Family Search for PF02656 (DUF202)

PF02656 hits 38 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.

YidH / b3676 DUF202 domain-containing inner membrane protein YidH from Escherichia coli K-12 substr. MG1655 (see 3 papers)
Aligns to 13:80 / 115 (59.1%), covers 100.0% of PF02656, 69.8 bits

VTC1_YEAST / P40046 Vacuolar transporter chaperone complex subunit 1; Negative regulator of CDC42 protein 1; Phosphate metabolism protein 4; SPX-dependent polyphosphate polymerase VTC subunit 1; Vacuolar membrane polyphosphate polymerase accessory subunit 1; PolyP polymerase from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 9 papers)
Aligns to 24:86 / 129 (48.8%), covers 98.5% of PF02656, 63.9 bits

• function: Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as a vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation (PubMed:19390046). The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen (PubMed:19390046, PubMed:25315834). PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase (PubMed:25315834). VTC1 contributes only 3 transmembrane domains to the complex (Probable). The VTC complex also plays a role in vacuolar membrane fusion (PubMed:10480897, PubMed:11102525, PubMed:11823419, PubMed:12584253). Required for SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0) trans-complex formation (PubMed:11823419).
  subunit: The VTC core complex is an integral membrane heterooligomer composed of the catalytic subunit VTC4 and the accessory subunits VTC1, VTC2 and VTC3. The complex exists in 2 different sub-complexes: VTC1- VTC2-VCT4 and VCT1-VTC3-VTC4. The VCT1-VTC3-VTC4 subcomplex is mostly found on the vacuolar membrane. The VTC1-VTC2-VCT4 subcomplex is observed in the cell periphery, probably ER and nuclear envelope, but localizes to the vacuole under phosphate starvation. Each subunit contains 3 transmembrane helices. VTC1 is a small membrane protein without hydrophilic domain. VTC2, VTC3 and VTC4 are related and have 2 hydrophilic domains that face the cytosol, an N-terminal SPX domain and the central core domain. The central core in VTC4 is the catalytic domain, with the essential catalytic lysine replaced by isoleucine and leucine in VTC2 and VTC3, respectively (PubMed:19390046). The core complex associates with the accessory subunit VTC5 (PubMed:27587415). The complex interacts with the v-SNARE NYV1 and with the V(0) subunit of V-ATPase VPH1 (PubMed:11823419).

VTC1_SCHPO / Q9UR17 Vacuolar transporter chaperone complex subunit 1; Negative regulator of cdc42; SPX-dependent polyphosphate polymerase VTC subunit 1; Vacuolar membrane polyphosphate polymerase accessory subunit 1; PolyP polymerase from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
Aligns to 24:86 / 122 (51.6%), covers 98.5% of PF02656, 61.5 bits

• function: Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as a vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation. The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen. PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase. Vtc1 contributes only 3 transmembrane domains to the complex. The VTC complex also plays a role in vacuolar membrane fusion (By similarity). Involved in the control of cell polarity (PubMed:10628977).
  subunit: The VTC core complex is an integral membrane heterooligomer composed of at least the catalytic subunit vtc4 and the accessory subunits vtc1 and vtc2. vtc1 is a small membrane protein without hydrophilic domain. Vtc2 and vtc4 are related and have 2 hydrophilic domains that face the cytosol, an N-terminal SPX domain and the central core domain. The central core in vtc4 is the catalytic domain (By similarity). Vtc1 interacts with GTP-bound Ras-like cdc42, which is subsequently inactivated (PubMed:10628977).
  disruption phenotype: Defects in endocytosis.

VTC1_TRYB2 / Q57UM0 Vacuolar transporter chaperone complex subunit 1; SPX-dependent polyphosphate polymerase VTC subunit 1; Vacuolar membrane polyphosphate polymerase accessory subunit 1; PolyP polymerase from Trypanosoma brucei brucei (strain 927/4 GUTat10.1) (see paper)
Aligns to 62:127 / 180 (36.7%), covers 97.1% of PF02656, 60.0 bits

• function: Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as a vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation. The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen. PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase. VTC1 contributes only 3 transmembrane domains to the complex. The VTC complex also plays a role in vacuolar membrane fusion.
  subunit: The VTC core complex is an integral membrane heterooligomer composed of at least the catalytic subunit vtc4 and the accessory subunits vtc1 and vtc2. vtc1 is a small membrane protein without hydrophilic domain. Vtc2 and vtc4 are related and have 2 hydrophilic domains that face the cytosol, an N-terminal SPX domain and the central core domain. The central core in vtc4 is the catalytic domain.
  disruption phenotype: Causes an abnormal morphology of acidocalcisomes, a significant decrease in the amount of polyP and a deficient response to hyposmotic stress.

