Ll_transcript_332848

Id TrinityTRINITY_DN28847_c0_g1_i1
Name TranscriptLl_transcript_332848
SequenceCTTGTCAACATTCAGGCTCAGCTCAAGAATGATGTTAAGTTGAACGACTATCTGATCAACCCGAGTATCAAGAAGAACATCAAGGTTGATGCAATCAAGG CAGCTGCAAAGCAGACCAATATGTCTGCCCCAGTCACCAACCTGCTGAGTCTTATGGCTGAGAACAATCGTCTGAAGCTTTTGAATGGTACCATCAACGC TTTCAAACAAATCATGGCTGCTGCCCGAGGAGAAGTGACATGTGAAGTCACCACTGCCAAGCCTCTGGATGCAGCTCTCCTGAAGGAAATTGAAGGAGCA CTCAAGGGCTTCGTGAAGTCAAACCAGAAAATTCTTCTGTCTACCAAGATTGATCCTAGCATCATTGGTGGAATGCTTGTCACCATTGGTGACAAGTATG TTGACATGAGCATTGCCTCTAAAGTTAGGAAGTATTCAAAGATTATTGGTGACAGTGCTTGAAGTTTGATTTTAATCATTGGATTGTAGTCCATTCATGT CTGTTATGTATATAAAC BLAST
Tissuepods
Gene nameLI_gene_125079; 
Additional informationdetails; 

Expression of Ll_transcript_332848

Labels

PAB abscising pods
PNAB non-abscising pods
PS1 seeds stages 1-3
PS2 seeds stages 4-6
PS3 seeds stages 7-8
PW1 pods wall stages 1-3
PW2 pods wall stages 4-6
PW3 pods wall stages 7-8

Annotations of Ll_transcript_332848

BlastpATP synthase subunit O, mitochondrial from Sophophora with 50.98% of identity
BlastxATP synthase subunit O, mitochondrial from Sophophora with 52.05% of identity
EggnogF(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity)(COG0712)
KeggLink to kegg annotations (Dmel_CG4307)
CantataDB-
Mirbase-
Ncbi proteinLink to NCBI protein (XP_015936928.1)
PfamATP synthase delta (OSCP) subunit (PF00213.17)
Rfam-
GOLinks to GO: General; Genes and gene products; Annotations; Ontology;
Links to GO: General; Genes and gene products; Annotations; Ontology;