SustainPineDB

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Assembly info
Unigenes
SNPs
SSRs
Descriptions
GOs
ECs
KEGGs
InterPros
miRNAs

Assembly Name: SustainPine v3.0

UniGene Name: sp_v3.0_unigene155408

Length: 458 nt

UniGene Fasta

>sp_v3.0_unigene155408
TCTATCGATATGGACAAGGCAGTCGAAAGCCGCGCTAAGCTCAATGATATCAGTCCCGCAAAGATCAGCTTCAACGATATGGTGATCAAGGCTGTATCCATCGCACTCAAACAACATCCAGCCATCAACAGCAGCTGGAGAGGCGAGACCATCCGCGTCAACCACCACGTGAATGTAGGCGTTGCTATCGCGATCCCCGACGGACTCGTAGTCCCGGTCATCCGCTTTGCAGACACCAAGAGCCTTTCGCAGATCGCAACCGAAGTCAAAGATTTCGCCGGCAAGGCCAAGAATAAAAAACTCCAGCCCTCAGATTGGGAAGGCAGCACTTTCACTATCTCTAACCTGGGTATGTTCGGTATCGATGATTTCACTGCTATCCTCAATCCCCCGGACTCCTGCATCCTCGCTGTCGGCGCTATCCAACAGGTACCCGTCGTCAAGAACGGCGCTGTAGT

Ace file of the UniGene sp_v3.0_unigene155408

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Annotations

Source	Descriptions	Term	Type	e value	Identity
AutoFact	Dihydrolipoyllysine-residue acetyltransferase (Dihydrolipoamide S-acetyltransferase) n=1 Tax=Pedobacter sp. BAL39 RepID=A6EAZ4_9SPHI	-	-	0.0	75%
FL-Next	tr=Putative uncharacterized protein; Picea sitchensis (Sitka spruce) (Pinus sitchensis).	-	-	0.0	49%
Sma3	PDCE2	-	-	9.004e-08	-

Source	ECs	Term	Type	e value	Identity
Sma3	Dihydrolipoyllysine-residue acetyltransferase.	EC:2.3.1.12	-	1.773e-15	-

Source	KEGGs	Term	e value	Identity
Sma3	Glycolysis / Gluconeogenesis	00010	1.773e-15	%
Sma3	Citrate cycle (TCA cycle)	00020	1.773e-15	%
Sma3	Pyruvate metabolism	00620	1.773e-15	%
Sma3	Biosynthesis of phenylpropanoids	01061	1.773e-15	%
Sma3	Biosynthesis of terpenoids and steroids	01062	1.773e-15	%
Sma3	Biosynthesis of alkaloids derived from shikimate pathway	01063	1.773e-15	%
Sma3	Biosynthesis of alkaloids derived from ornithine, lysine and nicotinic acid	01064	1.773e-15	%
Sma3	Biosynthesis of alkaloids derived from histidine and purine	01065	1.773e-15	%
Sma3	Biosynthesis of alkaloids derived from terpenoid and polyketide	01066	1.773e-15	%
Sma3	Biosynthesis of plant hormones	01070	1.773e-15	%
Sma3	Metabolic pathways	01100	1.773e-15	%
Sma3	Biosynthesis of secondary metabolites	01110	1.773e-15	%

Source	Gene names
Sma3	At1g54220; At3g13930; CHLREDRAFT_149709; DLA1; F20D21.4; GSVIVT00010806001; GSVIVT00016525001; MDC16.5; MICPUCDRAFT_25687; MICPUN_96637; OJ1212_C06.22; OJ1359_D06.3; OJA1212_C06.23; OSTLU_31760; Os02g0105200; Os06g0105400; Os07g0410100; OsI_00490; OsI_054

