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Protein Overview: FBpp0309737, CG3...

General Information:
Name(s) found: FBpp0309737 [FlyBase]
CG33080-PB / FBpp0070810 [FlyBase]
Description(s) found:
Found 23 descriptions.
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  • type=protein; loc=X:complement(5602940..5603076,5603161..5605006,5605510..5605605,5605668..5605766); ID=FBpp0309737; name=CG33080-PD; parent=FBgn0053080,FBtr0342972; dbxref=FlyBase:FBpp0309737,FlyBase_Annotation_IDs:CG33080-PD; MD5=49df534a24936aa99a003f01a9dde532; length=725; release=r5.56; species=Dmel; [FlyBase]
  • This gene is referred to in FlyBase by the symbol Dmel\CG33080 (CG33080, FBgn0053080). It is a protein_coding_gene from Drosophila melanogaster. Its sequence location is X:5602594..5611811. It has the cytological map location 5B1-5B2. Based on sequence similarity, it is predicted to have molecular function</span>: alpha-glucosidase activity. An electronic pipeline based on InterPro domains suggests that it is involved in the biological process</span>: carbohydrate metabolic process. 5 alleles are reported. No phenotypic data is available. It has 2 annotated transcripts and 2 annotated polypeptides. [FlyBase]
    • Organism: Drosophila melanogaster
    Length: 725 amino acids

    Gene Ontology:
    Cellular Component: alpha-glucosidase II complex [ISS]
    Biological Process: carbohydrate metabolic process [IEA]
    Molecular Function: alpha-glucosidase activity [ISS]


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MLASDFDSHS LASNQASITS VNSLASLLRE KMQAFPQLIR KKKRETKDYK IKIFVIIMFF  60
   61 IIIFLIGYAY VAYHQQVLTR SYFQKIKFNS HDRIFRILSH EDKEVISGQL GVTLGFDTAP 120
  121 FHCLEEQRRS DGSVCIEWNG VARLHLNFED KGVFRCYTLQ WQALTPGLLP TDCYELKRDN 180
  181 GLWFGGGVTK GQEWSLSYAN FDFAPYASGD SKIHQFGNGV KRYFINSIGV AMQVSEKTPL 240
  241 QLGVNRTENR FCLRAANDEF TFVNHLTPLP QLDYRICTTE DMRSLHMLMT QQSLWDGLKE 300
  301 QEFKVLHSLL EEPVWRIPHT ELPESLNESA ICDYSESAIA MGLGHIVINE FWQENIGDFT 360
  361 VDKARFPTLK DTIDVLHRRG FKVVLTIQPF ISTDSANFKD AVKRKLLIYE RHSERSIPAL 420
  421 TRYKSSSSAG VLDITNNASV PWLLEKLQRL KEEYGVQSFY LDLGTGYNLP HYYQCRQTLD 480
  481 NPDTYARLFT ASLEGAGLMA VSTASVVPKP PTFLSTPPAN ATWEGLRETL GAVLNYGVIG 540
  541 YPFVLPGVIG GDYLLQRPLS KMVSFYSLSQ PPLPDPELFI RWLQLATFMP AMQFSHLPSE 600
  601 YRSDLVTRVA QELKEVRQLI VIPLLKKYLN PSMNEGLPLV RPLWMMDPHD PACLIVSDEF 660
  661 SVGEELIVAP ILHANREERE VYLPQGVWKD GIDGSLRKGS RWMHGYRVPK DKIAYFRKMP 720
  721 DNTRF

    Protein Complex Data

    No complex found for this protein.

    Mass Spectrometry Data

    No mass spectrometry results found for this protein.

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    NOT SHOWING SINGLE HITS. [ Show Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

    No yeast two-hybrid interactions found for this protein.

    Microscopy / Localization Data

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    No microscopy data found in the PDR for this protein.

    Protein Structure Data


    [What does the above image mean?]
    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..177] deduced N/A No confident structure predictions are available.
    2 View Details [178..725] PSI-BLAST 103.0 Crystal Structure of Alpha-Xylosidase from Escherichia coli

    Functions predicted (by domain):

    # Gene Ontology predictions
    1 No functions predicted.
    2
    Term Confidence Notes
  • glucosidase activity
    		•  3.36236519085847 bayes_pls_golite062009
  • alpha-glucosidase activity
    		•  2.3919781440515 bayes_pls_golite062009
  • hydrolase activity, hydrolyzing O-glycosyl compounds
    		•  1.98403928115322 bayes_pls_golite062009
  • hydrolase activity, acting on glycosyl bonds
    		•  1.98114731783916 bayes_pls_golite062009
  • hydrolase activity
    		•  1.3322356610484 bayes_pls_golite062009
  • catalytic activity
    		•  0.95519213931595 bayes_pls_golite062009


    Reference: Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16


    Philius Transmembrane Prediction:

    [View Details]
    Source: Reynolds et al. 2008. Manuscript submitted Philius confidence legend
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