2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial; 2-hexaprenyl-6-methoxy-1,4-benzoquinone methyltransferase; involved in ubiquinone (Coenzyme Q) biosynthesis; localizes to the matrix face of the mitochondrial inner membrane in a large complex with other ubiquinone biosynthetic enzymes; respiratory defect of the null mutant is partially complemented by human COQ5; Belongs to the class I-like SAM-binding methyltransferase superfamily. MenG/UbiE family.

ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication.

Flavin-linked sulfhydryl oxidase of the mitochondrial IMS; N-terminus is an intrinsically disordered domain that in the cytosol helps target Erv1p to mitochondria, and in the intermembrane space oxidizes Mia40p as part of a disulfide relay system that promotes intermembrane space retention of imported proteins; functional ortholog of human GFER (ALR); human GFER carrying N-terminal 21 amino acids of Erv1p functionally complements the lethality of the erv1 null mutation.

10 kDa heat shock protein, mitochondrial; Mitochondrial matrix co-chaperonin; inhibits the ATPase activity of Hsp60p, a mitochondrial chaperonin; involved in protein folding and sorting in the mitochondria; 10 kD heat shock protein with similarity to E. coli groES.

Flavin-linked sulfhydryl oxidase of the mitochondrial IMS; N-terminus is an intrinsically disordered domain that in the cytosol helps target Erv1p to mitochondria, and in the intermembrane space oxidizes Mia40p as part of a disulfide relay system that promotes intermembrane space retention of imported proteins; functional ortholog of human GFER (ALR); human GFER carrying N-terminal 21 amino acids of Erv1p functionally complements the lethality of the erv1 null mutation.

Protein MGR2; Subunit of the TIM23 translocase complex; acts to couple Tim21p with the core Tim23 translocase; provides quality control for insertion of membrane proteins by regulating their release into the inner membrane by the TIM23 complex; absolutely required for mitochondrial import of presequence-containing proteins at elevated temperature; required for viability of cells lacking the mitochondrial genome (petite-negative phenotype); Belongs to the MGR2 family.

Flavin-linked sulfhydryl oxidase of the mitochondrial IMS; N-terminus is an intrinsically disordered domain that in the cytosol helps target Erv1p to mitochondria, and in the intermembrane space oxidizes Mia40p as part of a disulfide relay system that promotes intermembrane space retention of imported proteins; functional ortholog of human GFER (ALR); human GFER carrying N-terminal 21 amino acids of Erv1p functionally complements the lethality of the erv1 null mutation.

Import and assembly protein in mitochondrial intermembrane space; component of MIA pathway which mediates import and oxidative folding of substrates including small proteins containing twin cysteine motifs; acts in concert with Erv1p, which oxidizes the cysteine residues of Mia40p to comprise a disulfide relay system that catalyzes import; also mediates folding of Atp23p via a chaperone-like activity; forms a dimer that binds iron-sulfur cluster in vitro.

Flavin-linked sulfhydryl oxidase of the mitochondrial IMS; N-terminus is an intrinsically disordered domain that in the cytosol helps target Erv1p to mitochondria, and in the intermembrane space oxidizes Mia40p as part of a disulfide relay system that promotes intermembrane space retention of imported proteins; functional ortholog of human GFER (ALR); human GFER carrying N-terminal 21 amino acids of Erv1p functionally complements the lethality of the erv1 null mutation.

Component of the MICOS complex; MICOS (formerly MINOS or MitOS) is a mitochondrial inner membrane complex that extends into the intermembrane space and has a role in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane; Mic60p is also involved in import of intermembrane space (IMS) proteins, probably by positioning Mia40p relative to the TOM complex to receive incoming proteins; ortholog of mammalian mitofilin.

Flavin-linked sulfhydryl oxidase of the mitochondrial IMS; N-terminus is an intrinsically disordered domain that in the cytosol helps target Erv1p to mitochondria, and in the intermembrane space oxidizes Mia40p as part of a disulfide relay system that promotes intermembrane space retention of imported proteins; functional ortholog of human GFER (ALR); human GFER carrying N-terminal 21 amino acids of Erv1p functionally complements the lethality of the erv1 null mutation.

Component of the Sorting and Assembly Machinery (SAM) complex; the SAM (or TOB) complex is located in the mitochondrial outer membrane; the complex binds precursors of beta-barrel proteins and facilitates their outer membrane insertion; homologous to bacterial Omp85.

Flavin-linked sulfhydryl oxidase of the mitochondrial IMS; N-terminus is an intrinsically disordered domain that in the cytosol helps target Erv1p to mitochondria, and in the intermembrane space oxidizes Mia40p as part of a disulfide relay system that promotes intermembrane space retention of imported proteins; functional ortholog of human GFER (ALR); human GFER carrying N-terminal 21 amino acids of Erv1p functionally complements the lethality of the erv1 null mutation.

Heat shock protein SSC1, mitochondrial; Hsp70 family ATPase; constituent of the import motor component of the Translocase of the Inner Mitochondrial membrane (TIM23 complex); involved in protein translocation and folding; subunit of SceI endonuclease; SSC1 has a paralog, ECM10, that arose from the whole genome duplication.

Flavin-linked sulfhydryl oxidase of the mitochondrial IMS; N-terminus is an intrinsically disordered domain that in the cytosol helps target Erv1p to mitochondria, and in the intermembrane space oxidizes Mia40p as part of a disulfide relay system that promotes intermembrane space retention of imported proteins; functional ortholog of human GFER (ALR); human GFER carrying N-terminal 21 amino acids of Erv1p functionally complements the lethality of the erv1 null mutation.

