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Conserved domains on  [gi|88196796|ref|NP_001034633|]
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major urinary protein 3 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
lipocalin_FABP super family cl10502
lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low ...
27-184 2.81e-87

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.


The actual alignment was detected with superfamily member cd19428:

Pssm-ID: 415860  Cd Length: 158  Bit Score: 253.13  E-value: 2.81e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  27 SMERNFNVEQISGYWFSIAEASDEREKIEEHGSMRAFVENITVLENSLVFKFHLIVNEECTEMTAIGEQTEKAGIYYMNY 106
Cdd:cd19428   1 SVTRNFDVSKINGEWYSILLASDKREKIEENGSMRVFVEHIHVLENSLAFKFHTKVNGECTELNLVADKTEKAGEYSVTY 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88196796 107 DGFNTFSILKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENIIDLTNVNRCLEARE 184
Cdd:cd19428  81 DGYNTFTILETDYDNYIMFHLINFKNGETFQLMELYGREPDVSSDIKERFVKLCEEHGIIKENIIDLTKTDRCLQARG 158
 
Name Accession Description Interval E-value
lipocalin_MUP-like cd19428
major urinary proteins (MUPs) and similar proteins; Mouse urine contains major urinary ...
27-184 2.81e-87

major urinary proteins (MUPs) and similar proteins; Mouse urine contains major urinary proteins (MUPs) which bind low molecular weight hydrophobic organic compounds such as urinary volatile pheromones such as the male-specific 2-sec-butyl-4,5-dihydrothiazole (SB2HT) which hastens puberty in female mice. The association between MUPs and these volatiles slows the release of the volatiles into the air from urine marks. MUPs may also act as pheromones themselves. MUPs, expressed in the nasal and vomeronasal mucosa, may be important for delivering urinary volatiles to receptors in the vomeronasal organ. This group includes MUPs encoded by central genes in the MUP cluster, as well as those encoded by peripheral genes such as Darcin/Mup20 which binds most of the male pheromone SB2HT in urine and was the first MUP shown to have male pheromonal activity in its own right. This group includes rat MUPs (also called alpha-2U globulins) and other lipocalins such as major horse allergen Equ c 1 and boar salivary lipocalin, a pheromone-binding protein specifically expressed in the submaxillary glands of the boar. It 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: 381203  Cd Length: 158  Bit Score: 253.13  E-value: 2.81e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  27 SMERNFNVEQISGYWFSIAEASDEREKIEEHGSMRAFVENITVLENSLVFKFHLIVNEECTEMTAIGEQTEKAGIYYMNY 106
Cdd:cd19428   1 SVTRNFDVSKINGEWYSILLASDKREKIEENGSMRVFVEHIHVLENSLAFKFHTKVNGECTELNLVADKTEKAGEYSVTY 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88196796 107 DGFNTFSILKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENIIDLTNVNRCLEARE 184
Cdd:cd19428  81 DGYNTFTILETDYDNYIMFHLINFKNGETFQLMELYGREPDVSSDIKERFVKLCEEHGIIKENIIDLTKTDRCLQARG 158
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
38-174 6.64e-35

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: 119.47  E-value: 6.64e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796    38 SGYWFSIAEASDeREKIEEHGSMRAFVENITVLEN-SLVFKFHLIVNEECTEMTAIGEQTEKAGIYYMNYD---GFNTFS 113
Cdd:pfam00061   1 SGKWYLIASANF-NELEEEMKALGVGFATIKVLENgNLPVTEITKEGGKCKTVSVTFKKTEEPGKLGVEFDeyaGGRKVK 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196796   114 ILKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENIIDLT 174
Cdd:pfam00061  80 VLTTDYDNYLIFYQKGDKDGKTTIVRELYGRDPELSPELLEKFKKFLKELGIDEENIVRLY 140
 
