYEIARLENWFERGLEQVSATYEKRNDGGIRVLNRGYD 80
Cdd:PRK10477   1 MRLLPVVAAVTAAFLVVACSSPTPPKGVTVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983  81 PTKNKWSESEGKAYFTGDTKTAALKVSFFGPFYGGYNVIKLDDEYKYALVSGPNREYLWILARTQTIPDNVKADYVRTAQ 160
Cdd:PRK10477  81 PDRGMWQESEGKAYFTGAPTRAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQQMLAVAT 160

                        170
                 ....*....|....
gi 554702983 161 KLGFNVNELLWVKQ 174
Cdd:PRK10477 161 REGFDVSKLIWVKQ 174
 
Name Accession Description Interval E-value
PRK10477 PRK10477
outer membrane lipoprotein Blc; Provisional
 1-174 3.35e-124

outer membrane lipoprotein Blc; Provisional


Pssm-ID: 182489  Cd Length: 177  Bit Score: 346.69  E-value: 3.35e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983   1 MKLWPVLTGIALSFTLIACKAPTPPKGVQPITNFDANRYLGKWYEIARLENWFERGLEQVSATYEKRNDGGIRVLNRGYD 80
Cdd:PRK10477   1 MRLLPVVAAVTAAFLVVACSSPTPPKGVTVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983  81 PTKNKWSESEGKAYFTGDTKTAALKVSFFGPFYGGYNVIKLDDEYKYALVSGPNREYLWILARTQTIPDNVKADYVRTAQ 160
Cdd:PRK10477  81 PDRGMWQESEGKAYFTGAPTRAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQQMLAVAT 160

                        170
                 ....*....|....
gi 554702983 161 KLGFNVNELLWVKQ 174
Cdd:PRK10477 161 REGFDVSKLIWVKQ 174
Blc COG3040
Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];
1-174 1.40e-95

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


Pssm-ID: 442274  Cd Length: 178  Bit Score: 274.42  E-value: 1.40e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983   1 MKLWPVLTGIALSFTLIACkAPTPPKGVQPITNFDANRYLGKWYEIARLENWFERGLEQVSATYEKRNDGGIRVLNRGYD 80
Cdd:COG3040    1 MKRLRLLLALAAALLLAGC-ASAPPPPVTPVPPVDLDRYLGTWYEIARLPHRFERGCVNVTAEYSLREDGTIKVINRGRK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983  81 PTKNKWSESEGKAYFTGDTKTAALKVSFFGPFYGGYNVIKLDDEYKYALVSGPNREYLWILARTQTIPDNVKADYVRTAQ 160
Cdd:COG3040   80 GFDGEWKEAEGKARVVDDPTNAKLKVSFFGPFYGDYWILALDPDYQYALVGGPDRDYLWILSRTPTLPDAVYQELLARAR 159

                        170
                 ....*....|....
gi 554702983 161 KLGFNVNELLWVKQ 174
Cdd:COG3040  160 ALGYDTSKLIRVPQ 173
lipocalin_Blc-like cd19438
bacterial lipocalin Blc, Arabidopsis thaliana temperature-induced lipocalin-1, and similar ...
 33-172 6.02e-70

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: 208.19  E-value: 6.02e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983  33 NFDANRYLGKWYEIARLENWFERGLEQVSATYEKRNDGGIRVLNRGYDPTKNKWSESEGKAYFTGDTKTAALKVSFFG-P 111
Cdd:cd19438    3 NVDLDRYMGTWYEIARLPNRFEKGCVNVTATYTLNDDGTISVVNRCRDGDEGKWKEAEGKARVVDPSDNAKLKVSFFGpP 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 554702983 112 FYGGYNVIKLDDEYKYALVSGPNREYLWILARTQTIPDNVKADYVRTAQKLGFNVNELLWV 172
Cdd:cd19438   83 FYGDYWVLALDPDYQWALVGGPSRDYLWILSRTPQLSEETLQRLLEKARELGYDTDKLIRT 143
Lipocalin_2 pfam08212
Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as ...
 34-174 7.44e-51

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: 159.81  E-value: 7.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983   34 FDANRYLGKWYEIARLENWFERGLEQVSATYEKRNDGGIRVLNRGYDPtKNKWSESEGKAYFTGDTKTAALKVSFFG--- 110
Cdd:pfam08212   1 VDLSRYMGTWYEIARLPMRFQRGCVDVTATYTLRDDGTIAVTNRCRTF-DGKLKTAEGVAKVADPGSNAKLKVSFLGwff 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 554702983  111 PFYGGYNVIKLDDEYKYALVSGPNREYLWILARTQTIPDNVKADYVRTAQKLGFNVNELLWVKQ 174
Cdd:pfam08212  80 PVKGDYWVLYIDPDYSWAIVGSPSRKYLWILSRTPQLSDAQYEQLLEKARDQGYDTSKLIRVPQ 143
 
