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Conserved domains on  [gi|1624698687|ref|NP_650937|]
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uncharacterized protein Dmel_CG17279 [Drosophila melanogaster]

Protein Classification

JHBP domain-containing protein( domain architecture ID 10534990)

JHBP (juvenile hormone-binding protein) domain-containing protein similar to Drosophila melanogaster protein takeout that participates in a novel circadian output pathway that conveys temporal and food status information to feeding-relevant metabolisms and activities

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
JHBP pfam06585
Haemolymph juvenile hormone binding protein (JHBP); This family consists of several ...
 5-243 2.19e-53

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: 172.39  E-value: 2.19e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698687   5 VFVCCLWMAPSLGQLPPEIEKCRAGDSI---CIAETVTRILRLYPKGLPSIGLVALDSIGFEDVVVSRlePDGSSTFDLK 81
Cdd:pfam06585   1 LLLLLLAVAASAAELPSYIKKCKRSDPNlnkCLKEAIEALRPQLAKGIPELGIPPLDPLVIDELSIDQ--GSGPVGLKLN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698687  82 FPNLTVIGFADSTVTEAKGFDADLPrvLELSGWIPLLKLNGTYEMRGSLLTMPIHGKGQAKVEIRECRVRCKVRVlEDLR 161
Cdd:pfam06585  79 LKNVKIYGLSNFTIKKVKVDLKDLK--IEFDLLFPKLRLEGKYKADGRILLLPINGKGDFNITLENLKAKGTLKG-EPVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698687 162 DDGKLYAGISKVKCLLDVQGMHLNLENLFN-NPEMSDAMNVVANTKWLEIWHNLRRGITSAVDQLVESILQRVANKLPYD 240
Cdd:pfam06585 156 KNGKTYLKITDLKVKFKVGDVKFHLDNLFNgNKELGDAINQFLNENWREVLNELKPAIEEALSEIFTDILNKIFSNVPYD 235


                  ...
gi 1624698687 241 DLY 243
Cdd:pfam06585 236 ELF 238
 
Name Accession Description Interval E-value
JHBP pfam06585
Haemolymph juvenile hormone binding protein (JHBP); This family consists of several ...
 5-243 2.19e-53

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: 172.39  E-value: 2.19e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698687   5 VFVCCLWMAPSLGQLPPEIEKCRAGDSI---CIAETVTRILRLYPKGLPSIGLVALDSIGFEDVVVSRlePDGSSTFDLK 81
Cdd:pfam06585   1 LLLLLLAVAASAAELPSYIKKCKRSDPNlnkCLKEAIEALRPQLAKGIPELGIPPLDPLVIDELSIDQ--GSGPVGLKLN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698687  82 FPNLTVIGFADSTVTEAKGFDADLPrvLELSGWIPLLKLNGTYEMRGSLLTMPIHGKGQAKVEIRECRVRCKVRVlEDLR 161
Cdd:pfam06585  79 LKNVKIYGLSNFTIKKVKVDLKDLK--IEFDLLFPKLRLEGKYKADGRILLLPINGKGDFNITLENLKAKGTLKG-EPVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698687 162 DDGKLYAGISKVKCLLDVQGMHLNLENLFN-NPEMSDAMNVVANTKWLEIWHNLRRGITSAVDQLVESILQRVANKLPYD 240
Cdd:pfam06585 156 KNGKTYLKITDLKVKFKVGDVKFHLDNLFNgNKELGDAINQFLNENWREVLNELKPAIEEALSEIFTDILNKIFSNVPYD 235


                  ...
gi 1624698687 241 DLY 243
Cdd:pfam06585 236 ELF 238
JHBP smart00700
Juvenile hormone binding protein domains in insects; The juvenile hormone exerts pleiotropic ...
 18-243 1.34e-31

