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Conserved domains on  [gi|47777306|ref|NP_001001404|]
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voltage-dependent anion-selective channel protein 1 [Danio rerio]

Protein Classification

Porin3_VDAC domain-containing protein (domain architecture ID 10163986)

Porin3_VDAC domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Porin3_VDAC cd07306
Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent ...
4-282 7.03e-123

Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent anion channel (VDAC) regulates the flux of mostly anionic metabolites through the outer mitochondrial membrane, which is highly permeable to small molecules. VDAC is the most abundant protein in the outer membrane, and membrane potentials can toggle VDAC between open or high-conducting and closed or low-conducting forms. VDAC binds to and is regulated in part by hexokinase, an interaction that renders mitochondria less susceptible to pro-apoptotic signals, most likely by intefering with VDAC's capability to respond to Bcl-2 family proteins. While VDAC appears to play a key role in mitochondrially induced cell death, a proposed involvement in forming the mitochondrial permeability transition pore, which is characteristic for damaged mitochondria and apoptosis, has been challenged by more recent studies.


:

Pssm-ID: 132767  Cd Length: 276  Bit Score: 356.13  E-value: 7.03e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306   4 PPTYVDLGKSARDIFTKGYGFGLIKLDLKTRSENGLEFKSSGSANTETSKVAGTLETKYKWAehGLTFTEKWNTDNTLGT 83
Cdd:cd07306   1 PPTYFDIGKSAKDLLTKGYNFGAWKLDVKTKTPNGVEFTSTGSKKPDTGKVSGSLEAKYKIK--GLTLTQKWNTDNVLLT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306  84 EITLEDQLTKGLKLTFDSSFSPNTGKKSGKIKSSYQREHINLGCDVDYDiNGTAVHGALVLGLDGWLAGYQMTFEAGRNR 163
Cdd:cd07306  79 EITIEDLLAPGLKLTLDTTFPPNTGKKSGKLKAGYKHDPININADVDLN-KGPLVGASAVLGYKGFLLGAEVVYDTAKSK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306 164 ITQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNDNLETAVNLAWTAGNSNTRFGIAAKYQIDSDAAFSAKVNNSSLV 243
Cdd:cd07306 158 FTKYNFALGYTNGDFELSLKLNNGKTLRGSYFHKVSPRLAVGAKVTWYSGTNETTFAVGGQYALDPDALVKAKVNNDGQL 237
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 47777306 244 GLGYTQTLKPGIKLTLSALLDGKNINAGGHKMGLGLEFE 282
Cdd:cd07306 238 GLSYQHKLRPGVTLTLSAGFDAKNLNQGGHKFGLSLSLK 276
 
Name Accession Description Interval E-value
Porin3_VDAC cd07306
Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent ...
4-282 7.03e-123

Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent anion channel (VDAC) regulates the flux of mostly anionic metabolites through the outer mitochondrial membrane, which is highly permeable to small molecules. VDAC is the most abundant protein in the outer membrane, and membrane potentials can toggle VDAC between open or high-conducting and closed or low-conducting forms. VDAC binds to and is regulated in part by hexokinase, an interaction that renders mitochondria less susceptible to pro-apoptotic signals, most likely by intefering with VDAC's capability to respond to Bcl-2 family proteins. While VDAC appears to play a key role in mitochondrially induced cell death, a proposed involvement in forming the mitochondrial permeability transition pore, which is characteristic for damaged mitochondria and apoptosis, has been challenged by more recent studies.


Pssm-ID: 132767  Cd Length: 276  Bit Score: 356.13  E-value: 7.03e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306   4 PPTYVDLGKSARDIFTKGYGFGLIKLDLKTRSENGLEFKSSGSANTETSKVAGTLETKYKWAehGLTFTEKWNTDNTLGT 83
Cdd:cd07306   1 PPTYFDIGKSAKDLLTKGYNFGAWKLDVKTKTPNGVEFTSTGSKKPDTGKVSGSLEAKYKIK--GLTLTQKWNTDNVLLT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306  84 EITLEDQLTKGLKLTFDSSFSPNTGKKSGKIKSSYQREHINLGCDVDYDiNGTAVHGALVLGLDGWLAGYQMTFEAGRNR 163
Cdd:cd07306  79 EITIEDLLAPGLKLTLDTTFPPNTGKKSGKLKAGYKHDPININADVDLN-KGPLVGASAVLGYKGFLLGAEVVYDTAKSK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306 164 ITQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNDNLETAVNLAWTAGNSNTRFGIAAKYQIDSDAAFSAKVNNSSLV 243
Cdd:cd07306 158 FTKYNFALGYTNGDFELSLKLNNGKTLRGSYFHKVSPRLAVGAKVTWYSGTNETTFAVGGQYALDPDALVKAKVNNDGQL 237
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 47777306 244 GLGYTQTLKPGIKLTLSALLDGKNINAGGHKMGLGLEFE 282
Cdd:cd07306 238 GLSYQHKLRPGVTLTLSAGFDAKNLNQGGHKFGLSLSLK 276
Porin_3 pfam01459
Eukaryotic porin;
4-276 6.83e-96

Eukaryotic porin;