Name Accession Description Interval E-value
lipocalin_MUP-like cd19428
major urinary proteins (MUPs) and similar proteins; Mouse urine contains major urinary ...
27-184 2.81e-87

major urinary proteins (MUPs) and similar proteins; Mouse urine contains major urinary proteins (MUPs) which bind low molecular weight hydrophobic organic compounds such as urinary volatile pheromones such as the male-specific 2-sec-butyl-4,5-dihydrothiazole (SB2HT) which hastens puberty in female mice. The association between MUPs and these volatiles slows the release of the volatiles into the air from urine marks. MUPs may also act as pheromones themselves. MUPs, expressed in the nasal and vomeronasal mucosa, may be important for delivering urinary volatiles to receptors in the vomeronasal organ. This group includes MUPs encoded by central genes in the MUP cluster, as well as those encoded by peripheral genes such as Darcin/Mup20 which binds most of the male pheromone SB2HT in urine and was the first MUP shown to have male pheromonal activity in its own right. This group includes rat MUPs (also called alpha-2U globulins) and other lipocalins such as major horse allergen Equ c 1 and boar salivary lipocalin, a pheromone-binding protein specifically expressed in the submaxillary glands of the boar. It 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: 381203  Cd Length: 158  Bit Score: 253.13  E-value: 2.81e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  27 SMERNFNVEQISGYWFSIAEASDEREKIEEHGSMRAFVENITVLENSLVFKFHLIVNEECTEMTAIGEQTEKAGIYYMNY 106
Cdd:cd19428   1 SVTRNFDVSKINGEWYSILLASDKREKIEENGSMRVFVEHIHVLENSLAFKFHTKVNGECTELNLVADKTEKAGEYSVTY 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88196796 107 DGFNTFSILKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENIIDLTNVNRCLEARE 184
Cdd:cd19428  81 DGYNTFTILETDYDNYIMFHLINFKNGETFQLMELYGREPDVSSDIKERFVKLCEEHGIIKENIIDLTKTDRCLQARG 158
lipocalin_9 cd19429
lipocalin 9; Lipocalin 9 (LCN9) is specifically expressed in the epididymis. It belongs to the ...
28-179 9.34e-38

lipocalin 9; Lipocalin 9 (LCN9) is specifically expressed in the epididymis. It belongs to the lipocalin/cytosolic fatty-acid binding protein family. Lipocalins are typically small extracellular proteins that bind small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids and form covalent or non-covalent complexes with soluble macromolecules as well as membrane bound-receptors. They are involved in many important functions, like ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior.


Pssm-ID: 381204  Cd Length: 156  Bit Score: 127.26  E-value: 9.34e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  28 MERNFNVEQISGYWFSIAEASDEREKIEEHGSMRAFVENITVLEN-SLVFKFHLIVNEECTEMTAIGEQTEKAGIYYMNY 106
Cdd:cd19429   4 VRRDYNMARISGVWYSISMASDNMTRIEENGDLRLFIRNIELLNNgSLQFDFHFMLQGECVAVTVVCEKTKKNGEFSIAY 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88196796 107 DGFNTFSILKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENIIDLTNVNRC 179
Cdd:cd19429  84 EGENKVLLLETDYSMYIIFYLQNIRNGTETQVLALYGRSILLDKTHQRRFENICNKYGLGPRNTIDMAKKDFC 156
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
38-174 6.64e-35

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: 119.47  E-value: 6.64e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796    38 SGYWFSIAEASDeREKIEEHGSMRAFVENITVLEN-SLVFKFHLIVNEECTEMTAIGEQTEKAGIYYMNYD---GFNTFS 113
Cdd:pfam00061   1 SGKWYLIASANF-NELEEEMKALGVGFATIKVLENgNLPVTEITKEGGKCKTVSVTFKKTEEPGKLGVEFDeyaGGRKVK 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196796   114 ILKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENIIDLT 174
Cdd:pfam00061  80 VLTTDYDNYLIFYQKGDKDGKTTIVRELYGRDPELSPELLEKFKKFLKELGIDEENIVRLY 140
lipocalin_OBP-like cd19427
Lipocalin odorant-binding protein and similar proteins; Odorant-binding proteins (OBPs) ...
36-173 5.79e-22