Source	GOs	Term	Type	Identity
Sma3	mitochondrial matrix	GO:0005759	Cellular Component	-
Sma3	chloroplast envelope	GO:0009941	Cellular Component	-
Sma3	pyruvate dehydrogenase complex	GO:0045254	Cellular Component	-
Sma3	dihydrolipoyllysine-residue acetyltransferase activity	GO:0004742	Molecular Function	-
Sma3	protein binding	GO:0005515	Molecular Function	-
Sma3		GO:0008415	Molecular Function	-
Sma3	lipoic acid binding	GO:0031405	Molecular Function	-
Sma3	pyruvate metabolic process	GO:0006090	Biological Process	-
Sma3	glycolysis	GO:0006096	Biological Process	-
Sma3	metabolic process	GO:0008152	Biological Process	-

Source	InterPros	Term	Type	Identity
Sma3	Biotin/lipoyl attachment	IPR000089	-	-
Sma3	2-oxoacid dehydrogenase acyltransferase, catalytic domain	IPR001078	-	-
Sma3	2-oxo acid dehydrogenase, lipoyl-binding site	IPR003016	-	-
Sma3	E3 binding	IPR004167	-	-
Sma3	Dihydrolipoamide acetyltransferase, long form	IPR006257	-	-
Sma3	EF-Hand 1, calcium-binding site	IPR018247	-	-

Source	Species	ID	Description	e value	Identity
ATG	Arabidoptis thaliana	AT1G54220.1	Dihydrolipoamide acetyltransferase, long form protein chr1:20246460-20250208 REVERSE LENGTH=539	5.0e-36	46%
RefSeq	Arabidopsis thaliana	NP_564654.1	dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex [Arabidopsis thaliana]	7.0e-36	46%
RefSeq	Populus trichocarpa	XP_002303212.1	predicted protein [Populus trichocarpa]	3.0e-37	49%

Full-Lengther Next Prediction

Fln status: Internal

Fln database: coniferopsida.fasta

Fln subject: B8LLY8

Fln msg: Distance to subject end: 42 aas, your sequence is shorter than subject: 152 - 566

Fln protein: SIDMDKAVESRAKLNDISPAKISFNDMVIKAVSIALKQHPAINSSWRGETIRVNHHVNVGVAIAIPDGLVVPVIRFADTKSLSQIATEVKDFAGKAKNKKLQPSDWEGSTFTISNLGMFGIDDFTAILNPPDSCILAVGAIQQVPVVKNGAV

Protein Length: 153

Fln nts: TCTATCGATATGGACAAGGCAGTCGAAAGCCGCGCTAAGCTCAATGATATCAGTCCCGCAAAGATCAGCTTCAACGATATGGTGATCAAGGCTGTATCCATCGCACTCAAACAACATCCAGCCATCAACAGCAGCTGGAGAGGCGAGACCATCCGCGTCAACCACCACGTGAATGTAGGCGTTGCTATCGCGATCCCCGACGGACTCGTAGTCCCGGTCATCCGCTTTGCAGACACCAAGAGCCTTTCGCAGATCGCAACCGAAGTCAAAGATTTCGCCGGCAAGGCCAAGAATAAAAAACTCCAGCCCTCAGATTGGGAAGGCAGCACTTTCACTATCTCTAACCTGGGTATGTTCGGTATCGATGATTTCACTGCTATCCTCAATCCCCCGGACTCCTGCATCCTCGCTGTCGGCGCTATCCAACAGGTACCCGTCGTCAAGAACGGCGCTGTAGT

Fln Alignment:

HLKU4M004IN4NX___MDKAVESRAKLNDISPA----KISFNDMVIKAVSIALKQHPAINSSWRGETIRVNHHVNVGVAIAIPDGLVVPVIRFADTKSLSQIATEVKDFAGKAKNKKLQPSDWEGSTFTISNL-GMFGIDDFTAILNPPDSCILAVGAIQQ
B8LLY8________________VDKLMVLRNQLNALQEASNGKRISVNDFVIKAAASALRKVPQCNSSWTNEYIRQYHNINISVAVQTDKGLFVPVVKDADKKGLSAIGEDVKVLAQKAKENTLKPADYEGGTFTVSNLGGPFGIKQFCAIINPPQSAILAVGSAEK

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Biología Molecular y Biotecnología de Plantas, Facultad de Ciencias y Plataforma Andaluza de Bioinformática, Universidad de Málaga, E-29071 Málaga, Spain