SustainPineDB

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Assembly info
Unigenes
SNPs
SSRs
Descriptions
GOs
ECs
KEGGs
InterPros
miRNAs

Assembly Name: biogeco3 v1.0

UniGene Name: biog3_v1.0_unigene23251

Length: 347 nt

UniGene Fasta

>biog3_v1.0_unigene23251
AATGTATGGATAGGATGCGGCGACAAGCAGAACGATGGGGTGCTGAACTGTTCCAAGAAGATGTAGAGCATGTTGATCTGAAGAACAGGCCTTTACAATCCGAAGCAGTGAGCGTGAGGTCAAGTGTCACAGTTTAATAGTAGCAACAGGAGCCACAGTCAGAAGGTTAGGGTTTCCTCGTGAAAAAGAATTTTGGAGCAGAGGAATAAGTGCCTGTGCAATTTGTGATGGTGCATCCCCTTTATTTAAAGGTCAAGAGCTCGCAGTTGTTGGAGGTGGTGACACAGCCACAGAAGAAGCAGTATACCTCACTAAATATGCCCGACATGTACATTTGTTAGTACATT

Ace file of the UniGene biog3_v1.0_unigene23251

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Annotations

Parent Assembly	Parent UniGene	Reads (related/total)
SustainPine v2.0	sp_v2.0_unigene3147	1/2
SustainPine v2.0	sp_v2.0_unigene58302	1/2

Source	Descriptions	Term	Type	Identity
AutoFact	Thioredoxin reductase n=1 Tax=Picea sitchensis RepID=B8LPW6_PICSI	-	-	90%
FL-Next	sp=Thioredoxin reductase; Picea sitchensis (Sitka spruce) (Pinus sitchensis).	-	-	100%
Blast2go	nadph-dependent thioredoxin reductase 3-like	-	-	89%

Source	ECs	Term	Type	e value	Identity
Blast2go	Oxidoreductases, Acting on a sulfur group of donors, With a disulfide as acceptor.	EC:1.8.4.-	-	0.0	89%
Blast2go	Thioredoxin-disulfide reductase.	EC:1.8.1.9	-	0.0	89%

Source	KEGGs	Term	Type	e value	Identity
Blast2go	Pyrimidine metabolism	00240		0.0	89%
Blast2go	Selenocompound metabolism	00450		0.0	89%

Source	GOs	Term	Type	Identity
Blast2go	hydrogen peroxide catabolic process	GO:0042744	Biological Process	89%
Blast2go	oxidation-reduction process	GO:0055114	Biological Process	89%
Blast2go	cell redox homeostasis	GO:0045454	Biological Process	89%
Blast2go	regulation of chlorophyll biosynthetic process	GO:0010380	Biological Process	89%
Blast2go	regulation of starch biosynthetic process	GO:0010581	Biological Process	89%
Blast2go	removal of superoxide radicals	GO:0019430	Biological Process	89%
Blast2go	positive regulation of catalytic activity	GO:0043085	Biological Process	89%
Blast2go	enzyme activator activity	GO:0008047	Molecular Function	89%
Blast2go	oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor	GO:0016671	Molecular Function	89%
Blast2go	protein binding	GO:0005515	Molecular Function	89%
Blast2go	flavin adenine dinucleotide binding	GO:0050660	Molecular Function	89%
Blast2go	thioredoxin-disulfide reductase activity	GO:0004791	Molecular Function	89%
Blast2go	chloroplast stroma	GO:0009570	Cellular Component	89%

Source	InterPros	Term	Type	Identity
Sma3	Pyridine nucleotide-disulphide oxidoreductase, class-II	IPR000103	-	-
Sma3	Pyridine nucleotide-disulphide oxidoreductase, NAD-binding domain	IPR001327	-	-
Sma3	Thioredoxin reductase	IPR005982	-	-
Sma3	Pyridine nucleotide-disulphide oxidoreductase, class-II, active site	IPR008255	-	-
Sma3		IPR012335	-	-
Sma3	FAD-dependent pyridine nucleotide-disulphide oxidoreductase	IPR013027	-	-
Sma3	Thioredoxin domain	IPR013766	-	-
Sma3	NAD(P)-binding domain	IPR016040	-	-
Sma3		IPR017909	-	-
Sma3		IPR017936	-	-
Sma3	Thioredoxin, conserved site	IPR017937	-	-

Full-Lengther Next Prediction

Fln status: Internal

Fln database: coniferopsida.fasta

Fln subject: B8LPW6

Fln msg: Overlapping hits, possible frame ERROR between 92 and 80, Distance to subject end: 269 aas, your sequence is shorter than subject: 115 - 562

Fln protein: CMDRMRRQAERWGAELFQEDVEHVDxxxxxxTIRSSEREVKCHSLIVATGATVRRLGFPREKEFWSRGISACAICDGASPLFKGQELAVVGGGDTATEEAVYLTKYARHVHLLVH

Protein Length: 116

Fln nts: AATGTATGGATAGGATGCGGCGACAAGCAGAACGATGGGGTGCTGAACTGTTCCAAGAAGATGTAGAGCATGTTGATxxxxxxxxxxxxxxxxxxACAATCCGAAGCAGTGAGCGTGAGGTCAAGTGTCACAGTTTAATAGTAGCAACAGGAGCCACAGTCAGAAGGTTAGGGTTTCCTCGTGAAAAAGAATTTTGGAGCAGAGGAATAAGTGCCTGTGCAATTTGTGATGGTGCATCCCCTTTATTTAAAGGTCAAGAGCTCGCAGTTGTTGGAGGTGGTGACACAGCCACAGAAGAAGCAGTATACCTCACTAAATATGCCCGACATGTACATTTGTTAGTACATT

Fln Alignment:

biogeco3_mira_c22347___MDRMRRQAERWGAELFQEDVEHVDLxxxxFTIRSSEREVKCHSLIVATGATVRRLGFPREKEFWSRGISACAICDGASPLFKGQELAVVGGGDTATEEAVYLTKYARHVHLLV
B8LPW6__________________MDRMRRQAERWGAELFQEDVEHVDLxxxxFTIRSSDREVKCHSLIVATGATARRLGFPREKEFWSRGISACAICDGASPLFKGQELAVVGGGDTATEEAIYLTKYARHVHLLV

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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