Lipocalin odorant-binding protein and similar proteins; Odorant-binding proteins (OBPs) transport small hydrophobic molecules in the nasal mucosa of vertebrates. This subfamily includes mouse odorant-binding protein 1a (Obp1a), Obp1b, and probasin. Mouse Obp1a and Obp1b, which are expressed in the nasal mucosa, bind the chemical odorant 2-isobutyl-3-methoxypyrazine, and may form a OBPO1a/Opb1B heterodimer. Mouse probasin may play a role in the biology of the prostate gland. This group also includes hamster female-specific lacrimal gland protein (FLP) and aphrodisin. FLP may bind tear lipids or lipid-like pheromones found in hamster tears; aphrodisin is found in hamster vaginal discharge, carries pheromones, and stimulates copulatory behavior in males. This group also includes dog allergen Ca f4 which is expressed by tongue epithelial tissue and found in saliva and dander. Bovine OBP is believed to act as a homodimer, having the C-terminal alpha-helix of each monomer stacking against the beta-barrel of the other monomer; this is possible due to its lack of cysteines and therefore lack of disulfide bonds. 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: 381202  Cd Length: 147  Bit Score: 86.55  E-value: 5.79e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  36 QISGYWFSIAEASDEREKIEEHGSMRAFVENITVLE--NSLVFKFHLIVNEECTEMTAIGEQTEkAGIYYMNYDGFNTFS 113
Cdd:cd19427   3 ELSGPWRTIYIAADNVEKIEEGGPLRTYFREIECDDecQKIKITFYVKKNGQCQETTVVGYKQE-DGTYVADYEGQNYFK 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196796 114 ILKTDyDNYIMIHLINK-KDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENIIDL 173
Cdd:cd19427  82 VVSVS-EDALVFYNVNVdRAGRKTKLTLLLGKGNSLTPEQKEKFKKLAEEKGIPEENIRNL 141
lipocalin_L-PGDS cd19419
lipocalin-type prostaglandin D synthase; Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5. ...
31-179 5.95e-20

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: 81.63  E-value: 5.95e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  31 NFNVEQISGYWFSIAEASDEREKIEEHGSMRAFVENITVLEN---SLVFKFhlIVNEECTEMTAIGEQTEKAG--IYYMN 105
Cdd:cd19419   4 DFDLDKFAGRWYSVGLASNSNWFVEKKAKLKMCTTVVAPTTDgnlNLTMTF--LKKNGCETRTYLYEKTEQPGrfTYKSP 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88196796 106 YDGFNT-FSILKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENIIDLTNVNRC 179
Cdd:cd19419  82 RWGSDHdVRVVETNYDEYALVHTIKTKGNEEFTMVTLYSRTQTLRPELKEKFRQFAKAQGFTEENIVTLPQTDEC 156
lipocalin_FABP cd00301
lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low ...
36-144 1.04e-17

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: 74.50  E-value: 1.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  36 QISGYWFSIAEASDEREKieehGSMRAFVENITVL-ENSLVFKFHLIVNEECTEMTAIGEQTEKAGIYYMNYDGF---NT 111
Cdd:cd00301   1 KFSGKWYEVASASNAPEE----DEGKCTTAEYTLEgNGNLKVTNSFVRDGVCKSITGTLKKTDGPGKFTVTYPGYtgkNE 76
                        90       100       110
                ....*....|....*....|....*....|...
gi 88196796 112 FSILKTDYDNYIMIHLINKKDGKTFQLMELYGR 144
Cdd:cd00301  77 LYVLSTDYDNYAIVYSCKNLDGGHTVVAWLLSR 109
lipocalin_trichosorin-like cd19430
trichosurin and similar proteins; Trichosurin is a protein from the milk whey of the common ...
37-179 7.93e-17

