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Conserved domains on  [gi|34328049|ref|NP_032517|]
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neutrophil gelatinase-associated lipocalin precursor [Mus musculus]

Protein Classification

lipocalin/fatty-acid binding family protein (domain architecture ID 14443817)

lipocalin/fatty-acid binding family protein such as lipocalins, which are transporters for small hydrophobic molecules, including lipids, steroid hormones, bilins, and retinoids

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
lipocalin_2-like cd19457
lipocalin 2 and similar proteins; Lipocalin-2 (LCN2, also known as siderocalin, uterocalin, ...
24-198 8.78e-118

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: 331.26  E-value: 8.78e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  24 TQNLIPAPSLLTVPLQPDFRSDQFRGRWYVVGLAGNAVQKKTEGSFTMYSTIYELQENNSYNVTSILVRDQdqGCRYWIR 103
Cdd:cd19457   1 TPDLIPAPPLSKVPLQPDFQDDQFQGKWYVIGVAGNTIQNESLSQLTMYSTIYELKDDHSYNVTSILFRDK--GCEHWIR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049 104 TFVPSSRAGQFTLGNMHRYPQVQSYNVQVATTDYNQFAMVFFRKTSENKQYFKITLYGRTKELSPELKERFTRFAKSLGL 183
Cdd:cd19457  79 TFVPSVQPGQFTLGNITSYPGLQSYTVRVVATDYNQFAMVFFKKTSENRVYFEITLYGRTKELSPELKERFIKFSKSLGL 158
                       170
                ....*....|....*
gi 34328049 184 KDDNIIFSVPTDQCI 198
Cdd:cd19457 159 PDDNIIFTVPIGQCI 173
 
Name Accession Description Interval E-value
lipocalin_2-like cd19457
lipocalin 2 and similar proteins; Lipocalin-2 (LCN2, also known as siderocalin, uterocalin, ...
24-198 8.78e-118

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: 331.26  E-value: 8.78e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  24 TQNLIPAPSLLTVPLQPDFRSDQFRGRWYVVGLAGNAVQKKTEGSFTMYSTIYELQENNSYNVTSILVRDQdqGCRYWIR 103
Cdd:cd19457   1 TPDLIPAPPLSKVPLQPDFQDDQFQGKWYVIGVAGNTIQNESLSQLTMYSTIYELKDDHSYNVTSILFRDK--GCEHWIR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049 104 TFVPSSRAGQFTLGNMHRYPQVQSYNVQVATTDYNQFAMVFFRKTSENKQYFKITLYGRTKELSPELKERFTRFAKSLGL 183
Cdd:cd19457  79 TFVPSVQPGQFTLGNITSYPGLQSYTVRVVATDYNQFAMVFFKKTSENRVYFEITLYGRTKELSPELKERFIKFSKSLGL 158
                       170
                ....*....|....*
gi 34328049 184 KDDNIIFSVPTDQCI 198
Cdd:cd19457 159 PDDNIIFTVPIGQCI 173
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
49-195 4.48e-30

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: 107.91  E-value: 4.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049    49 GRWYVVGLAGNAVQKKTEGSFTMYSTIYELQENNSYNVTSILVRDQDqgCRYWIRTFVPSSRAGQFTlgnMHRYPQVQSY 128
Cdd:pfam00061   2 GKWYLIASANFNELEEEMKALGVGFATIKVLENGNLPVTEITKEGGK--CKTVSVTFKKTEEPGKLG---VEFDEYAGGR 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34328049   129 NVQVATTDYNQFAMVFFRKTSENKQYFKITLYGRTKELSPELKERFTRFAKSLGLKDDNIIFSVPTD 195
Cdd:pfam00061  77 KVKVLTTDYDNYLIFYQKGDKDGKTTIVRELYGRDPELSPELLEKFKKFLKELGIDEENIVRLYQKD 143
 
Name Accession Description Interval E-value
lipocalin_2-like cd19457
lipocalin 2 and similar proteins; Lipocalin-2 (LCN2, also known as siderocalin, uterocalin, ...
24-198 8.78e-118