Name Accession Description Interval E-value
PRK10477 PRK10477
outer membrane lipoprotein Blc; Provisional
 1-174 3.35e-124

outer membrane lipoprotein Blc; Provisional


Pssm-ID: 182489  Cd Length: 177  Bit Score: 346.69  E-value: 3.35e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983   1 MKLWPVLTGIALSFTLIACKAPTPPKGVQPITNFDANRYLGKWYEIARLENWFERGLEQVSATYEKRNDGGIRVLNRGYD 80
Cdd:PRK10477   1 MRLLPVVAAVTAAFLVVACSSPTPPKGVTVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983  81 PTKNKWSESEGKAYFTGDTKTAALKVSFFGPFYGGYNVIKLDDEYKYALVSGPNREYLWILARTQTIPDNVKADYVRTAQ 160
Cdd:PRK10477  81 PDRGMWQESEGKAYFTGAPTRAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQQMLAVAT 160

                        170
                 ....*....|....
gi 554702983 161 KLGFNVNELLWVKQ 174
Cdd:PRK10477 161 REGFDVSKLIWVKQ 174
Blc COG3040
Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];
1-174 1.40e-95

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


Pssm-ID: 442274  Cd Length: 178  Bit Score: 274.42  E-value: 1.40e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983   1 MKLWPVLTGIALSFTLIACkAPTPPKGVQPITNFDANRYLGKWYEIARLENWFERGLEQVSATYEKRNDGGIRVLNRGYD 80
Cdd:COG3040    1 MKRLRLLLALAAALLLAGC-ASAPPPPVTPVPPVDLDRYLGTWYEIARLPHRFERGCVNVTAEYSLREDGTIKVINRGRK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983  81 PTKNKWSESEGKAYFTGDTKTAALKVSFFGPFYGGYNVIKLDDEYKYALVSGPNREYLWILARTQTIPDNVKADYVRTAQ 160
Cdd:COG3040   80 GFDGEWKEAEGKARVVDDPTNAKLKVSFFGPFYGDYWILALDPDYQYALVGGPDRDYLWILSRTPTLPDAVYQELLARAR 159

                        170
                 ....*....|....
gi 554702983 161 KLGFNVNELLWVKQ 174
Cdd:COG3040  160 ALGYDTSKLIRVPQ 173
lipocalin_Blc-like cd19438
bacterial lipocalin Blc, Arabidopsis thaliana temperature-induced lipocalin-1, and similar ...
 33-172 6.02e-70

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: 208.19  E-value: 6.02e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983  33 NFDANRYLGKWYEIARLENWFERGLEQVSATYEKRNDGGIRVLNRGYDPTKNKWSESEGKAYFTGDTKTAALKVSFFG-P 111
Cdd:cd19438    3 NVDLDRYMGTWYEIARLPNRFEKGCVNVTATYTLNDDGTISVVNRCRDGDEGKWKEAEGKARVVDPSDNAKLKVSFFGpP 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 554702983 112 FYGGYNVIKLDDEYKYALVSGPNREYLWILARTQTIPDNVKADYVRTAQKLGFNVNELLWV 172
Cdd:cd19438   83 FYGDYWVLALDPDYQWALVGGPSRDYLWILSRTPQLSEETLQRLLEKARELGYDTDKLIRT 143
Lipocalin_2 pfam08212
Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as ...
 34-174 7.44e-51

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: 159.81  E-value: 7.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983   34 FDANRYLGKWYEIARLENWFERGLEQVSATYEKRNDGGIRVLNRGYDPtKNKWSESEGKAYFTGDTKTAALKVSFFG--- 110
Cdd:pfam08212   1 VDLSRYMGTWYEIARLPMRFQRGCVDVTATYTLRDDGTIAVTNRCRTF-DGKLKTAEGVAKVADPGSNAKLKVSFLGwff 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 554702983  111 PFYGGYNVIKLDDEYKYALVSGPNREYLWILARTQTIPDNVKADYVRTAQKLGFNVNELLWVKQ 174
Cdd:pfam08212  80 PVKGDYWVLYIDPDYSWAIVGSPSRKYLWILSRTPQLSDAQYEQLLEKARDQGYDTSKLIRVPQ 143
lipocalin_apoD-like cd19437
apolipoprotein D and similar proteins; Human apolipoprotein D (ApoD) is a small glycoprotein ...
 20-174 7.45e-41

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: 135.07  E-value: 7.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983  20 KAPTPPkgVQPitNFDANRYLGKWYEIARLENWFERGLEQVSATYEKRNDGGIRVLNRGYDPTKNKWSESEGKAYFTGDT 99
Cdd:cd19437    3 KCPTVP--VQE--DFDVDKYLGRWYEIERYPAPFEKGGDCVTANYSLNDDGTVRVVNSGINLTDGSINTIEGSARCPDPN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983 100 KTAALKVSFFG-PFYGGYNVikLDDEYK-YALV-SGPNR------EYLWILARTQTIPDNVKADYVRTAQKLGFNVNELL 170
Cdd:cd19437   79 EPAKLGVSFPGfPPAGPYWV--LDTDYDnYAIVySCTDVlglfkvEYAWILSRQRTLSAETLTKAKEILTSYGIDVSKLK 156