trichosurin and similar proteins; Trichosurin is a protein from the milk whey of the common brushtail possum, Trichosurus Vulpecula, and shows a preference for binding small phenolic ligands. 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: 381205  Cd Length: 153  Bit Score: 73.56  E-value: 7.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  37 ISGYWFSIAEASDEREKIEEHGSMRAFVENITVLENSLVFKFHLIVNEECTEMTAIGEQTEKAGIYYMNYDGFNTFSILK 116
Cdd:cd19430  11 LSRHWHTVVLASSDRSLIEEEGPFRNFIQNITVESGNLNGFFLTRKNGQCIPLYLTAFKTEEARQFKLNYYGTNDVYYES 90
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88196796 117 TDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENIIDLTNVNRC 179
Cdd:cd19430  91 SKPNEYAKFIFYNYHDGKVNVVANLFGRTPNLSNEIKKRFEEDFMNRGFRRENILDISEVDHC 153
lipocalin_Can_f_2 cd19431
Minor allergen Can f 2; The minor dog lipocalin allergen Can f 2 is an important cause of ...
24-184 2.47e-14

Minor allergen Can f 2; The minor dog lipocalin allergen Can f 2 is an important cause of allergic sensitization in humans worldwide. It is one of two major allergens present in dog dander extracts, and is produced by tongue and the parotid gland (a major salivary gland). Can f 2 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: 381206  Cd Length: 162  Bit Score: 67.03  E-value: 2.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  24 ESSSMERNFNVEQISGYWFSIAEASDEREKIEEHGSMRAFVENITVLENSLVFKFHLIVNEECTEMTAIGEQTEKAGIYY 103
Cdd:cd19431   2 EGNHEEPQGGLEELSGRWHSVALASNKSDLIKPWGHFRVFIHSMSAKDGNLHGDILIPQDGQCEKVSLTAFKTATSNKFD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796 104 MNYDGFNTFSILKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENIIDLTNVNRCLEAR 183
Cdd:cd19431  82 LEYWGHNDLYLAEVDPKSYLILYMINQYNDDTSLVAHLMVRDLSRQQDFLPAFESVCEDIGLHKDQIVVLSDDDRCQGSR 161

                .
gi 88196796 184 E 184
Cdd:cd19431 162 D 162
lipocalin_Ex-FABP-like cd19439
extracellular fatty acid-binding protein; Ex-FABP (also known as siderocalin, lipocalin Q83 or ...
36-162 3.75e-13

extracellular fatty acid-binding protein; Ex-FABP (also known as siderocalin, lipocalin Q83 or protein Ch21) displays a dual ligand binding mode as it can bind siderophore and fatty acids simultaneously. ExFABP has a cavity which extends through the protein and has two separate ligand specificities, one for bacterial siderophores at one end, and other specifically binding co-purified lysophosphatidic acid (LPA), a potent cell signaling molecule, at the other end. As well as acting as an LPA "sensor", Ex-FABP is bacteriostatic, and tightly binds the 2,3-catechol-type ferric siderophores enterobactin, bacillibactin, and parabactin, associated with enteric bacteria and Gram-positive bacilli. 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: 381214  Cd Length: 142  Bit Score: 63.45  E-value: 3.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  36 QISGYWFSIAEASDEREKIEEHGSMRAFVENITVL-ENSLVFKFHLIVNEECTEMTAIGEQTEKAGIYYMNYDGFNTFSI 114
Cdd:cd19439   3 ELAGKWYLVALASNTDFFLREKGKMKMMMARISFLgEDELLVSYAFPSPGGCRKWETTFKKTSDDGEVYYSEEARKTVEV 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 88196796 115 LKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEE 162
Cdd:cd19439  83 LDTDYKSYAVIYATRVKDGRTLHMMRLYSRSQEVSPEAEAIFRKLAEE 130
lipocalin_15-like cd19422
lipocalin 15 and similar proteins, such as chicken CALbeta; This subfamily includes ...
36-159 1.35e-11