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: 331.26  E-value: 8.78e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  24 TQNLIPAPSLLTVPLQPDFRSDQFRGRWYVVGLAGNAVQKKTEGSFTMYSTIYELQENNSYNVTSILVRDQdqGCRYWIR 103
Cdd:cd19457   1 TPDLIPAPPLSKVPLQPDFQDDQFQGKWYVIGVAGNTIQNESLSQLTMYSTIYELKDDHSYNVTSILFRDK--GCEHWIR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049 104 TFVPSSRAGQFTLGNMHRYPQVQSYNVQVATTDYNQFAMVFFRKTSENKQYFKITLYGRTKELSPELKERFTRFAKSLGL 183
Cdd:cd19457  79 TFVPSVQPGQFTLGNITSYPGLQSYTVRVVATDYNQFAMVFFKKTSENRVYFEITLYGRTKELSPELKERFIKFSKSLGL 158
                       170
                ....*....|....*
gi 34328049 184 KDDNIIFSVPTDQCI 198
Cdd:cd19457 159 PDDNIIFTVPIGQCI 173
lipocalin_2_12-like cd19432
lipocalin 2 and 12 and similar proteins; Lipocalin-2 (LCN2, also known as siderocalin, ...
42-197 1.51e-66

lipocalin 2 and 12 and similar proteins; Lipocalin-2 (LCN2, also known as siderocalin, uterocalin, 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 a 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. Lipocalin 12 (LCN12) is an epididymis-specific protein which binds all-trans retinoic acid. It may act as a retinoid carrier protein within the epididymis and play a role in male reproduction. 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: 381207  Cd Length: 154  Bit Score: 200.99  E-value: 1.51e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  42 FRSDQFRGRWYVVGLAGNAVQKKTEGSFTMYSTIYELQENNSYNVTSILVRDQDqgCRYWIRTFVPSSRAGQFTLGNMHR 121
Cdd:cd19432   1 FQDNQFQGKWYVVGLAGNAILREDKDPQKMYATIYELKEDKSYNVTSVLFRKKK--CDYWIRTFVPGNQPGEFTLGNIKS 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34328049 122 YPQVQSYNVQVATTDYNQFAMVFFRKTSENKQYFKITLYGRTKELSPELKERFTRFAKSLGLKDDNIIFSVPTDQC 197
Cdd:cd19432  79 YPGLTSYLVRVVSTNYNQHAMVFFKKVSQNREYFKITLYGRTKELTSELKENFIRFSKSLGLPENHIVFPVPIDQC 154
lipocalin_L-PGDS cd19419
lipocalin-type prostaglandin D synthase; Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5. ...
38-199 6.16e-38

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: 128.24  E-value: 6.16e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  38 LQPDFRSDQFRGRWYVVGLAGNA---VQKKTEgsFTMYSTIYELQENNSYNVTSILVRDQdqGCryWIRTFV--PSSRAG 112
Cdd:cd19419   1 PQPDFDLDKFAGRWYSVGLASNSnwfVEKKAK--LKMCTTVVAPTTDGNLNLTMTFLKKN--GC--ETRTYLyeKTEQPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049 113 QFTL-----GNMHrypqvqsyNVQVATTDYNQFAMVFFRKTSENKQYFKITLYGRTKELSPELKERFTRFAKSLGLKDDN 187
Cdd:cd19419  75 RFTYksprwGSDH--------DVRVVETNYDEYALVHTIKTKGNEEFTMVTLYSRTQTLRPELKEKFRQFAKAQGFTEEN 146
                       170
                ....*....|..
gi 34328049 188 IIFSVPTDQCID 199
Cdd:cd19419 147 IVTLPQTDECPP 158
lipocalin_12 cd19458
Lipocalin 12; Lipocalin 12 (LCN12) is an epididymis-specific protein which binds all-trans ...
37-199 2.16e-32

Lipocalin 12; Lipocalin 12 (LCN12) is an epididymis-specific protein which binds all-trans retinoic acid. It may act as a retinoid carrier protein within the epididymis and play a role in male reproduction. 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: 381233  Cd Length: 165  Bit Score: 114.65  E-value: 2.16e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  37 PLQPDFRSDQFRGRWYVVGLAGNAVQKKTEGSFTMYSTIYELQENNSYNVTSILVRDQDqgCRYWIRTFVPSSRAGQFTL 116
Cdd:cd19458   1 PQMTSFQSNQFQGEWFVLGLADNTFRREHRALLNAFTTLFELSDDSRFQVTNSMTRGKH--CDTWSYTLIPAAKPGQFTR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049 117 GNMHRYPQVQSYNVQVATTDYNQFAMVFFRKTSENKQYFKITLYGRTKELSPELKERFTRFAKSLGLKDDNIIFSVPTDQ 196
Cdd:cd19458  79 DNRGSGPGADRENIQVIETDYTQFALVLSLRQTSRQNITRVSLLGRSWLLPHKTIDQFICLTRTQNLTKDNILFPDLTDW 158

