D8QS56_SELML protein (Selaginella moellendorffii)

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D8QS56_SELML

Lactamase_B domain-containing protein. (283 aa)

Predicted Functional Partners:

LIP1

0.644

D8SRD1_SELML

0.644

LIP1P

0.644

LIP1P-2

0.644

D8RBS5_SELML

0.595

D8RXV4_SELML

0.595

D8S6F6_SELML

0.595

Your Current Organism:

Selaginella moellendorffii

NCBI taxonomy Id: 88036
Other names: S. moellendorffii, Selaginella moellendorffii Hieron., Selaginella moellendorfii

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
D8QS56_SELML	D8RBS5_SELML	D8QS56	D8RBS5	Lactamase_B domain-containing protein.	BPL/LPL catalytic domain-containing protein.	0.595
D8QS56_SELML	D8RXV4_SELML	D8QS56	D8RXV4	Lactamase_B domain-containing protein.	BPL/LPL catalytic domain-containing protein.	0.595
D8QS56_SELML	D8S6F6_SELML	D8QS56	D8S6F6	Lactamase_B domain-containing protein.	Uncharacterized protein.	0.595
D8QS56_SELML	D8SRD1_SELML	D8QS56	D8SRD1	Lactamase_B domain-containing protein.	Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.644
D8QS56_SELML	LIP1	D8QS56	D8SNA7	Lactamase_B domain-containing protein.	Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.644
D8QS56_SELML	LIP1P	D8QS56	D8T3Q2	Lactamase_B domain-containing protein.	Lipoyl synthase, chloroplastic; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.644
D8QS56_SELML	LIP1P-2	D8QS56	D8TA61	Lactamase_B domain-containing protein.	Lipoyl synthase, chloroplastic; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.644
D8RBS5_SELML	D8QS56_SELML	D8RBS5	D8QS56	BPL/LPL catalytic domain-containing protein.	Lactamase_B domain-containing protein.	0.595
D8RBS5_SELML	D8SRD1_SELML	D8RBS5	D8SRD1	BPL/LPL catalytic domain-containing protein.	Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.795
D8RBS5_SELML	LIP1	D8RBS5	D8SNA7	BPL/LPL catalytic domain-containing protein.	Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.795
D8RBS5_SELML	LIP1P	D8RBS5	D8T3Q2	BPL/LPL catalytic domain-containing protein.	Lipoyl synthase, chloroplastic; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.795
D8RBS5_SELML	LIP1P-2	D8RBS5	D8TA61	BPL/LPL catalytic domain-containing protein.	Lipoyl synthase, chloroplastic; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.795
D8RXV4_SELML	D8QS56_SELML	D8RXV4	D8QS56	BPL/LPL catalytic domain-containing protein.	Lactamase_B domain-containing protein.	0.595
D8RXV4_SELML	D8SRD1_SELML	D8RXV4	D8SRD1	BPL/LPL catalytic domain-containing protein.	Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.795
D8RXV4_SELML	LIP1	D8RXV4	D8SNA7	BPL/LPL catalytic domain-containing protein.	Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.795
D8RXV4_SELML	LIP1P	D8RXV4	D8T3Q2	BPL/LPL catalytic domain-containing protein.	Lipoyl synthase, chloroplastic; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.795
D8RXV4_SELML	LIP1P-2	D8RXV4	D8TA61	BPL/LPL catalytic domain-containing protein.	Lipoyl synthase, chloroplastic; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.795
D8S6F6_SELML	D8QS56_SELML	D8S6F6	D8QS56	Uncharacterized protein.	Lactamase_B domain-containing protein.	0.595
D8S6F6_SELML	D8SRD1_SELML	D8S6F6	D8SRD1	Uncharacterized protein.	Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.795
D8S6F6_SELML	LIP1	D8S6F6	D8SNA7	Uncharacterized protein.	Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.795