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: 115.85  E-value: 1.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698687   18 QLPPEIEKCRAGD-SICIAETVTRILRLYPKGLPSIGLVALDSIGFEDVVVSRLEPDGSSTFDLKfpNLTVIGFADSTVT 96
Cdd:smart00700   2 EGPAFLKPCKLGDpSECLRDAIEALLPQLKNGIPEYGIPPLDPLEIDDLKISIDSGVIGLRLTFK--NVKIYGLSNFEIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698687   97 EAKGFDADlpRVLELSGWIPLLKLNGTYEMRGSLLTMPIHGKGQAKVEIRECRVRCKVRVleDLRDDGKLYAGISKVKCL 176
Cdd:smart00700  80 KFKMDLKD--KKIELKIEFPKLNVKGDYKLDGRLLGLPLNGKGDANFTLENVKIRGTLKL--KLGPDGKTYLKIKSLKVN 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624698687  177 LDVQGMHLNLENLFN-NPEMSDAMNVVANTKWLEIWHNLRRGITSAVDQLVESILQRVANKLPYDDLY 243
Cdd:smart00700 156 FEVGDVKSHLDNLFNgNKDLNDAINKFLNENWKALINELLPAIVEKLESIFLDLVNKVFAKVPIDEFF 223
 
Name Accession Description Interval E-value
JHBP pfam06585
Haemolymph juvenile hormone binding protein (JHBP); This family consists of several ...
 5-243 2.19e-53

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: 172.39  E-value: 2.19e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698687   5 VFVCCLWMAPSLGQLPPEIEKCRAGDSI---CIAETVTRILRLYPKGLPSIGLVALDSIGFEDVVVSRlePDGSSTFDLK 81
Cdd:pfam06585   1 LLLLLLAVAASAAELPSYIKKCKRSDPNlnkCLKEAIEALRPQLAKGIPELGIPPLDPLVIDELSIDQ--GSGPVGLKLN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698687  82 FPNLTVIGFADSTVTEAKGFDADLPrvLELSGWIPLLKLNGTYEMRGSLLTMPIHGKGQAKVEIRECRVRCKVRVlEDLR 161
Cdd:pfam06585  79 LKNVKIYGLSNFTIKKVKVDLKDLK--IEFDLLFPKLRLEGKYKADGRILLLPINGKGDFNITLENLKAKGTLKG-EPVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698687 162 DDGKLYAGISKVKCLLDVQGMHLNLENLFN-NPEMSDAMNVVANTKWLEIWHNLRRGITSAVDQLVESILQRVANKLPYD 240
Cdd:pfam06585 156 KNGKTYLKITDLKVKFKVGDVKFHLDNLFNgNKELGDAINQFLNENWREVLNELKPAIEEALSEIFTDILNKIFSNVPYD 235


                  ...
gi 1624698687 241 DLY 243
Cdd:pfam06585 236 ELF 238
JHBP smart00700
Juvenile hormone binding protein domains in insects; The juvenile hormone exerts pleiotropic ...
 18-243 1.34e-31

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: 115.85  E-value: 1.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698687   18 QLPPEIEKCRAGD-SICIAETVTRILRLYPKGLPSIGLVALDSIGFEDVVVSRLEPDGSSTFDLKfpNLTVIGFADSTVT 96
Cdd:smart00700   2 EGPAFLKPCKLGDpSECLRDAIEALLPQLKNGIPEYGIPPLDPLEIDDLKISIDSGVIGLRLTFK--NVKIYGLSNFEIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698687   97 EAKGFDADlpRVLELSGWIPLLKLNGTYEMRGSLLTMPIHGKGQAKVEIRECRVRCKVRVleDLRDDGKLYAGISKVKCL 176
Cdd:smart00700  80 KFKMDLKD--KKIELKIEFPKLNVKGDYKLDGRLLGLPLNGKGDANFTLENVKIRGTLKL--KLGPDGKTYLKIKSLKVN 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624698687  177 LDVQGMHLNLENLFN-NPEMSDAMNVVANTKWLEIWHNLRRGITSAVDQLVESILQRVANKLPYDDLY 243
Cdd:smart00700 156 FEVGDVKSHLDNLFNgNKDLNDAINKFLNENWKALINELLPAIVEKLESIFLDLVNKVFAKVPIDEFF 223
 
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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