                ...
gi 34328049 197 CID 199
Cdd:cd19458 159 LPD 161
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
49-195 4.48e-30

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: 107.91  E-value: 4.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049    49 GRWYVVGLAGNAVQKKTEGSFTMYSTIYELQENNSYNVTSILVRDQDqgCRYWIRTFVPSSRAGQFTlgnMHRYPQVQSY 128
Cdd:pfam00061   2 GKWYLIASANFNELEEEMKALGVGFATIKVLENGNLPVTEITKEGGK--CKTVSVTFKKTEEPGKLG---VEFDEYAGGR 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34328049   129 NVQVATTDYNQFAMVFFRKTSENKQYFKITLYGRTKELSPELKERFTRFAKSLGLKDDNIIFSVPTD 195
Cdd:pfam00061  77 KVKVLTTDYDNYLIFYQKGDKDGKTTIVRELYGRDPELSPELLEKFKKFLKELGIDEENIVRLYQKD 143
lipocalin_FABP cd00301
lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low ...
46-162 2.52e-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: 68.73  E-value: 2.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  46 QFRGRWYVVGLAGNAvqkKTEGSFTMYSTIYELQENNSYNVTSILVRDQdqGCRYWIRTFVPSSRAGQFTlgnMHRYPQV 125
Cdd:cd00301   1 KFSGKWYEVASASNA---PEEDEGKCTTAEYTLEGNGNLKVTNSFVRDG--VCKSITGTLKKTDGPGKFT---VTYPGYT 72
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 34328049 126 QSYNVQVATTDYNQFAMVFFRKTSENKQYFKITLYGR 162
Cdd:cd00301  73 GKNELYVLSTDYDNYAIVYSCKNLDGGHTVVAWLLSR 109
lipocalin_15-like cd19422
lipocalin 15 and similar proteins, such as chicken CALbeta; This subfamily includes ...
46-186 1.08e-13

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: 65.27  E-value: 1.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  46 QFRGRWYVVGLAGN-AVQKKTEGSFTMYSTIYELQENNsyNVTSILVRDQDQGCRYWIRTFVPSSRAGQFTLgnmhryPQ 124
Cdd:cd19422   1 KFAGLWHVMAMASDcPVFLGMKDHMTSSTTAIRPTPEG--DLTMHTEFPLPDGCKQIEAEFQKSGQAGHFRV------PE 72
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34328049 125 VQSYNVQVATTDYNQFAMVFFRKTSENKQYFKITLYGRTKELSPELKERFTRFAKSLGLKDD 186
Cdd:cd19422  73 LGKRDLRVMDTDYSSYAILYIYKELEGESSTMVQLYTRNQDVSPQLLQKFKELYPTLGLTED 134
lipocalin_Ex-FABP-like cd19439
extracellular fatty acid-binding protein; Ex-FABP (also known as siderocalin, lipocalin Q83 or ...
49-188 1.59e-11

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: 59.60  E-value: 1.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  49 GRWYVVGLAGNA--VQKKTEGSFTMYSTIYELQENN---SYNVTSilvrdqDQGCRYWIRTFVPSSRAGQFTlgnmhrYP 123
Cdd:cd19439   6 GKWYLVALASNTdfFLREKGKMKMMMARISFLGEDEllvSYAFPS------PGGCRKWETTFKKTSDDGEVY------YS 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34328049 124 QVQSYNVQVATTDYNQFAMVFFRKTSENKQYFKITLYGRTKELSPELKERFTRFAKSLGLKDDNI 188
Cdd:cd19439  74 EEARKTVEVLDTDYKSYAVIYATRVKDGRTLHMMRLYSRSQEVSPEAEAIFRKLAEERNYTDEMV 138
lipocalin_A1M-like cd19418
lipocalin domain of alpha1-microglobulin and similar proteins; Alpha(1)-microglobulin (A1M, ...
36-198 3.04e-11