lipocalin 15 and similar proteins, such as chicken CALbeta; This subfamily includes uncharacterized human lipocalin 15, and chicken chondrogenesis-associated lipocalin (CAL) beta which is associated with chondrogenesis and inflammation. It 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: 381197  Cd Length: 143  Bit Score: 59.10  E-value: 1.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  36 QISGYWFSIAEASDEREKIEEHGSMRAFVENITVLENS-LVFKFHLIVNEECTEMTAIGEQTEKAGIYYMNYDGFNTFSI 114
Cdd:cd19422   1 KFAGLWHVMAMASDCPVFLGMKDHMTSSTTAIRPTPEGdLTMHTEFPLPDGCKQIEAEFQKSGQAGHFRVPELGKRDLRV 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 88196796 115 LKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKL 159
Cdd:cd19422  81 MDTDYSSYAILYIYKELEGESSTMVQLYTRNQDVSPQLLQKFKEL 125
lipocalin_1_3_4_13-like cd19414
lipocalin-1, -3, -4, -13 and similar proteins; Lipocalin-1 (LCN1, also known as tear lipocalin, ...
35-171 3.23e-10

lipocalin-1, -3, -4, -13 and similar proteins; Lipocalin-1 (LCN1, also known as tear lipocalin, von ebner's gland protein, or tear specific prealbumin), the main lipid carrier in human tears, is critical to functions involving lipids in protection of the ocular surface. Its large ligand pocket accommodates a range of ligands including alkyl alcohols, glycolipids, phospholipids, cholesterol, steroids, and siderophores. Lipocalin-3 (LCN3, also known as vomeronasal secretory protein 1) and lipocalin-4 (LCN4, also known as vomeronasal secretory protein 2) are involved in transport of lipophilic molecules, and are possibly pheromone-carriers. Lipocalin-13 (LCN13, also known as odorant binding protein 2A) may bind and transport small hydrophobic volatile molecules with a higher affinity for aldehydes and large fatty acids. Another member of this family is late lactation protein B (LLPB), a milk protein produced during the late phase of lactation, which may be involved in transporting a small ligand released during the hydrolysis of milk fat. 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: 381189  Cd Length: 147  Bit Score: 55.80  E-value: 3.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  35 EQISGYWFSIAEASDeREKIEEHGSMRAFVENITVLEN-SLVFKFHLIVNEECTEMTAIGEQTEKAGIYYMnYDGFNTFS 113
Cdd:cd19414   3 EDVSGTWYLKAMVVD-KEFPEKRRPRKVSPVTVTALEGgNLEAKFTFMINGRCEEVKIVLEKTDEPGKYTA-FSGKKVVY 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 88196796 114 ILKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENII 171
Cdd:cd19414  81 IQETSVKDHYILYCEGELHGMTFRMAKLVGRDPEENPEALEEFKKFVQRKGLNEENIV 138
lipocalin_A1M-like cd19418
lipocalin domain of alpha1-microglobulin and similar proteins; Alpha(1)-microglobulin (A1M, ...
29-179 4.10e-09

