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Conserved domains on  [gi|322510100|sp|Q9HC24|]
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RecName: Full=Protein lifeguard 4; AltName: Full=Golgi anti-apoptotic protein; AltName: Full=Protein S1R; AltName: Full=Transmembrane BAX inhibitor motif-containing protein 4; AltName: Full=Z-protein

Protein Classification

Bax inhibitor-1 family protein( domain architecture ID 10179630)

Bax inhibitor-1 family protein similar to protein lifeguard 4 (LFG4/GAAP) which can inhibit apoptosis induced by intrinsic and extrinsic apoptotic stimuli and to yeast Bax inhibitor Bxi1p which links the unfolded protein response and programmed cell death and mediates mitochondrial-dependent apoptosis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GAAP_like cd10429
Golgi antiapoptotic protein; GAAP (or transmembrane BAX inhibitor motif containing 4) is a ...
 6-236 3.13e-100

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: 291.04  E-value: 3.13e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100   6 PRYPRSSIEDDFNYGSSVASATVHIRMAFLRKVYSILSLQVLLTTVTSTVFLYFESVRTFVHESPALILLFALGSLGLIF 85
Cdd:cd10429    2 SRYAEADIPDDFKYGTNVASAEPEIRMAFLRKVYSILSVQLLATTAVSALFYLSPSIKTFVQSHPWLFLISLIGSLILLI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  86 ALILNRHKYPLNLYLLFGFTLLEALTVAVVVTFYDVYIILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILC- 164
Cdd:cd10429   82 ALYWKRHSHPVNLILLSLFTLCEAYTVGLVVSFYDGKIVLQALILTLGVFVGLTAYTFQTKRDFSSFGALLFILLWALIl 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 322510100 165 LSGFLKFFFYSEIMELVLAAAGALLFCGFIIYDTHSLMHKLSPEEYVLAAISLYLDIINLFLHLLRFLEAVN 236
Cdd:cd10429  162 LALIFQFFPYSPTFELVYAGLGALLFSGYIVYDTQLIMKRLSPDEYILAAISLYLDIINLFLSILRILAAMN 233
 
Name Accession Description Interval E-value
GAAP_like cd10429
Golgi antiapoptotic protein; GAAP (or transmembrane BAX inhibitor motif containing 4) is a ...
 6-236 3.13e-100

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: 291.04  E-value: 3.13e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100   6 PRYPRSSIEDDFNYGSSVASATVHIRMAFLRKVYSILSLQVLLTTVTSTVFLYFESVRTFVHESPALILLFALGSLGLIF 85
Cdd:cd10429    2 SRYAEADIPDDFKYGTNVASAEPEIRMAFLRKVYSILSVQLLATTAVSALFYLSPSIKTFVQSHPWLFLISLIGSLILLI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  86 ALILNRHKYPLNLYLLFGFTLLEALTVAVVVTFYDVYIILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILC- 164
Cdd:cd10429   82 ALYWKRHSHPVNLILLSLFTLCEAYTVGLVVSFYDGKIVLQALILTLGVFVGLTAYTFQTKRDFSSFGALLFILLWALIl 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 322510100 165 LSGFLKFFFYSEIMELVLAAAGALLFCGFIIYDTHSLMHKLSPEEYVLAAISLYLDIINLFLHLLRFLEAVN 236
Cdd:cd10429  162 LALIFQFFPYSPTFELVYAGLGALLFSGYIVYDTQLIMKRLSPDEYILAAISLYLDIINLFLSILRILAAMN 233
Bax1-I pfam01027
Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family ...
 32-232 1.58e-38

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: 132.68  E-value: 1.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100   32 MAFLRKVYSILSLQVLLTTVTSTVFLYFESvRTFVHESPALILLFALGSLGLIFALIL----NRHKYPLNLYLLFGFTLL 107
Cdd:pfam01027   1 RQFLRKVYGLLALGLLLTAAVAYLVLSSPA-LLFPSLHPPLFWVLIIAPLGLLFGALLlarkRKYSSNVALLLLLAFTLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  108 EALTVAVVVTFYDVYIILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILCLSGFLKFFFYSEIMELVLAAAGA 187
Cdd:pfam01027  80 MGLTLGPLLLVYTGAIIATAFLGTAAIFGGLSLYALTTKRDLSFLGGFLFAGLIGLIVASLVNIFLPSSALSLAISYLGV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 322510100  188 LLFCGFIIYDTHSLMHK---LSPEEYVLAAISLYLDIINLFLHLLRFL 232
Cdd:pfam01027 160 LLFSGFILYDTQRIIKRygeYGDYDAILAALSLYLDFINLFLSLLRIL 207
YbhL COG0670
Integral membrane protein YbhL, putative Ca2+ regulator, Bax inhibitor (BI-1)/TMBIM family ...
 18-232 2.01e-36

