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Conserved domains on  [gi|442634170|ref|NP_001262213|]
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uncharacterized protein Dmel_CG14457, isoform C [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 ...
8-252 3.52e-67

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: 208.60  E-value: 3.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442634170    8 VLLVTFTTCLVRAEdgflkEPHYIKECRIADKDFVNCSTHSIQQLFDKLNDGIPGLtSIRSFDPFYLNRIRITQGNsNAI 87
Cdd:pfam06585   1 LLLLLLAVAASAAE-----LPSYIKKCKRSDPNLNKCLKEAIEALRPQLAKGIPEL-GIPPLDPLVIDELSIDQGS-GPV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442634170   88 NLKVELANVKIIGFGHTNVLDSQVFKKDYSWKTTFTLPEMKLQADYSLFGRILLIPLNGKGQVFLDAENMTVTMHTKTRL 167
Cdd:pfam06585  74 GLKLNLKNVKIYGLSNFTIKKVKVDLKDLKIEFDLLFPKLRLEGKYKADGRILLLPINGKGDFNITLENLKAKGTLKGEP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442634170  168 YSKGGFTFYNVTNLHVDFKMDGLKSYFSNLFNGNKQLEDSTNKFFNDNWRMLADALYTVITQTIEDILLDVLKKIFHFIP 247
Cdd:pfam06585 154 VEKNGKTYLKITDLKVKFKVGDVKFHLDNLFNGNKELGDAINQFLNENWREVLNELKPAIEEALSEIFTDILNKIFSNVP 233

                  ....*
gi 442634170  248 ANFFV 252
Cdd:pfam06585 234 YDELF 238
 
Name Accession Description Interval E-value
JHBP pfam06585
Haemolymph juvenile hormone binding protein (JHBP); This family consists of several ...
8-252 3.52e-67

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: 208.60  E-value: 3.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442634170    8 VLLVTFTTCLVRAEdgflkEPHYIKECRIADKDFVNCSTHSIQQLFDKLNDGIPGLtSIRSFDPFYLNRIRITQGNsNAI 87
Cdd:pfam06585   1 LLLLLLAVAASAAE-----LPSYIKKCKRSDPNLNKCLKEAIEALRPQLAKGIPEL-GIPPLDPLVIDELSIDQGS-GPV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442634170   88 NLKVELANVKIIGFGHTNVLDSQVFKKDYSWKTTFTLPEMKLQADYSLFGRILLIPLNGKGQVFLDAENMTVTMHTKTRL 167
Cdd:pfam06585  74 GLKLNLKNVKIYGLSNFTIKKVKVDLKDLKIEFDLLFPKLRLEGKYKADGRILLLPINGKGDFNITLENLKAKGTLKGEP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442634170  168 YSKGGFTFYNVTNLHVDFKMDGLKSYFSNLFNGNKQLEDSTNKFFNDNWRMLADALYTVITQTIEDILLDVLKKIFHFIP 247
Cdd:pfam06585 154 VEKNGKTYLKITDLKVKFKVGDVKFHLDNLFNGNKELGDAINQFLNENWREVLNELKPAIEEALSEIFTDILNKIFSNVP 233

                  ....*
gi 442634170  248 ANFFV 252
Cdd:pfam06585 234 YDELF 238
JHBP smart00700
Juvenile hormone binding protein domains in insects; The juvenile hormone exerts pleiotropic ...
28-253 2.40e-54