lipocalin domain of alpha1-microglobulin and similar proteins; Alpha(1)-microglobulin (A1M, also known as protein AMBP, alpha-1 microglycoprotein, and protein HC), has immunosuppressive properties, such as inhibition of antigen induced lymphocyte cell-proliferation, cytokine secretion, and oxidative burst of neutrophils. A1M may participate in the reducing and scavenging of biological pro-oxidants such as heme and heme-proteins. It binds heme strongly, and a C-terminally processed form of the protein degrades the heme. It can reduce cytochrome C, nitroblue tetrazolium, methemoglobin and free iron, using NADH, NADPH or ascorbate as cofactor. Intravenous administration of recombinant A1M in animal models eliminates or significantly reduces the manifestations of preeclampsia. A1M is a useful biomarker in clinical diagnostics for monitoring pre-eclampsia, hepatitis E, renal tubular dysfunction, and renal toxicity. A1M 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: 381193  Cd Length: 163  Bit Score: 52.84  E-value: 4.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  29 ERNFNVEQISGYWFSIAEASD--EREKIEEHGSMRAFVENITVLENSLVFKFHLIVNEECTEMTAIGEQTEKAGIYYMNY 106
Cdd:cd19418   5 QENFNLSRIYGKWYDLAVGSTcpWLKRIKDKMAIGTLVLQEGATGAELSMTRTRLRRGTCEEISGEYEKTDTPGKFLYHK 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 88196796 107 DGFNT---FSILKTDYDNY-IMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENIIDLTNVNRC 179
Cdd:cd19418  85 SKWNAtvdAYVVHTNYDEYaIFLMKKFKRHGEPTTTLKLYGRTPQLRPTLLQDFRTLALEQGIPEDSIIIKADKGEC 161
lipocalin_beta-LG-like cd19416
beta-lactoglobulin and similar proteins; Beta-Lactoglobulin (beta-LG) is the major whey ...
34-158 7.31e-09

beta-lactoglobulin and similar proteins; Beta-Lactoglobulin (beta-LG) is the major whey protein of ruminant species and present in the milk of many other species, with a notable exception of human. It is the major allergen of bovine milk. Beta-LG has been shown to bind hydrophobic ligands such as curcumin, vitamin E or fatty acids, or hydrophilic such as vitamin B9. This group also includes human glycodelin (also known as placental protein 14, pregnancy-associated endometrial alpha-2 globulin, and progestagen-associated endometrial protein) which is involved in crucial biological processes such as reproduction and immune reaction. Four glycoforms of glycodelin have been identified in reproductive tissue that differ in glycosylation and biological activity. 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: 381191  Cd Length: 160  Bit Score: 52.15  E-value: 7.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  34 VEQISGYWFSIAEA-SDEREKIEEHGSMRAFVENITVL-ENSLVFKFHLIVNEECTEMTAIGEQTEKAGIYYMNYDGFNT 111
Cdd:cd19416  10 VQKVAGTWYSLAMAaSDISLLDAQSAPLRVYIEELKPTpEGNLEIVLQKWENGRCAEKKLLAEKTKIPAVFKINALNENK 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 88196796 112 FSILKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAK 158
Cdd:cd19416  90 VLVLDTDYDSYLLFCMENSAEPEQSLACQCLVRTLEVDNEAMEKFDK 136
lipocalin_C8gamma cd19417
complement protein C8 gamma; Human complement protein C8 gamma, together with C8alpha and ...
31-165 2.31e-07

