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Conserved domains on  [gi|442618779|ref|NP_001262516|]
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yellow-f, isoform B [Drosophila melanogaster]

Protein Classification

major royal jelly family protein( domain architecture ID 10503411)

major royal jelly family protein similar to Drosophila melanogaster L-dopachrome tautomerase yellow-f and yellow-f2 that catalyze the tautomerization of L-dopachrome with decarboxylation to give 5,6-dihydroxyindole

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MRJP pfam03022
Major royal jelly protein; Royal jelly is the food of queen bee larvae, and is responsible for ...
129-417 7.27e-138

Major royal jelly protein; Royal jelly is the food of queen bee larvae, and is responsible for the high reproductive ability of the queen. Major royal jelly proteins make up around 90% of larval jelly proteins. This family also the sequence-related yellow protein of drosophila which controls pigmentation of the adult cuticle and larval mouth parts.


:

Pssm-ID: 308585  Cd Length: 288  Bit Score: 395.96  E-value: 7.27e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618779  129 VSVYRTSVDVCGRLWFVDTGMLEFPNNRQQIRHPSIWVIDLANDRLLKRFEIPQSIVEIGRGLASITIDVGARRCNDAYA 208
Cdd:pfam03022   1 VSVYRIAVDECDRLWVLDSGIVNTLQPPKQICPPKLLVFDLATDKLLKRIELPADVAKGNSRLVNLVVDAGDDTCDDTFA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618779  209 YIPDLVNRRLHVYHLRSDRIWSFEHSFFNFDPLSDNLNIGGQTFRWDDGIFSATLGSYKPDGsRDVFFHPMASTNEFVVS 288
Cdd:pfam03022  81 YIADAGGRGLIVYDLADDRSWRVEHNFFYPDPDFGKFTIAGESFQLDDGIFGLALSPITPDG-RTLYFHPLASTRLFSVP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618779  289 NRVLQQEFNAARSDHGDDFHLLGTRGpsTQSTMHKYDPrTGVIFFAEVQKSGVGCWKTSKPFSTENHGSVYSNSSEMIYP 368
Cdd:pfam03022 160 TEVLRNETNWGNNAQYEDFKDLGDRN--SQSTALAVDP-NGVLFFGLVGQNAIGCWNTSTPYSRANLGMVARNSDTLQFP 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442618779  369 SDLTIDE---EGYIWVMSNSMPIFVYSKLDVEKYNFRIWRQSTLLAKRGTVC 417
Cdd:pfam03022 237 SDLKIDKregEEYLWVLSNRMQKFLYNDLDYDEVNFRILGANVDLLIRNTVC 288
 
Name Accession Description Interval E-value
MRJP pfam03022
Major royal jelly protein; Royal jelly is the food of queen bee larvae, and is responsible for ...
129-417 7.27e-138

Major royal jelly protein; Royal jelly is the food of queen bee larvae, and is responsible for the high reproductive ability of the queen. Major royal jelly proteins make up around 90% of larval jelly proteins. This family also the sequence-related yellow protein of drosophila which controls pigmentation of the adult cuticle and larval mouth parts.


Pssm-ID: 308585  Cd Length: 288  Bit Score: 395.96  E-value: 7.27e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618779  129 VSVYRTSVDVCGRLWFVDTGMLEFPNNRQQIRHPSIWVIDLANDRLLKRFEIPQSIVEIGRGLASITIDVGARRCNDAYA 208
Cdd:pfam03022   1 VSVYRIAVDECDRLWVLDSGIVNTLQPPKQICPPKLLVFDLATDKLLKRIELPADVAKGNSRLVNLVVDAGDDTCDDTFA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618779  209 YIPDLVNRRLHVYHLRSDRIWSFEHSFFNFDPLSDNLNIGGQTFRWDDGIFSATLGSYKPDGsRDVFFHPMASTNEFVVS 288
Cdd:pfam03022  81 YIADAGGRGLIVYDLADDRSWRVEHNFFYPDPDFGKFTIAGESFQLDDGIFGLALSPITPDG-RTLYFHPLASTRLFSVP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618779  289 NRVLQQEFNAARSDHGDDFHLLGTRGpsTQSTMHKYDPrTGVIFFAEVQKSGVGCWKTSKPFSTENHGSVYSNSSEMIYP 368
Cdd:pfam03022 160 TEVLRNETNWGNNAQYEDFKDLGDRN--SQSTALAVDP-NGVLFFGLVGQNAIGCWNTSTPYSRANLGMVARNSDTLQFP 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442618779  369 SDLTIDE---EGYIWVMSNSMPIFVYSKLDVEKYNFRIWRQSTLLAKRGTVC 417
Cdd:pfam03022 237 SDLKIDKregEEYLWVLSNRMQKFLYNDLDYDEVNFRILGANVDLLIRNTVC 288
 
Name Accession Description Interval E-value
MRJP pfam03022
Major royal jelly protein; Royal jelly is the food of queen bee larvae, and is responsible for ...
129-417 7.27e-138

Major royal jelly protein; Royal jelly is the food of queen bee larvae, and is responsible for the high reproductive ability of the queen. Major royal jelly proteins make up around 90% of larval jelly proteins. This family also the sequence-related yellow protein of drosophila which controls pigmentation of the adult cuticle and larval mouth parts.


Pssm-ID: 308585  Cd Length: 288  Bit Score: 395.96  E-value: 7.27e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618779  129 VSVYRTSVDVCGRLWFVDTGMLEFPNNRQQIRHPSIWVIDLANDRLLKRFEIPQSIVEIGRGLASITIDVGARRCNDAYA 208
Cdd:pfam03022   1 VSVYRIAVDECDRLWVLDSGIVNTLQPPKQICPPKLLVFDLATDKLLKRIELPADVAKGNSRLVNLVVDAGDDTCDDTFA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618779  209 YIPDLVNRRLHVYHLRSDRIWSFEHSFFNFDPLSDNLNIGGQTFRWDDGIFSATLGSYKPDGsRDVFFHPMASTNEFVVS 288
Cdd:pfam03022  81 YIADAGGRGLIVYDLADDRSWRVEHNFFYPDPDFGKFTIAGESFQLDDGIFGLALSPITPDG-RTLYFHPLASTRLFSVP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618779  289 NRVLQQEFNAARSDHGDDFHLLGTRGpsTQSTMHKYDPrTGVIFFAEVQKSGVGCWKTSKPFSTENHGSVYSNSSEMIYP 368
Cdd:pfam03022 160 TEVLRNETNWGNNAQYEDFKDLGDRN--SQSTALAVDP-NGVLFFGLVGQNAIGCWNTSTPYSRANLGMVARNSDTLQFP 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442618779  369 SDLTIDE---EGYIWVMSNSMPIFVYSKLDVEKYNFRIWRQSTLLAKRGTVC 417
Cdd:pfam03022 237 SDLKIDKregEEYLWVLSNRMQKFLYNDLDYDEVNFRILGANVDLLIRNTVC 288
 
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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