Integral membrane protein YbhL, putative Ca2+ regulator, Bax inhibitor (BI-1)/TMBIM family [Inorganic ion transport and metabolism];


Pssm-ID: 440434  Cd Length: 231  Bit Score: 127.99  E-value: 2.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  18 NYGSSVASATVHIRMAFLRKVYSILSLQVLLTTVTSTVFLYFESVRTFVHESPALILLFALGSLGLIFAL--ILNRHKYP 95
Cdd:COG0670    6 RNAGAAAAASDAGLRKVLRNTYGLLALGLLLTALVAYLGMALPGLAALLFGSPGLFWVLLIAPLGLVFLLskLANRANSA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  96 LNLYLLFGFTLLEALTVAVVVTFY----DVYIILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILCLSGFLKF 171
Cdd:COG0670   86 AALALLFAYTALMGLTLSPILLVYtglsGPASIAQAFGGTAATFGGLSLYGYTTKRDLSFLGSFLFMGLIGLIIASLVNI 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 322510100 172 FFYSEIMELVLAAAGALLFCGFIIYDTHSLMHK-LSPEEYVLAAISLYLDIINLFLHLLRFL 232
Cdd:COG0670  166 FLQSPALSLAISVAGVLLFSGLTLYDTQRIKHGyETNKQYIMAALSLYLDFINLFLSLLRLL 227
PRK10447 PRK10447
FtsH protease modulator YccA;
35-232 8.08e-05

FtsH protease modulator YccA;


Pssm-ID: 182469  Cd Length: 219  Bit Score: 42.52  E-value: 8.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  35 LRKVYSILSLQVLLTTVTSTVflyfesVRTFVHESPALILLFAlGSLGLIFaLILNRHKYPLNLYLLFGFTLLEALTVAV 114
Cdd:PRK10447  21 LRNTYFLLSLTLAFSAITATA------STVLMLPSPGLILTLV-GMYGLMF-LTYKTANKPTGILSAFAFTGFLGYILGP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100 115 VVTFYDVY----IILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILCLSGFLKFFFYSEIMELVLAAAGALLF 190
Cdd:PRK10447  93 ILNTYLSAgmgdVIALALGGTALVFFCCSAYVLTTRKDMSFLGGMLMAGIVVVLIGMVANIFLQLPALHLAISAVFILIS 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 322510100 191 CGFIIYDTHSLMHKlSPEEYVLAAISLYLDIINLFLHLLRFL 232
Cdd:PRK10447 173 SGAILFETSNIIHG-GETNYIRATVSLYVSLYNIFVSLLSIL 213
 
Name Accession Description Interval E-value
GAAP_like cd10429
Golgi antiapoptotic protein; GAAP (or transmembrane BAX inhibitor motif containing 4) is a ...
 6-236 3.13e-100

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: 291.04  E-value: 3.13e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100   6 PRYPRSSIEDDFNYGSSVASATVHIRMAFLRKVYSILSLQVLLTTVTSTVFLYFESVRTFVHESPALILLFALGSLGLIF 85
Cdd:cd10429    2 SRYAEADIPDDFKYGTNVASAEPEIRMAFLRKVYSILSVQLLATTAVSALFYLSPSIKTFVQSHPWLFLISLIGSLILLI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  86 ALILNRHKYPLNLYLLFGFTLLEALTVAVVVTFYDVYIILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILC- 164
Cdd:cd10429   82 ALYWKRHSHPVNLILLSLFTLCEAYTVGLVVSFYDGKIVLQALILTLGVFVGLTAYTFQTKRDFSSFGALLFILLWALIl 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 322510100 165 LSGFLKFFFYSEIMELVLAAAGALLFCGFIIYDTHSLMHKLSPEEYVLAAISLYLDIINLFLHLLRFLEAVN 236
Cdd:cd10429  162 LALIFQFFPYSPTFELVYAGLGALLFSGYIVYDTQLIMKRLSPDEYILAAISLYLDIINLFLSILRILAAMN 233
BI-1-like cd06181
BAX inhibitor (BI)-1/YccA-like protein family; Mammalian members of the BAX inhibitor (BI)-1 ...
 30-233 4.38e-54