complement protein C8 gamma; Human complement protein C8 gamma, together with C8alpha and C8beta, form one of five components of the cytolytic membrane attack complex (MAC), a pore-like structure that assembles on bacterial membranes. C8alpha and C8gamma form a disulfide-linked heterodimer that is noncovalently associated with C8beta. MAC plays an important role in the defense against gram-negative bacteria and other pathogenic organisms. C8gamma 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: 381192  Cd Length: 162  Bit Score: 48.21  E-value: 2.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  31 NFNVEQISGYWFSIAEASDEREKIEEHGSMRAFVENITVLENSL-VFKFHLIvNEECTEMTAIGEQTEKAGIYYMNYDG- 108
Cdd:cd19417   5 NFDIQQFSGKWYLVAVASACRYLQESGHKVEATVLTVAPPKTTVaVSTFRKL-NGICWEIKQEYGKTGTLGRFLLKARRp 83
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 88196796 109 -FNT-FSILKTDYDNYIMIHLinKKDGKTfqLMELYGREPDLSLDIKEKFAKLCEEHGI 165
Cdd:cd19417  84 rGNTdIVVGETDYSSYAILYY--QRAGKL--TMKLYGRSTELSENILDKFEQRAQKAHL 138
lipocalin_RBP_like cd00743
retinol-binding protein 4 and similar proteins; Retinol-Binding Protein 4 (RBP4) is a plasma ...
24-122 2.62e-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: 42.43  E-value: 2.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  24 ESSSMERNFNVEQISGYWFSIAEASDE----------REKIEEHGSMRAFVE-NITVLENSLVfkfhlivneeCTEMTAI 92
Cdd:cd00743   4 SSFRVKENFDKARYAGTWYAMAKKDPEglflqdnivaEFSVDENGTMTATAKgRVRLLNNWDV----------CADMVGT 73
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 88196796  93 GEQTEKAGIYYMNY--------DGFNTFSILKTDYDNY 122
Cdd:cd00743  74 FTDTEDPAKFKMKYwgvasylqKGNDDHWVIDTDYDTY 111
lipocalin_5_8-like cd19421
lipocalin similar to human epididymal-specific lipocalin-8, mouse lipocalin-5 and -8, and ...
32-144 8.03e-05

lipocalin similar to human epididymal-specific lipocalin-8, mouse lipocalin-5 and -8, and similar proteins; Lipocalin 5 (LCN5; also known as epididymal retinoic acid binding protein Erabp, mouse epididymal protein 10, MEP10, and E-RABP) and Lipocalin 8 (LCN8; also known as mouse epididymal protein 17, MEP17) are homologous proteins belonging to the epididymis-specific lipocalins; they may play a role in male fertility, and may act as retinoid carrier proteins within the epididymis. In mice, genes encoding the two proteins are contiguous; in humans, there is one gene LCN8 (which has been previously called LCN5). 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: 381196  Cd Length: 150  Bit Score: 41.06  E-value: 8.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196796  32 FNVEQISGYWFSIAEASDEREKIEEHGSMRAFVenITVLENSLVFKFHLIVNEECTEMTAIGeqTEKAGIYYMNYDGFNT 111
Cdd:cd19421   5 LDISKILGFWYEVAVASDQGLVLHAEERVEGLF--LTLSGNNLTVKTTYNSSGSCVLEKVTG--SEGDGPGKFAFPGKRE 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 88196796 112 FSILKTDYDNYIMIHLINKKDGKTFQLMELYGR 144
Cdd:cd19421  81 IHVLDTDYETYAILDITLLWAGRNFRVLKYFTR 113
lipocalin_2-like cd19457
lipocalin 2 and similar proteins; Lipocalin-2 (LCN2, also known as siderocalin, uterocalin, ...
104-171 1.88e-04

lipocalin 2 and similar proteins; Lipocalin-2 (LCN2, also known as siderocalin, uterocalin, oncogene 24p3, and neutrophil gelatinase-associated lipocalin) is expressed in renal, endothelial, liver, smooth muscle cells, cardiomyocytes, in various populations of immune cells and dendritic cells. Roles ascribed to LCN2, include chemotactic and bacteriostatic effects, and iron trafficking. LCN2 can also act as a growth factor. It plays an key role in the pathophysiology of renal and cardiovascular diseases, and is involved in various deleterious processes, such as inflammation and fibrosis. It is used as a renal injury biomarker. This subgroup 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: 381232  Cd Length: 173  Bit Score: 40.05  E-value: 1.88e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88196796 104 MNYdgfnTFSILKTDYDNYIMIHLINKKDGKTFQLMELYGREPDLSLDIKEKFAKLCEEHGIIRENII 171
Cdd:cd19457 101 QSY----TVRVVATDYNQFAMVFFKKTSENRVYFEITLYGRTKELSPELKERFIKFSKSLGLPDDNII 164
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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