JHBP (juvenile hormone-binding protein) domain-containing protein similar to Drosophila melanogaster circadian clock-controlled protein that is component of the circadian clock or downstream effector of clock function
Juvenile hormone binding protein domains in insects; The juvenile hormone exerts pleiotropic ...
7-236
7.91e-57
Juvenile hormone binding protein domains in insects; The juvenile hormone exerts pleiotropic functions during insect life cycles and its binding proteins regulate these functions.
:
Pssm-ID: 214779 Cd Length: 224 Bit Score: 180.95 E-value: 7.91e-57
Juvenile hormone binding protein domains in insects; The juvenile hormone exerts pleiotropic ...
7-236
7.91e-57
Juvenile hormone binding protein domains in insects; The juvenile hormone exerts pleiotropic functions during insect life cycles and its binding proteins regulate these functions.
Pssm-ID: 214779 Cd Length: 224 Bit Score: 180.95 E-value: 7.91e-57
Haemolymph juvenile hormone binding protein (JHBP); This family consists of several ...
9-234
9.24e-37
Haemolymph juvenile hormone binding protein (JHBP); This family consists of several insect-specific haemolymph juvenile hormone binding proteins (JHBP). Juvenile hormone regulates embryogenesis, maintains the status quo of larval development and stimulates reproductive maturation in the adult insect. JH is transported from the sites of its synthesis to target tissues by a haemolymph carrier called juvenile hormone-binding protein (JHBP). JHBP protects the JH molecules from hydrolysis by non-specific esterases present in the insect haemolymph. The crystal structure of the JHBP from Galleria mellonella shows an unusual fold consisting of a long alpha-helix wrapped in a much curved antiparallel beta-sheet. The folding pattern for this structure closely resembles that found in some tandem-repeat mammalian lipid-binding and bactericidal permeability-increasing proteins, with a similar organization of the major cavity and a disulfide bond linking the long helix and the beta-sheet. It would appear that JHBP forms two cavities, only one of which, the one near the N- and C-termini, binds the hormone; binding induces a conformational change, of unknown significance. This family now includes DUF233, pfam03027.
Pssm-ID: 461956 Cd Length: 239 Bit Score: 129.63 E-value: 9.24e-37
Juvenile hormone binding protein domains in insects; The juvenile hormone exerts pleiotropic ...
7-236
7.91e-57
Juvenile hormone binding protein domains in insects; The juvenile hormone exerts pleiotropic functions during insect life cycles and its binding proteins regulate these functions.
Pssm-ID: 214779 Cd Length: 224 Bit Score: 180.95 E-value: 7.91e-57
Haemolymph juvenile hormone binding protein (JHBP); This family consists of several ...
9-234
9.24e-37
Haemolymph juvenile hormone binding protein (JHBP); This family consists of several insect-specific haemolymph juvenile hormone binding proteins (JHBP). Juvenile hormone regulates embryogenesis, maintains the status quo of larval development and stimulates reproductive maturation in the adult insect. JH is transported from the sites of its synthesis to target tissues by a haemolymph carrier called juvenile hormone-binding protein (JHBP). JHBP protects the JH molecules from hydrolysis by non-specific esterases present in the insect haemolymph. The crystal structure of the JHBP from Galleria mellonella shows an unusual fold consisting of a long alpha-helix wrapped in a much curved antiparallel beta-sheet. The folding pattern for this structure closely resembles that found in some tandem-repeat mammalian lipid-binding and bactericidal permeability-increasing proteins, with a similar organization of the major cavity and a disulfide bond linking the long helix and the beta-sheet. It would appear that JHBP forms two cavities, only one of which, the one near the N- and C-termini, binds the hormone; binding induces a conformational change, of unknown significance. This family now includes DUF233, pfam03027.
Pssm-ID: 461956 Cd Length: 239 Bit Score: 129.63 E-value: 9.24e-37
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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