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: 172.60  E-value: 4.38e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  30 IRMAFLRKVYSILSLQVLLTTVTSTVFLYFESvrtfvhESPALILLFALGS--LGLIFALILNRHKYPLNLYLLFGFTLL 107
Cdd:cd06181    1 STKDFLRKVYMILALQLLLTAATATAFTVCDP------GWYWSPALMGLLTsmLALMATAAMIRAKMPVNLILLFGFTGL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100 108 EALTVAVVVTFYDVYIILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILCLSGFLKFFFYSEIMELVLAAAGA 187
Cdd:cd06181   75 MGYVVGPLLFFYGPTILLRALGGTALVFFGLTVYALQARKDFLFLGGPLMAGLGFLLLSFLLNTFFYSPWLHLVAAAVGL 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 322510100 188 LLFCGFIIYDTHSLMHK--LSPEEYVLAAISLYLDIINLFLHLLRFLE 233
Cdd:cd06181  155 VLFCGFLLYDTQLIIHKaeVGPEDYINACISLYLDIINIFIRLLTILA 202
LFG_like cd10428
Proteins similar to and including lifeguard (LFG), a putative regulator of apoptosis; ...
 30-232 2.24e-42

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: 143.07  E-value: 2.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  30 IRMAFLRKVYSILSLQVLLTTVTSTVFLYFESVRTFVHESPALILLFALGSLGLIFALILN---RHKYPLNLYLLFGFTL 106
Cdd:cd10428    7 IRRAFIRKVYSILTIQLLVTVAVIALFTFHDPVKKFVRKNPWLYYVSYIVFFITYIALACCeglRRRFPWNLILLGIFTL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100 107 LEALTVAVVVTFYDVYIILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILCLSGFLKFFFYSEIMELVLAAAG 186
Cdd:cd10428   87 AMSYMLGTIASFYDTKAVLIAVGITAVVCLGLTLFAFQTKYDFTSCGGVLFVLSIVLLIFGIVAIFFYVKWLHIVYASLG 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 322510100 187 ALLFCGFIIYDTHSLM----HKLSPEEYVLAAISLYLDIINLFLHLLRFL 232
Cdd:cd10428  167 ALLFSLYLAVDTQLLMggrkYELSPEEYIFAALNIYVDIVNIFLYILQLI 216
Bax1-I pfam01027
Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family ...
 32-232 1.58e-38

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: 132.68  E-value: 1.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100   32 MAFLRKVYSILSLQVLLTTVTSTVFLYFESvRTFVHESPALILLFALGSLGLIFALIL----NRHKYPLNLYLLFGFTLL 107
Cdd:pfam01027   1 RQFLRKVYGLLALGLLLTAAVAYLVLSSPA-LLFPSLHPPLFWVLIIAPLGLLFGALLlarkRKYSSNVALLLLLAFTLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  108 EALTVAVVVTFYDVYIILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILCLSGFLKFFFYSEIMELVLAAAGA 187
Cdd:pfam01027  80 MGLTLGPLLLVYTGAIIATAFLGTAAIFGGLSLYALTTKRDLSFLGGFLFAGLIGLIVASLVNIFLPSSALSLAISYLGV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 322510100  188 LLFCGFIIYDTHSLMHK---LSPEEYVLAAISLYLDIINLFLHLLRFL 232
Cdd:pfam01027 160 LLFSGFILYDTQRIIKRygeYGDYDAILAALSLYLDFINLFLSLLRIL 207
YbhL COG0670
Integral membrane protein YbhL, putative Ca2+ regulator, Bax inhibitor (BI-1)/TMBIM family ...
 18-232 2.01e-36

Integral membrane protein YbhL, putative Ca2+ regulator, Bax inhibitor (BI-1)/TMBIM family [Inorganic ion transport and metabolism];


Pssm-ID: 440434  Cd Length: 231  Bit Score: 127.99  E-value: 2.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  18 NYGSSVASATVHIRMAFLRKVYSILSLQVLLTTVTSTVFLYFESVRTFVHESPALILLFALGSLGLIFAL--ILNRHKYP 95
Cdd:COG0670    6 RNAGAAAAASDAGLRKVLRNTYGLLALGLLLTALVAYLGMALPGLAALLFGSPGLFWVLLIAPLGLVFLLskLANRANSA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  96 LNLYLLFGFTLLEALTVAVVVTFY----DVYIILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILCLSGFLKF 171
Cdd:COG0670   86 AALALLFAYTALMGLTLSPILLVYtglsGPASIAQAFGGTAATFGGLSLYGYTTKRDLSFLGSFLFMGLIGLIIASLVNI 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 322510100 172 FFYSEIMELVLAAAGALLFCGFIIYDTHSLMHK-LSPEEYVLAAISLYLDIINLFLHLLRFL 232
Cdd:COG0670  166 FLQSPALSLAISVAGVLLFSGLTLYDTQRIKHGyETNKQYIMAALSLYLDFINLFLSLLRLL 227
BI-1-like_bacterial cd10432
Bacterial BAX inhibitor (BI)-1/YccA-like proteins; This family is comprised of bacterial ...
 31-232 2.22e-33