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: 59.00  E-value: 3.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  36 VPLQPDFRSDQFRGRWYVVGLAGNAVQ-KKTEGSFTMySTIyELQEN---NSYNVTSILVRdqdQG-CRYWIRTFVPSSR 110
Cdd:cd19418   2 IQTQENFNLSRIYGKWYDLAVGSTCPWlKRIKDKMAI-GTL-VLQEGatgAELSMTRTRLR---RGtCEEISGEYEKTDT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049 111 AGQFTLGNMHRYPQVQSYnvqVATTDYNQFA---MVFFRKTSENKQYFKitLYGRTKELSPELKERFTRFAKSLGLKDDN 187
Cdd:cd19418  77 PGKFLYHKSKWNATVDAY---VVHTNYDEYAiflMKKFKRHGEPTTTLK--LYGRTPQLRPTLLQDFRTLALEQGIPEDS 151
                       170
                ....*....|.
gi 34328049 188 IIFSVPTDQCI 198
Cdd:cd19418 152 IIIKADKGECV 162
lipocalin_MUP-like cd19428
major urinary proteins (MUPs) and similar proteins; Mouse urine contains major urinary ...
41-198 3.26e-11

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: 58.99  E-value: 3.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  41 DFRSDQFRGRWYVVGLAGNAVQKKTE-GSFTMYSTIYELQENNSYNVTSILVrdqDQGCRYWIRTFVPSSRAGQFTLgnm 119
Cdd:cd19428   5 NFDVSKINGEWYSILLASDKREKIEEnGSMRVFVEHIHVLENSLAFKFHTKV---NGECTELNLVADKTEKAGEYSV--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049 120 hrypQVQSYNV-QVATTDYNQFAMVFFRKTSENKQYFKITLYGRTKELSPELKERFTRFAKSLGLKDDNIIFSVPTDQCI 198
Cdd:cd19428  79 ----TYDGYNTfTILETDYDNYIMFHLINFKNGETFQLMELYGREPDVSSDIKERFVKLCEEHGIIKENIIDLTKTDRCL 154
lipocalin_C8gamma cd19417
complement protein C8 gamma; Human complement protein C8 gamma, together with C8alpha and ...
37-194 3.14e-08

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: 50.90  E-value: 3.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  37 PLQPDFRSDQFRGRWYVVGLA--GNAVQkktEGSFTMYSTIYELQeNNSYNVTSILVRDQDQGCRYWIRTFVPSSRAGQF 114
Cdd:cd19417   1 QPAQNFDIQQFSGKWYLVAVAsaCRYLQ---ESGHKVEATVLTVA-PPKTTVAVSTFRKLNGICWEIKQEYGKTGTLGRF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049 115 TLgnMHRYPQVQSYNVqVATTDYNQFAMVFFRKTsenkQYFKITLYGRTKELSPELKERFTRFAKSLGLKDDnIIFSVPT 194
Cdd:cd19417  77 LL--KARRPRGNTDIV-VGETDYSSYAILYYQRA----GKLTMKLYGRSTELSENILDKFEQRAQKAHLGLD-QIFYFPK 148
lipocalin_6 cd19426
Epididymal-specific lipocalin-6; Epididymal-specific lipocalin-6 (LCN6) may play a role in ...
46-183 9.84e-04

Epididymal-specific lipocalin-6; Epididymal-specific lipocalin-6 (LCN6) may play a role in male fertility. It 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: 381201  Cd Length: 144  Bit Score: 38.05  E-value: 9.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  46 QFRGRWYVVGLA----GNAVQKKTEGSFTMYSTIyeLQENNSYNVTSilvRDQDQGCRYWIRTFVpsSRAGQFTLGNmhr 121
Cdd:cd19426  11 QLLGPWYVLAVAsrekSFAVEKDMKNVAGVVVTL--TPENNLRVLSS---QHGLGGCSQSVTELL--KRNSGWVFEN--- 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34328049 122 yPQVQSYNVQVATTDYNQFAMVFFRKTSENKQYFKITLYGRTKELSPELKERFTRFAKSLGL 183
Cdd:cd19426  81 -PSIGVLELRVLGTNFRDYAIVFTQLEFGDEPFNTVELYSRTETASQEAMGLFTKWSRGLGF 141
lipocalin_VDE cd19420
lipocalin domain of violaxanthin deepoxidase and similar proteins; Plant violaxanthin ...
29-184 1.70e-03