                 ....
gi 554702983 171 WVKQ 174
Cdd:cd19437  157 KTDQ 160
lipocalin_FABP cd00301
lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low ...
 38-143 1.33e-09

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: 52.93  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983  38 RYLGKWYEIARLENWFERGLEQVS-ATYEKRNDGGIRVLNRGYDPtkNKWSESEGKAYFTGDtktaALKVSFFGPFYGGY 116
Cdd:cd00301    1 KFSGKWYEVASASNAPEEDEGKCTtAEYTLEGNGNLKVTNSFVRD--GVCKSITGTLKKTDG----PGKFTVTYPGYTGK 74

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 554702983 117 NVIK-LDDEYK-YALV------SGPNREYLWILAR 143
Cdd:cd00301   75 NELYvLSTDYDnYAIVyscknlDGGHTVVAWLLSR 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 ...
 32-153 4.69e-08

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: 49.80  E-value: 4.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983  32 TNFDANRYLGKWYEIARLENWFERGLEQVSATYEKRNDGGIRVLNRGYDPTKNKWSESEGKAYFTGDTKtaaLKVSFFGP 111
Cdd:cd19440    9 TGFDYTKYLGVWYEAFRTPNAHEEQYKCWIDRFSLDPEGPIAVTSVAYDSRGKNRVTLTGTVPVSTGNK---FDIDYGDD 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 554702983 112 --FYGGYNVIKLDdeYK-YALVSG-----PNREYLWILARTQTIPDNVKA 153
Cdd:cd19440   86 eaWSSQYWVLGTD--YEtYAILAGcpaqdSNKHLIWVQSRDTSFDNATKK 133
lipocalin_crustacyanin cd19436
crustacyanin Type I CRTC and Type II CRTA subunits; Alpha crustacyanin bound with the ...
 33-122 2.42e-06

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: 45.15  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983  33 NFDANRYLGKWYEIARLENWFERGLEQVSATYE-KRNDGGIRVLNRGYDPtKNKWSESEGKAYFTGDTKTAALKVSFFGP 111
Cdd:cd19436   18 NFDLRRYAGRWYQTHLINNPYQPVTRCVHSNYSySGSDYGFKVTSAGFNP-DNNYLKRNGKVYPTKEFPAAHMLIDYPSV 96

                         90
                 ....*....|.
gi 554702983 112 FYGGYNVIKLD 122
Cdd:cd19436   97 FAAPYEVIETD 107
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
 40-165 1.29e-03

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: 37.42  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983   40 LGKWYEIArLEN--WFERGLEQVS---ATYEKRNDGGIRVLNrgYDPTKNKWSESEGKAYFTGDTKTaaLKVSFfgPFYG 114
Cdd:pfam00061   1 SGKWYLIA-SANfnELEEEMKALGvgfATIKVLENGNLPVTE--ITKEGGKCKTVSVTFKKTEEPGK--LGVEF--DEYA 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 554702983  115 GYNVIK-LDDEYK-YALV------SGPNREYLWILARTQTIPDNVKADYVRTAQKLGFN 165
Cdd:pfam00061  74 GGRKVKvLTTDYDnYLIFyqkgdkDGKTTIVRELYGRDPELSPELLEKFKKFLKELGID 132
lipocalin_L-PGDS cd19419
lipocalin-type prostaglandin D synthase; Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5. ...
 28-165 1.43e-03

lipocalin-type prostaglandin D synthase; Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5.3.99.2) is a secreted enzyme and the second most abundant protein in human cerebrospinal fluid. L-PGDS acts as both, an enzyme and as a lipid transporter, converting prostaglandin H2 to prostaglandin D2 and serving as a carrier for hydrophobic ligands including retinoids, hemoglobin metabolites, thyroid hormones, gangliosides, and fatty acids. L-PGDS belongs to the lipocalin/cytosolic fatty-acid binding protein family which has 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: 381194  Cd Length: 158  Bit Score: 37.33  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554702983  28 VQPitNFDANRYLGKWYEI--ARLENWFERGLEQVS---ATYEKRNDGGIRVLNrgydpTKNKWSESEGKAYFTGDTKTA 102
Cdd:cd19419    1 PQP--DFDLDKFAGRWYSVglASNSNWFVEKKAKLKmctTVVAPTTDGNLNLTM-----TFLKKNGCETRTYLYEKTEQP 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 554702983 103 AlKVSFFGPFYGGYNVIKL-DDEY-KYALV----SGPNREYLW--ILARTQTIPDNVKADYVRTAQKLGFN 165
Cdd:cd19419   74 G-RFTYKSPRWGSDHDVRVvETNYdEYALVhtikTKGNEEFTMvtLYSRTQTLRPELKEKFRQFAKAQGFT 143
 
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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