RvY_16911-1 protein (Ramazzottius varieornatus)

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RvY_16911-1

Post-GPI attachment to proteins factor 3; Involved in the lipid remodeling steps of GPI-anchor maturation; Belongs to the PGAP3 family. (121 aa)

Predicted Functional Partners:

RvY_09732-1

0.629

RvY_04543-1

0.525

RvY_12745-1

0.486

RvY_02987-1

0.444

RvY_07686

0.439

RvY_07686-1

0.439

RvY_09053-1

0.435

RvY_13791-1

0.435

RvY_05478-1

0.412

Your Current Organism:

Ramazzottius varieornatus

NCBI taxonomy Id: 947166
Other names: R. varieornatus

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
RvY_02987-1	RvY_04543-1	A0A1D1ULH9	A0A1D1URY5	GPI-anchor transamidase; Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein. Belongs to the peptidase C13 family.	Metallophos domain-containing protein.	0.554
RvY_02987-1	RvY_07686	A0A1D1ULH9	A0A1D1V336	GPI-anchor transamidase; Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein. Belongs to the peptidase C13 family.	Uncharacterized protein.	0.885
RvY_02987-1	RvY_07686-1	A0A1D1ULH9	A0A1D1VCI9	GPI-anchor transamidase; Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein. Belongs to the peptidase C13 family.	Uncharacterized protein.	0.885
RvY_02987-1	RvY_09732-1	A0A1D1ULH9	A0A1D1VJD8	GPI-anchor transamidase; Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein. Belongs to the peptidase C13 family.	Uncharacterized protein.	0.554
RvY_02987-1	RvY_12745-1	A0A1D1ULH9	A0A1D1VT56	GPI-anchor transamidase; Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein. Belongs to the peptidase C13 family.	Metallophos domain-containing protein.	0.434
RvY_02987-1	RvY_16911-1	A0A1D1ULH9	A0A1D1W165	GPI-anchor transamidase; Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein. Belongs to the peptidase C13 family.	Post-GPI attachment to proteins factor 3; Involved in the lipid remodeling steps of GPI-anchor maturation; Belongs to the PGAP3 family.	0.444
RvY_04543-1	RvY_02987-1	A0A1D1URY5	A0A1D1ULH9	Metallophos domain-containing protein.	GPI-anchor transamidase; Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein. Belongs to the peptidase C13 family.	0.554
RvY_04543-1	RvY_07686	A0A1D1URY5	A0A1D1V336	Metallophos domain-containing protein.	Uncharacterized protein.	0.441
RvY_04543-1	RvY_07686-1	A0A1D1URY5	A0A1D1VCI9	Metallophos domain-containing protein.	Uncharacterized protein.	0.441
RvY_04543-1	RvY_09732-1	A0A1D1URY5	A0A1D1VJD8	Metallophos domain-containing protein.	Uncharacterized protein.	0.600
RvY_04543-1	RvY_16911-1	A0A1D1URY5	A0A1D1W165	Metallophos domain-containing protein.	Post-GPI attachment to proteins factor 3; Involved in the lipid remodeling steps of GPI-anchor maturation; Belongs to the PGAP3 family.	0.525
RvY_05478-1	RvY_16911-1	A0A1D1V0R4	A0A1D1W165	Uncharacterized protein.	Post-GPI attachment to proteins factor 3; Involved in the lipid remodeling steps of GPI-anchor maturation; Belongs to the PGAP3 family.	0.412
RvY_07686	RvY_02987-1	A0A1D1V336	A0A1D1ULH9	Uncharacterized protein.	GPI-anchor transamidase; Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein. Belongs to the peptidase C13 family.	0.885
RvY_07686	RvY_04543-1	A0A1D1V336	A0A1D1URY5	Uncharacterized protein.	Metallophos domain-containing protein.	0.441
RvY_07686	RvY_16911-1	A0A1D1V336	A0A1D1W165	Uncharacterized protein.	Post-GPI attachment to proteins factor 3; Involved in the lipid remodeling steps of GPI-anchor maturation; Belongs to the PGAP3 family.	0.439
RvY_07686-1	RvY_02987-1	A0A1D1VCI9	A0A1D1ULH9	Uncharacterized protein.	GPI-anchor transamidase; Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein. Belongs to the peptidase C13 family.	0.885
RvY_07686-1	RvY_04543-1	A0A1D1VCI9	A0A1D1URY5	Uncharacterized protein.	Metallophos domain-containing protein.	0.441
RvY_07686-1	RvY_16911-1	A0A1D1VCI9	A0A1D1W165	Uncharacterized protein.	Post-GPI attachment to proteins factor 3; Involved in the lipid remodeling steps of GPI-anchor maturation; Belongs to the PGAP3 family.	0.439
RvY_09053-1	RvY_13791-1	A0A1D1VCL4	A0A1D1VR91	Uncharacterized protein.	Uncharacterized protein.	0.554
RvY_09053-1	RvY_16911-1	A0A1D1VCL4	A0A1D1W165	Uncharacterized protein.	Post-GPI attachment to proteins factor 3; Involved in the lipid remodeling steps of GPI-anchor maturation; Belongs to the PGAP3 family.	0.435