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: 175.17  E-value: 2.40e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442634170    28 PHYIKECRIadKDFVNCSTHSIQQLFDKLNDGIPGLtSIRSFDPFYLNRIRITQGNSNaINLKVELANVKIIGFGHTNVL 107
Cdd:smart00700   4 PAFLKPCKL--GDPSECLRDAIEALLPQLKNGIPEY-GIPPLDPLEIDDLKISIDSGV-IGLRLTFKNVKIYGLSNFEIT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442634170   108 DSQVFKKDYSWKTTFTLPEMKLQADYSLFGRILLIPLNGKGQVFLDAENMTVTMHTKTRLYSKGgFTFYNVTNLHVDFKM 187
Cdd:smart00700  80 KFKMDLKDKKIELKIEFPKLNVKGDYKLDGRLLGLPLNGKGDANFTLENVKIRGTLKLKLGPDG-KTYLKIKSLKVNFEV 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442634170   188 DGLKSYFSNLFNGNKQLEDSTNKFFNDNWRMLADALYTVITQTIEDILLDVLKKIFHFIPANFFVS 253
Cdd:smart00700 159 GDVKSHLDNLFNGNKDLNDAINKFLNENWKALINELLPAIVEKLESIFLDLVNKVFAKVPIDEFFV 224
 
Name Accession Description Interval E-value
JHBP pfam06585
Haemolymph juvenile hormone binding protein (JHBP); This family consists of several ...
8-252 3.52e-67

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: 208.60  E-value: 3.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442634170    8 VLLVTFTTCLVRAEdgflkEPHYIKECRIADKDFVNCSTHSIQQLFDKLNDGIPGLtSIRSFDPFYLNRIRITQGNsNAI 87
Cdd:pfam06585   1 LLLLLLAVAASAAE-----LPSYIKKCKRSDPNLNKCLKEAIEALRPQLAKGIPEL-GIPPLDPLVIDELSIDQGS-GPV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442634170   88 NLKVELANVKIIGFGHTNVLDSQVFKKDYSWKTTFTLPEMKLQADYSLFGRILLIPLNGKGQVFLDAENMTVTMHTKTRL 167
Cdd:pfam06585  74 GLKLNLKNVKIYGLSNFTIKKVKVDLKDLKIEFDLLFPKLRLEGKYKADGRILLLPINGKGDFNITLENLKAKGTLKGEP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442634170  168 YSKGGFTFYNVTNLHVDFKMDGLKSYFSNLFNGNKQLEDSTNKFFNDNWRMLADALYTVITQTIEDILLDVLKKIFHFIP 247
Cdd:pfam06585 154 VEKNGKTYLKITDLKVKFKVGDVKFHLDNLFNGNKELGDAINQFLNENWREVLNELKPAIEEALSEIFTDILNKIFSNVP 233

                  ....*
gi 442634170  248 ANFFV 252
Cdd:pfam06585 234 YDELF 238
JHBP smart00700
Juvenile hormone binding protein domains in insects; The juvenile hormone exerts pleiotropic ...
28-253 2.40e-54

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: 175.17  E-value: 2.40e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442634170    28 PHYIKECRIadKDFVNCSTHSIQQLFDKLNDGIPGLtSIRSFDPFYLNRIRITQGNSNaINLKVELANVKIIGFGHTNVL 107
Cdd:smart00700   4 PAFLKPCKL--GDPSECLRDAIEALLPQLKNGIPEY-GIPPLDPLEIDDLKISIDSGV-IGLRLTFKNVKIYGLSNFEIT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442634170   108 DSQVFKKDYSWKTTFTLPEMKLQADYSLFGRILLIPLNGKGQVFLDAENMTVTMHTKTRLYSKGgFTFYNVTNLHVDFKM 187
Cdd:smart00700  80 KFKMDLKDKKIELKIEFPKLNVKGDYKLDGRLLGLPLNGKGDANFTLENVKIRGTLKLKLGPDG-KTYLKIKSLKVNFEV 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442634170   188 DGLKSYFSNLFNGNKQLEDSTNKFFNDNWRMLADALYTVITQTIEDILLDVLKKIFHFIPANFFVS 253
Cdd:smart00700 159 GDVKSHLDNLFNGNKDLNDAINKFLNENWKALINELLPAIVEKLESIFLDLVNKVFAKVPIDEFFV 224
 
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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