VTC2_TOXGM / A0A125YS36 Vacuolar transporter chaperone complex subunit 2; SPX-dependent polyphosphate polymerase VTC subunit 2; Vacuolar membrane polyphosphate polymerase accessory subunit 2; PolyP polymerase from Toxoplasma gondii (strain ATCC 50611 / Me49) (see paper)
Aligns to 1075:1137 / 1308 (4.8%), covers 100.0% of PF02656, 56.8 bits

• function: Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as a vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation. The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen. PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase. The VTC complex also plays a role in vacuolar membrane fusion.
  subunit: The VTC core complex is an integral membrane heterooligomer composed of at least the catalytic subunit vtc4 and the accessory subunits vtc1 and vtc2. vtc1 is a small membrane protein without hydrophilic domain. Vtc2 and vtc4 are related and have 2 hydrophilic domains that face the cytosol, an N-terminal SPX domain and the central core domain. The central core in vtc4 is the catalytic domain.
  disruption phenotype: The VTC2 locus is refractory to knockout, and may be essential. Partial disruption of the gene results in reduced polyP accumulation.

VTC2_YEAST / P43585 Vacuolar transporter chaperone complex subunit 2; Phosphate metabolism protein 1; SPX-dependent polyphosphate polymerase VTC subunit 2; Vacuolar membrane polyphosphate polymerase accessory subunit 2; PolyP polymerase from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 9 papers)
Aligns to 686:752 / 828 (8.1%), covers 97.1% of PF02656, 51.5 bits

• function: Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as a vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation (PubMed:19390046). The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen (PubMed:19390046, PubMed:25315834). PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase (PubMed:25315834). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules (PubMed:27080106). Inositol polyphosphate binding promotes vacuolar polyphosphate synthesis (PubMed:27080106). The VTC complex also plays a role in vacuolar membrane fusion (PubMed:11102525, PubMed:11823419). Required for SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0) trans-complex formation (PubMed:11823419).
  subunit: The VTC core complex is an integral membrane heterooligomer composed of the catalytic subunit VTC4 and the accessory subunits VTC1, VTC2 and VTC3. The complex exists in 2 different sub-complexes: VTC1- VTC2-VCT4 and VCT1-VTC3-VTC4. The VCT1-VTC3-VTC4 subcomplex is mostly found on the vacuolar membrane. The VTC1-VTC2-VCT4 subcomplex is observed in the cell periphery, probably ER and nuclear envelope, but localizes to the vacuole under phosphate starvation. Each subunit contains 3 transmembrane helices. VTC1 is a small membrane protein without hydrophilic domain. VTC2, VTC3 and VTC4 are related and have 2 hydrophilic domains that face the cytosol, an N-terminal SPX domain and the central core domain. The central core in VTC4 is the catalytic domain, with the essential catalytic lysine replaced by isoleucine and leucine in VTC2 and VTC3, respectively (PubMed:19390046). The core complex associates with the accessory subunit VTC5 (PubMed:27587415). The complex interacts with the v-SNARE NYV1 and with the V(0) subunit of V-ATPase VPH1 (PubMed:11823419).

VTC3_YEAST / Q02725 Vacuolar transporter chaperone 3 complex subunit 3; Phosphate metabolism protein 2; SPX-dependent polyphosphate polymerase VTC subunit 3; Vacuolar membrane polyphosphate polymerase accessory subunit 3; PolyP polymerase from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 9 papers)
Aligns to 698:765 / 835 (8.1%), covers 97.1% of PF02656, 51.4 bits

• function: Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as a vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation (PubMed:19390046). The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen (PubMed:19390046, PubMed:25315834). PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase (PubMed:25315834). The VTC complex also plays a role in vacuolar membrane fusion (PubMed:11102525, PubMed:11823419). Required for SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0) trans-complex formation (PubMed:11823419). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules. Inositol polyphosphate binding promotes vacuolar polyphosphate synthesis (PubMed:27080106).
  subunit: The VTC core complex is an integral membrane heterooligomer composed of the catalytic subunit VTC4 and the accessory subunits VTC1, VTC2 and VTC3. The complex exists in 2 different sub-complexes: VTC1- VTC2-VCT4 and VCT1-VTC3-VTC4. The VCT1-VTC3-VTC4 subcomplex is mostly found on the vacuolar membrane. The VTC1-VTC2-VCT4 subcomplex is observed in the cell periphery, probably ER and nuclear envelope, but localizes to the vacuole under phosphate starvation. Each subunit contains 3 transmembrane helices. VTC1 is a small membrane protein without hydrophilic domain. VTC2, VTC3 and VTC4 are related and have 2 hydrophilic domains that face the cytosol, an N-terminal SPX domain and the central core domain. The central core in VTC4 is the catalytic domain, with the essential catalytic lysine replaced by isoleucine and leucine in VTC2 and VTC3, respectively (PubMed:19390046). The core complex associates with the accessory subunit VTC5 (PubMed:27587415). The complex interacts with the v-SNARE NYV1 and with the V(0) subunit of V-ATPase VPH1 (PubMed:11823419).