Mitochondrial import inner membrane translocase subunit TIM44; Essential component of the TIM23 complex; tethers the import motor and regulatory factors (PAM complex) to the translocation channel (Tim23p-Tim17p core complex); TIM23 complex is short for the translocase of the inner mitochondrial membrane; Belongs to the Tim44 family.

Flavin-linked sulfhydryl oxidase of the mitochondrial IMS; N-terminus is an intrinsically disordered domain that in the cytosol helps target Erv1p to mitochondria, and in the intermembrane space oxidizes Mia40p as part of a disulfide relay system that promotes intermembrane space retention of imported proteins; functional ortholog of human GFER (ALR); human GFER carrying N-terminal 21 amino acids of Erv1p functionally complements the lethality of the erv1 null mutation.

Mitochondrial import receptor subunit TOM20; Component of the TOM (translocase of outer membrane) complex; responsible for recognition and initial import steps for all mitochondrially directed proteins; acts as a receptor for incoming precursor proteins.

Flavin-linked sulfhydryl oxidase of the mitochondrial IMS; N-terminus is an intrinsically disordered domain that in the cytosol helps target Erv1p to mitochondria, and in the intermembrane space oxidizes Mia40p as part of a disulfide relay system that promotes intermembrane space retention of imported proteins; functional ortholog of human GFER (ALR); human GFER carrying N-terminal 21 amino acids of Erv1p functionally complements the lethality of the erv1 null mutation.

Mitochondrial import receptor subunit TOM22; Component of the TOM (Translocase of Outer Membrane) complex; responsible for initial import of mitochondrially directed proteins; mediates interaction between TOM and TIM complexes and acts as a receptor for precursor proteins; Belongs to the Tom22 family.

Flavin-linked sulfhydryl oxidase of the mitochondrial IMS; N-terminus is an intrinsically disordered domain that in the cytosol helps target Erv1p to mitochondria, and in the intermembrane space oxidizes Mia40p as part of a disulfide relay system that promotes intermembrane space retention of imported proteins; functional ortholog of human GFER (ALR); human GFER carrying N-terminal 21 amino acids of Erv1p functionally complements the lethality of the erv1 null mutation.

Mitochondrial import receptor subunit TOM40; Component of the TOM (translocase of outer membrane) complex; responsible for recognition and initial import steps for all mitochondrially directed proteins; constitutes the core element of the protein conducting pore; pre-Tom40p is phosphorylated by PKA, which impairs its import into mitochondria under non-respiratory conditions.

Flavin-linked sulfhydryl oxidase of the mitochondrial IMS; N-terminus is an intrinsically disordered domain that in the cytosol helps target Erv1p to mitochondria, and in the intermembrane space oxidizes Mia40p as part of a disulfide relay system that promotes intermembrane space retention of imported proteins; functional ortholog of human GFER (ALR); human GFER carrying N-terminal 21 amino acids of Erv1p functionally complements the lethality of the erv1 null mutation.

Mitochondrial import receptor subunit TOM7; Component of the TOM (translocase of outer membrane) complex; responsible for recognition and initial import steps for all mitochondrially directed proteins; promotes assembly and stability of the TOM complex; Belongs to the Tom7 family.

Flavin-linked sulfhydryl oxidase of the mitochondrial IMS; N-terminus is an intrinsically disordered domain that in the cytosol helps target Erv1p to mitochondria, and in the intermembrane space oxidizes Mia40p as part of a disulfide relay system that promotes intermembrane space retention of imported proteins; functional ortholog of human GFER (ALR); human GFER carrying N-terminal 21 amino acids of Erv1p functionally complements the lethality of the erv1 null mutation.

Mitochondrial import receptor subunit TOM70; Component of the TOM (translocase of outer membrane) complex; involved in the recognition and initial import steps for all mitochondrially directed proteins; acts as a receptor for incoming precursor proteins; TOM70 has a paralog, TOM71, that arose from the whole genome duplication.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

10 kDa heat shock protein, mitochondrial; Mitochondrial matrix co-chaperonin; inhibits the ATPase activity of Hsp60p, a mitochondrial chaperonin; involved in protein folding and sorting in the mitochondria; 10 kD heat shock protein with similarity to E. coli groES.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

Component of the Sorting and Assembly Machinery (SAM) complex; the SAM (or TOB) complex is located in the mitochondrial outer membrane; the complex binds precursors of beta-barrel proteins and facilitates their outer membrane insertion; homologous to bacterial Omp85.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

Heat shock protein SSC1, mitochondrial; Hsp70 family ATPase; constituent of the import motor component of the Translocase of the Inner Mitochondrial membrane (TIM23 complex); involved in protein translocation and folding; subunit of SceI endonuclease; SSC1 has a paralog, ECM10, that arose from the whole genome duplication.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

Mitochondrial import receptor subunit TOM20; Component of the TOM (translocase of outer membrane) complex; responsible for recognition and initial import steps for all mitochondrially directed proteins; acts as a receptor for incoming precursor proteins.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

Mitochondrial import receptor subunit TOM22; Component of the TOM (Translocase of Outer Membrane) complex; responsible for initial import of mitochondrially directed proteins; mediates interaction between TOM and TIM complexes and acts as a receptor for precursor proteins; Belongs to the Tom22 family.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

Mitochondrial import receptor subunit TOM40; Component of the TOM (translocase of outer membrane) complex; responsible for recognition and initial import steps for all mitochondrially directed proteins; constitutes the core element of the protein conducting pore; pre-Tom40p is phosphorylated by PKA, which impairs its import into mitochondria under non-respiratory conditions.