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: 119.59  E-value: 2.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  31 RMAFLRKVYSILSLQVLLTTVTSTVFLYFESVRTFVheSPALILLFALGSLGLIFALILNRHKYPL--NLYLLFGFTLLE 108
Cdd:cd10432    2 LRSFMKKVYGLMAAGLLLTAVGAYVGASTPALLLIA--GSPLMWVLLIAELALVFGLSFRINKMSVatALPLFFAFAALT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100 109 ALTVAVVVTFYDVYIILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILCLSGFLKFFFYSEIMELVLAAAGAL 188
Cdd:cd10432   80 GLTLSPILLVYTGASIAQAFFTTAATFGGLSLYGYTTKKDLSFLGSFLFMGLIGLIIASLVNIFLQSSALQFAISAIGVL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 322510100 189 LFCGFIIYDTHSLMH-------KLSPEEYVLAAISLYLDIINLFLHLLRFL 232
Cdd:cd10432  160 IFSGLIAYDTQRIKRmyeagggESGYKDAIMGALSLYLDFINLFLFLLRLF 210
YccA_like cd10433
YccA-like proteins; A prokaryotic member of the BAX inhibitor (BI)-1 like family of small ...
 35-236 2.91e-21

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: 87.64  E-value: 2.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  35 LRKVYSILSLQVLLTTVTSTVFLYFESvrTFVHespalILLFALGSLGLIFALILNRHKyPLNLYLLFGFTLLEALTVAV 114
Cdd:cd10433    7 LRNTYMLLSMTLAFSALGAGVSMAGGS--PIMG-----LLLTLVGAYGLLFLIEKTRNS-AWGIVLVFAFTGFMGYTLGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100 115 VVTFYDVY-----IILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILCLSGFLKFFFYSEIMELVLAAAGALL 189
Cdd:cd10433   79 ILNMYLALpnggqIIMTALGGTAAIFFGLSAYALTTKKDFSFLGGFLFVGAIVLLLAAVANIFLQIPALSLAISAAFVLF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 322510100 190 FCGFIIYDTHSLMHKlSPEEYVLAAISLYLDIINLFLHLLRFLEAVN 236
Cdd:cd10433  159 SSGFILYDTSRIIHG-GETNYIMATVSLYVSIYNLFVSLLNLLGAFS 204
BI-1 cd10430
BAX inhibitor (BI)-1; Mammalian members of the BAX inhibitor (BI)-1 like family of small ...
 35-232 1.19e-13

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: 67.63  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  35 LRKVYSILSLQVLLTTVTSTVFLYfesvrtfvheSPALILLFALGSLGLIFALILNRHKY---PLNLYLLFGFTLLEALT 111
Cdd:cd10430   12 LKKVYLTLAVALLAAAVGAYVHMV----------INIGGLLTGLLSLGLSLWLAFTPSTGknePKRLGLLLGFAFLTGAS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100 112 VAVVVTFY---DVYIILQAFILTTTVFFGLTVYTLQSKK-DFSKFGAGLFALLWILCLSGFLKFFFYSEIMELVLAAAGA 187
Cdd:cd10430   82 LGPLLDLViaiNPSIIVTAFLGTAVIFACFSLAALLAKRrEYLYLGGLLSSALSILLLVSLANIFGGSKFLFQAELYLGL 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 322510100 188 LLFCGFIIYDTHSLMHK--LSPEEYVLAAISLYLDIINLFLHLLRFL 232
Cdd:cd10430  162 LVFCGFVLFDTQMIIEKaeNGDRDYIWHALDLFVDFVALFRRLLIIL 208
PRK10447 PRK10447
FtsH protease modulator YccA;
35-232 8.08e-05

FtsH protease modulator YccA;


Pssm-ID: 182469  Cd Length: 219  Bit Score: 42.52  E-value: 8.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100  35 LRKVYSILSLQVLLTTVTSTVflyfesVRTFVHESPALILLFAlGSLGLIFaLILNRHKYPLNLYLLFGFTLLEALTVAV 114
Cdd:PRK10447  21 LRNTYFLLSLTLAFSAITATA------STVLMLPSPGLILTLV-GMYGLMF-LTYKTANKPTGILSAFAFTGFLGYILGP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322510100 115 VVTFYDVY----IILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILCLSGFLKFFFYSEIMELVLAAAGALLF 190
Cdd:PRK10447  93 ILNTYLSAgmgdVIALALGGTALVFFCCSAYVLTTRKDMSFLGGMLMAGIVVVLIGMVANIFLQLPALHLAISAVFILIS 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 322510100 191 CGFIIYDTHSLMHKlSPEEYVLAAISLYLDIINLFLHLLRFL 232
Cdd:PRK10447 173 SGAILFETSNIIHG-GETNYIRATVSLYVSLYNIFVSLLSIL 213
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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