lipocalin domain of violaxanthin deepoxidase and similar proteins; Plant violaxanthin de-epoxidase (VDE, EC 1.23.5.1) participates in the xanthophyll cycle for controlling the concentration of zeaxanthin in chloroplasts. It catalyzes the conversion of violaxanthin to antheraxanthin and zeaxanthin in strong light, and plays a central role in adjusting photosynthetic activity to changing light conditions. In addition, maize VDE has been shown to interact with sugarcane mosaic virus helper component-proteinase, HC-(SCMV), and to attenuate the RNA silencing suppression activity of the latter. VDE 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: 381195  Cd Length: 177  Bit Score: 37.52  E-value: 1.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  29 PAPSLLTvpLQPDFRSDQFRGRWYVVglagnAVQKKTEGSFTMYSTIYELQENNS-YNVTSILVRDQDQG--CRYWIRTF 105
Cdd:cd19420   6 PVPDPSV--LVQSFDMNDFNGKWYIT-----AGLNPTFDTFDCQLHFFHVEGDDKlVGKINWRIKTPDGGffTRSAVQRF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049 106 V--PSSRAGQFTLGNMHRYPQ----VQSYNVQVATTDYnqfAMVFFRKTSEN-KQYFKITLYGRTKELSPELKERFTRFA 178
Cdd:cd19420  79 VqdPNQPGILYNHDNEYLHYQddwyILSYKIENKPEDY---IFVYYRGRNDAwDGYGGAVVYTRSSTLPPSYIPELEKAA 155

                ....*.
gi 34328049 179 KSLGLK 184
Cdd:cd19420 156 KKVGVD 161
lipocalin_Bla_g_4_Per_a_4 cd19440
major allergens Bla g 4 and Per a 4; Inhalant allergens from cockroaches are an important ...
38-143 1.86e-03

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: 37.09  E-value: 1.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  38 LQPDFRSDQFRGRWYVVGLAGNAVQKKTEgsfTMYSTiYELQENNSYNVTSIlVRDQDQGCRYWIRTFVPSSRAGQFTLg 117
Cdd:cd19440   7 LFTGFDYTKYLGVWYEAFRTPNAHEEQYK---CWIDR-FSLDPEGPIAVTSV-AYDSRGKNRVTLTGTVPVSTGNKFDI- 80
                        90       100
                ....*....|....*....|....*...
gi 34328049 118 nmhRYPQVQSYNVQ--VATTDYNQFAMV 143
Cdd:cd19440  81 ---DYGDDEAWSSQywVLGTDYETYAIL 105
lipocalin_AGP-like cd19451
alpha1-acid glycoprotein and similar proteins; Alpha1-acid glycoprotein (AGP), also known as ...
29-197 3.81e-03

alpha1-acid glycoprotein and similar proteins; Alpha1-acid glycoprotein (AGP), also known as orosomucoid, has many important biological roles such as in the acute-phase reaction in response to inflammation, in immune regulation, in drug-binding and drug-transportation, in regulating sphingolipid synthesis and metabolism, and in maintaining the capillary barrier. 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: 381226  Cd Length: 173  Bit Score: 36.56  E-value: 3.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049  29 PAPSLLTVPLQPDFRSDQFRGRWYVVGLAGNAVQKKTEGSFTMYSTIYeLQENNSYNvtSILVRD----QDQgCRYwIRT 104
Cdd:cd19451   1 PACANLTAAPITNATLDQLSGKWFYIGSAFRNPEYKKEVQEIQAAFFY-LTPNKTED--TILLREyqtiGDQ-CVY-NSS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328049 105 FVPSSRAGqftlGNMHRY-PQVQSYNVQVATTDYNQFAMVFFRKTSENKQYFkitLYGRTKELSPELKERFTRFAKSLGL 183
Cdd:cd19451  76 KLTVQREN----GTLSKYeGGVEHVAHLLLLRDPGTFMLAFFPEDEKNVGLS---FYADKPEATPEQLKEFYEALKCLGM 148
                       170
                ....*....|....*
gi 34328049 184 KDDNIIFSVPT-DQC 197
Cdd:cd19451 149 DESEIMYTDWKkDKC 163
lipocalin_OBP-like cd19427
Lipocalin odorant-binding protein and similar proteins; Odorant-binding proteins (OBPs) ...
157-197 7.74e-03

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: 35.32  E-value: 7.74e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 34328049 157 ITLYGRTKELSPELKERFTRFAKSLGLKDDNIIFSVPTDQC 197
Cdd:cd19427 107 TLLLGKGNSLTPEQKEKFKKLAEEKGIPEENIRNLLETDNC 147
 
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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