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Conserved domains on  [gi|161078310|ref|NP_001097798|]
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uncharacterized protein Dmel_CG34316 [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
JHBP super family cl12117
Haemolymph juvenile hormone binding protein (JHBP); This family consists of several ...
 32-231 5.57e-26

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.


The actual alignment was detected with superfamily member pfam06585:

Pssm-ID: 472279  Cd Length: 239  Bit Score: 101.90  E-value: 5.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078310   32 ILAFLQEFRMRMCHPIPNLGLPALDPLQLGPAETELNNKyLVDFTGSIDNFQLHGLSDFDVPALSLSPvPGLKNTINVTL 111
Cdd:pfam06585  33 LKEAIEALRPQLAKGIPELGIPPLDPLVIDELSIDQGSG-PVGLKLNLKNVKIYGLSNFTIKKVKVDL-KDLKIEFDLLF 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078310  112 PLTYFKSLYTAKGSLAyILNLAGDGNAETSITNFSILISFRLRSVSP-----LAISSLQIELRLGGLWINFDNLMEEDRI 186
Cdd:pfam06585 111 PKLRLEGKYKADGRIL-LLPINGKGDFNITLENLKAKGTLKGEPVEKngktyLKITDLKVKFKVGDVKFHLDNLFNGNKE 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 161078310  187 -NDFIHALVNEMGVELLGDVWDYEQGTVVSKVQAAVNNFLGQYSLS 231
Cdd:pfam06585 190 lGDAINQFLNENWREVLNELKPAIEEALSEIFTDILNKIFSNVPYD 235
 
Name Accession Description Interval E-value
JHBP pfam06585
Haemolymph juvenile hormone binding protein (JHBP); This family consists of several ...
 32-231 5.57e-26

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: 101.90  E-value: 5.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078310   32 ILAFLQEFRMRMCHPIPNLGLPALDPLQLGPAETELNNKyLVDFTGSIDNFQLHGLSDFDVPALSLSPvPGLKNTINVTL 111
Cdd:pfam06585  33 LKEAIEALRPQLAKGIPELGIPPLDPLVIDELSIDQGSG-PVGLKLNLKNVKIYGLSNFTIKKVKVDL-KDLKIEFDLLF 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078310  112 PLTYFKSLYTAKGSLAyILNLAGDGNAETSITNFSILISFRLRSVSP-----LAISSLQIELRLGGLWINFDNLMEEDRI 186
Cdd:pfam06585 111 PKLRLEGKYKADGRIL-LLPINGKGDFNITLENLKAKGTLKGEPVEKngktyLKITDLKVKFKVGDVKFHLDNLFNGNKE 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 161078310  187 -NDFIHALVNEMGVELLGDVWDYEQGTVVSKVQAAVNNFLGQYSLS 231
Cdd:pfam06585 190 lGDAINQFLNENWREVLNELKPAIEEALSEIFTDILNKIFSNVPYD 235
JHBP smart00700
Juvenile hormone binding protein domains in insects; The juvenile hormone exerts pleiotropic ...
 32-205 1.64e-19

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: 84.26  E-value: 1.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078310    32 ILAFLQEFRMRMCHPIPNLGLPALDPLQLGPAETELNNKyLVDFTGSIDNFQLHGLSDFDVPALSLSPVpGLKNTINVTL 111
Cdd:smart00700  19 LRDAIEALLPQLKNGIPEYGIPPLDPLEIDDLKISIDSG-VIGLRLTFKNVKIYGLSNFEITKFKMDLK-DKKIELKIEF 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078310   112 PLTYFKSLYTAKGSLaYILNLAGDGNAETSITNFSILISFRLR----SVSPLAISSLQIELRLGGLWINFDNLMEEDR-I 186
Cdd:smart00700  97 PKLNVKGDYKLDGRL-LGLPLNGKGDANFTLENVKIRGTLKLKlgpdGKTYLKIKSLKVNFEVGDVKSHLDNLFNGNKdL 175

                          170
                   ....*....|....*....
gi 161078310   187 NDFIHALVNEMGVELLGDV 205
Cdd:smart00700 176 NDAINKFLNENWKALINEL 194
 
Name Accession Description Interval E-value
JHBP pfam06585
Haemolymph juvenile hormone binding protein (JHBP); This family consists of several ...
 32-231 5.57e-26

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: 101.90  E-value: 5.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078310   32 ILAFLQEFRMRMCHPIPNLGLPALDPLQLGPAETELNNKyLVDFTGSIDNFQLHGLSDFDVPALSLSPvPGLKNTINVTL 111
Cdd:pfam06585  33 LKEAIEALRPQLAKGIPELGIPPLDPLVIDELSIDQGSG-PVGLKLNLKNVKIYGLSNFTIKKVKVDL-KDLKIEFDLLF 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078310  112 PLTYFKSLYTAKGSLAyILNLAGDGNAETSITNFSILISFRLRSVSP-----LAISSLQIELRLGGLWINFDNLMEEDRI 186
Cdd:pfam06585 111 PKLRLEGKYKADGRIL-LLPINGKGDFNITLENLKAKGTLKGEPVEKngktyLKITDLKVKFKVGDVKFHLDNLFNGNKE 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 161078310  187 -NDFIHALVNEMGVELLGDVWDYEQGTVVSKVQAAVNNFLGQYSLS 231
Cdd:pfam06585 190 lGDAINQFLNENWREVLNELKPAIEEALSEIFTDILNKIFSNVPYD 235
JHBP smart00700
Juvenile hormone binding protein domains in insects; The juvenile hormone exerts pleiotropic ...
 32-205 1.64e-19

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: 84.26  E-value: 1.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078310    32 ILAFLQEFRMRMCHPIPNLGLPALDPLQLGPAETELNNKyLVDFTGSIDNFQLHGLSDFDVPALSLSPVpGLKNTINVTL 111
Cdd:smart00700  19 LRDAIEALLPQLKNGIPEYGIPPLDPLEIDDLKISIDSG-VIGLRLTFKNVKIYGLSNFEITKFKMDLK-DKKIELKIEF 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078310   112 PLTYFKSLYTAKGSLaYILNLAGDGNAETSITNFSILISFRLR----SVSPLAISSLQIELRLGGLWINFDNLMEEDR-I 186
Cdd:smart00700  97 PKLNVKGDYKLDGRL-LGLPLNGKGDANFTLENVKIRGTLKLKlgpdGKTYLKIKSLKVNFEVGDVKSHLDNLFNGNKdL 175

                          170
                   ....*....|....*....
gi 161078310   187 NDFIHALVNEMGVELLGDV 205
Cdd:smart00700 176 NDAINKFLNENWKALINEL 194
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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