Bax inhibitor-1/YccA family protein similar to Escherichia coli YccA, which negatively regulates the FtsH protease and is degraded by in an FtsH-dependent manner
YccA-like proteins; A prokaryotic member of the BAX inhibitor (BI)-1 like family of small ...
16-219
3.76e-78
YccA-like proteins; A prokaryotic member of the BAX inhibitor (BI)-1 like family of small transmembrane proteins, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.
:
Pssm-ID: 198415 Cd Length: 205 Bit Score: 233.25 E-value: 3.76e-78
YccA-like proteins; A prokaryotic member of the BAX inhibitor (BI)-1 like family of small ...
16-219
3.76e-78
YccA-like proteins; A prokaryotic member of the BAX inhibitor (BI)-1 like family of small transmembrane proteins, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.
Pssm-ID: 198415 Cd Length: 205 Bit Score: 233.25 E-value: 3.76e-78
Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family ...
19-214
6.54e-31
Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family proteins, some of which inhibit apoptosis (Bcl-2 and Bcl-XL) and some of which promote it (Bax and Bak). Human Bax inhibitor, BI-1, is an evolutionarily conserved integral membrane protein containing multiple membrane-spanning segments predominantly localized to intracellular membranes. It has 6-7 membrane-spanning domains. The C termini of the mammalian BI-1 proteins are comprised of basic amino acids resembling some nuclear targeting sequences, but otherwise the predicted proteins lack motifs that suggest a function. As plant BI-1 appears to localize predominantly to the ER, we hypothesized that plant BI-1 could also regulate cell death triggered by ER stress. BI-1 appears to exert its effect through an interaction with calmodulin. The budding yeast member of this family has been found unexpectedly to encode a BH3 domain-containing protein (Ybh3p) that regulates the mitochondrial pathway of apoptosis in a phylogenetically conserved manner. Examination of the crystal structure of a bacterial member of this family shows that these proteins mediate a calcium leak across the membrane that is pH-dependent. Calcium homoeostasis balances passive calcium leak with active calcium uptake. The structure exists in a pore-closed and pore-open conformation, at pHs of 8 and 6 respectively, and the pore can be opened by intracrystalline transition; together these findings suggest that pH controls the conformational transition.
Pssm-ID: 460029 Cd Length: 207 Bit Score: 112.65 E-value: 6.54e-31
YccA-like proteins; A prokaryotic member of the BAX inhibitor (BI)-1 like family of small ...
16-219
3.76e-78
YccA-like proteins; A prokaryotic member of the BAX inhibitor (BI)-1 like family of small transmembrane proteins, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.
Pssm-ID: 198415 Cd Length: 205 Bit Score: 233.25 E-value: 3.76e-78
BAX inhibitor (BI)-1/YccA-like protein family; Mammalian members of the BAX inhibitor (BI)-1 ...
18-215
1.54e-32
BAX inhibitor (BI)-1/YccA-like protein family; Mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. Their broad tissue distribution and high degree of conservation suggests an important regulatory role. This superfamily also contains the lifeguard(LFG)-like proteins and other subfamilies which appear to be related by common descent and also function as inhibitors of apoptosis. In plants, BI-1 like proteins play a role in pathogen resistance. A prokaryotic member, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.
Pssm-ID: 198409 Cd Length: 202 Bit Score: 116.74 E-value: 1.54e-32
Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family ...
19-214
6.54e-31
Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family proteins, some of which inhibit apoptosis (Bcl-2 and Bcl-XL) and some of which promote it (Bax and Bak). Human Bax inhibitor, BI-1, is an evolutionarily conserved integral membrane protein containing multiple membrane-spanning segments predominantly localized to intracellular membranes. It has 6-7 membrane-spanning domains. The C termini of the mammalian BI-1 proteins are comprised of basic amino acids resembling some nuclear targeting sequences, but otherwise the predicted proteins lack motifs that suggest a function. As plant BI-1 appears to localize predominantly to the ER, we hypothesized that plant BI-1 could also regulate cell death triggered by ER stress. BI-1 appears to exert its effect through an interaction with calmodulin. The budding yeast member of this family has been found unexpectedly to encode a BH3 domain-containing protein (Ybh3p) that regulates the mitochondrial pathway of apoptosis in a phylogenetically conserved manner. Examination of the crystal structure of a bacterial member of this family shows that these proteins mediate a calcium leak across the membrane that is pH-dependent. Calcium homoeostasis balances passive calcium leak with active calcium uptake. The structure exists in a pore-closed and pore-open conformation, at pHs of 8 and 6 respectively, and the pore can be opened by intracrystalline transition; together these findings suggest that pH controls the conformational transition.
Pssm-ID: 460029 Cd Length: 207 Bit Score: 112.65 E-value: 6.54e-31
Bacterial BAX inhibitor (BI)-1/YccA-like proteins; This family is comprised of bacterial ...
17-215
1.36e-29
Bacterial BAX inhibitor (BI)-1/YccA-like proteins; This family is comprised of bacterial relatives of the mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. In plants, BI-1 like proteins play a role in pathogen resistance. A characterized prokaryotic member, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.
Pssm-ID: 198414 Cd Length: 211 Bit Score: 109.19 E-value: 1.36e-29
Golgi antiapoptotic protein; GAAP (or transmembrane BAX inhibitor motif containing 4) is a ...
22-217
6.16e-19
Golgi antiapoptotic protein; GAAP (or transmembrane BAX inhibitor motif containing 4) is a regulator of apoptosis that is related to the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. Human GAAP has been linked to the modulation of intracellular fluxes of Ca(2+), by suppressing influx from the extracellular medium and reducing release from intracellular stores. A viral homolog (vaccinia virus vGAAP) acts similar to its human counterpart in inhibiting apoptosis.
Pssm-ID: 198411 Cd Length: 233 Bit Score: 81.88 E-value: 6.16e-19
BAX inhibitor (BI)-1; Mammalian members of the BAX inhibitor (BI)-1 like family of small ...
18-214
4.05e-12
BAX inhibitor (BI)-1; Mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. Their broad tissue distribution and high degree of conservation suggests an important regulatory role. In plants, BI-1 like proteins play a role in pathogen resistance.
Pssm-ID: 198412 Cd Length: 213 Bit Score: 63.01 E-value: 4.05e-12
Proteins similar to and including lifeguard (LFG), a putative regulator of apoptosis; ...
77-215
3.72e-10
Proteins similar to and including lifeguard (LFG), a putative regulator of apoptosis; Lifeguard (LFG) inhibits Fas-mediated apoptosis and interacts with the death receptor FasR/CD95/Apo1. LFG has been shown to interact with Bax and is supposed to be integral to cellular membranes such as the ER. A close homolog, PP1201 or RECS1, appears located in the Golgi compartment and also interacts with the Fas receptor CD95/Apo1. PP1201 is expressed in response to shear stress.
Pssm-ID: 198410 Cd Length: 217 Bit Score: 57.55 E-value: 3.72e-10
Growth-hormone inducible transmembrane protein; GHITM appears to be ubiquitiously expressed in ...
82-219
3.62e-05
Growth-hormone inducible transmembrane protein; GHITM appears to be ubiquitiously expressed in mammalian cells and expression has also been observed in various cancer cell lines. A cytoprotective function has been suggested. It is closely related to the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect.
Pssm-ID: 198413 Cd Length: 264 Bit Score: 43.52 E-value: 3.62e-05
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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