YidG / b3675 inner membrane protein YidG from Escherichia coli K-12 substr. MG1655 (see 2 papers)
Aligns to 12:74 / 120 (52.5%), covers 83.8% of PF02656, 46.0 bits

VTC4_YEAST / P47075 Vacuolar transporter chaperone complex subunit 4; Phosphate metabolism protein 3; Polyphosphate kinase; SPX-dependent polyphosphate polymerase VTC subunit 4; Vacuolar membrane polyphosphate polymerase catalytic subunit; PolyP polymerase; EC 2.7.4.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 12 papers)
Aligns to 622:684 / 721 (8.7%), covers 97.1% of PF02656, 45.0 bits

• function: Catalytic subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as a vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation (PubMed:19390046). The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen (PubMed:19390046, PubMed:25315834). PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase (PubMed:25315834). The VTC complex also plays a role in vacuolar membrane fusion (PubMed:11102525, PubMed:11823419, PubMed:12584253). Required for SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0) trans-complex formation (PubMed:11823419). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules. Inositol polyphosphate binding promotes vacuolar polyphosphate synthesis (PubMed:27080106). The VTC complex is required for microautophagy. It is a constituent of autophagic tubes and is required for scission of microautophagic vesicles from these tubes (PubMed:17079729).
  catalytic activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP (RHEA:19573)
  cofactor: Mn(2+)
  subunit: The VTC core complex is an integral membrane heterooligomer composed of the catalytic subunit VTC4 and the accessory subunits VTC1, VTC2 and VTC3. The complex exists in 2 different sub-complexes: VTC1- VTC2-VCT4 and VCT1-VTC3-VTC4. The VCT1-VTC3-VTC4 subcomplex is mostly found on the vacuolar membrane. The VTC1-VTC2-VCT4 subcomplex is observed in the cell periphery, probably ER and nuclear envelope, but localizes to the vacuole under phosphate starvation. Each subunit contains 3 transmembrane helices. VTC1 is a small membrane protein without hydrophilic domain. VTC2, VTC3 and VTC4 are related and have 2 hydrophilic domains that face the cytosol, an N-terminal SPX domain and the central core domain. The central core in VTC4 is the catalytic domain, with the essential catalytic lysine replaced by isoleucine and leucine in VTC2 and VTC3, respectively (PubMed:19390046). The core complex associates with the accessory subunit VTC5 (PubMed:27587415). The complex interacts with the v-SNARE NYV1 and with the V(0) subunit of V-ATPase VPH1 (PubMed:11823419).
  disruption phenotype: Leads to a decrease in intracellular arginine, consistent with a role for polyP in vacuolar arginine storage.

VTC4_TRYCC / Q4E409 Vacuolar transporter chaperone complex subunit 4; Polyphosphate kinase; SPX-dependent polyphosphate polymerase VTC subunit 4; Vacuolar membrane polyphosphate polymerase catalytic subunit; PolyP polymerase; EC 2.7.4.1 from Trypanosoma cruzi (strain CL Brener) (see paper)
Aligns to 674:753 / 801 (10.0%), covers 97.1% of PF02656, 24.2 bits

• function: Component of a polyphosphate synthase complex that utilizes ATP to synthesize and translocate polyphosphate to acidocalcisomes in epimastigotes, insect-stages of Trypanosoma brucei (PubMed:24386955). Catalytic subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as a vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation. The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen. PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase. The VTC complex also plays a role in vacuolar membrane fusion (By similarity). Essential for infection and parasite survival in the mammalian host (By similarity).
  catalytic activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP (RHEA:19573)
  cofactor: Mn(2+)
  subunit: The VTC core complex is an integral membrane heterooligomer composed of at least the catalytic subunit vtc4 and the accessory subunits vtc1 and vtc2. vtc1 is a small membrane protein without hydrophilic domain. Vtc2 and vtc4 are related and have 2 hydrophilic domains that face the cytosol, an N-terminal SPX domain and the central core domain. The central core in vtc4 is the catalytic domain.
  disruption phenotype: Results in growth defects in procyclic forms (PCF) and changes in acidocalcisome morphology and number. The mean number of acidocalcisomes drops by approximately 2-fold, but individual acidocalcisomes are considerably larger and less circular. Also affects cellular polyP and PPi content. Short chain polyP drops almost 2-fold, while PPi nearly doubles.

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