Pssm-ID: 307560  Cd Length: 271  Bit Score: 287.18  E-value: 6.83e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306     4 PPTYVDLGKSARDIFTKGYGFGLIKLDLKTRSENGLEFKSSGSANTETSKVAGTLETKYKWaeHGLTFTEKWNTDNTLGT 83
Cdd:pfam01459   2 PGTYEDIGKKAKDLLNKDYHFDGAKLDVTTKTGLGVAFQVSGSKSLGSGLVSGDFEAKYKD--KGLTLTLKGDTDNTLST 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306    84 EITLEDQLTKGLKLTFDSSFSPNTGKKSGKIKSSYQREHINLGCDVDYDINGTaVHGALVLGLDGWLAGYQMTFEAGRNR 163
Cdd:pfam01459  80 TATVNEQLAPGLKTKLSTQLVPGKGKKSAKLELDYKGDDFTASLKVGLLKGPV-VVGSYLQGVTGLALGAEAGYDTASGK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306   164 ITQSNFAVGYKTDEFQLHTNV-NDGTEFGGSIYQKVNDNLETAVNLAWTAGNSNTRFGIAAKYQIDSDAAFSAKVNNSSL 242
Cdd:pfam01459 159 FTKYNAALGYTARDYIASLTLnNNGGVLTASYYHKVSEKLEVGAELTLNFSSNETTATIGYKYDLDKSTTVKAKVNSNGK 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 47777306   243 VGLGYTQTLKPGIKLTLSALLDGKNiNAGGHKMG 276
Cdd:pfam01459 239 VGLLYEQKLRPGVTLTLSAEVDHKK-LNGAHKFG 271
 
Name Accession Description Interval E-value
Porin3_VDAC cd07306
Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent ...
4-282 7.03e-123

Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent anion channel (VDAC) regulates the flux of mostly anionic metabolites through the outer mitochondrial membrane, which is highly permeable to small molecules. VDAC is the most abundant protein in the outer membrane, and membrane potentials can toggle VDAC between open or high-conducting and closed or low-conducting forms. VDAC binds to and is regulated in part by hexokinase, an interaction that renders mitochondria less susceptible to pro-apoptotic signals, most likely by intefering with VDAC's capability to respond to Bcl-2 family proteins. While VDAC appears to play a key role in mitochondrially induced cell death, a proposed involvement in forming the mitochondrial permeability transition pore, which is characteristic for damaged mitochondria and apoptosis, has been challenged by more recent studies.


Pssm-ID: 132767  Cd Length: 276  Bit Score: 356.13  E-value: 7.03e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306   4 PPTYVDLGKSARDIFTKGYGFGLIKLDLKTRSENGLEFKSSGSANTETSKVAGTLETKYKWAehGLTFTEKWNTDNTLGT 83
Cdd:cd07306   1 PPTYFDIGKSAKDLLTKGYNFGAWKLDVKTKTPNGVEFTSTGSKKPDTGKVSGSLEAKYKIK--GLTLTQKWNTDNVLLT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306  84 EITLEDQLTKGLKLTFDSSFSPNTGKKSGKIKSSYQREHINLGCDVDYDiNGTAVHGALVLGLDGWLAGYQMTFEAGRNR 163
Cdd:cd07306  79 EITIEDLLAPGLKLTLDTTFPPNTGKKSGKLKAGYKHDPININADVDLN-KGPLVGASAVLGYKGFLLGAEVVYDTAKSK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306 164 ITQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNDNLETAVNLAWTAGNSNTRFGIAAKYQIDSDAAFSAKVNNSSLV 243
Cdd:cd07306 158 FTKYNFALGYTNGDFELSLKLNNGKTLRGSYFHKVSPRLAVGAKVTWYSGTNETTFAVGGQYALDPDALVKAKVNNDGQL 237
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 47777306 244 GLGYTQTLKPGIKLTLSALLDGKNINAGGHKMGLGLEFE 282
Cdd:cd07306 238 GLSYQHKLRPGVTLTLSAGFDAKNLNQGGHKFGLSLSLK 276
Porin_3 pfam01459
Eukaryotic porin;
4-276 6.83e-96

Eukaryotic porin;


Pssm-ID: 307560  Cd Length: 271  Bit Score: 287.18  E-value: 6.83e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306     4 PPTYVDLGKSARDIFTKGYGFGLIKLDLKTRSENGLEFKSSGSANTETSKVAGTLETKYKWaeHGLTFTEKWNTDNTLGT 83
Cdd:pfam01459   2 PGTYEDIGKKAKDLLNKDYHFDGAKLDVTTKTGLGVAFQVSGSKSLGSGLVSGDFEAKYKD--KGLTLTLKGDTDNTLST 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306    84 EITLEDQLTKGLKLTFDSSFSPNTGKKSGKIKSSYQREHINLGCDVDYDINGTaVHGALVLGLDGWLAGYQMTFEAGRNR 163
Cdd:pfam01459  80 TATVNEQLAPGLKTKLSTQLVPGKGKKSAKLELDYKGDDFTASLKVGLLKGPV-VVGSYLQGVTGLALGAEAGYDTASGK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306   164 ITQSNFAVGYKTDEFQLHTNV-NDGTEFGGSIYQKVNDNLETAVNLAWTAGNSNTRFGIAAKYQIDSDAAFSAKVNNSSL 242
Cdd:pfam01459 159 FTKYNAALGYTARDYIASLTLnNNGGVLTASYYHKVSEKLEVGAELTLNFSSNETTATIGYKYDLDKSTTVKAKVNSNGK 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 47777306   243 VGLGYTQTLKPGIKLTLSALLDGKNiNAGGHKMG 276
Cdd:pfam01459 239 VGLLYEQKLRPGVTLTLSAEVDHKK-LNGAHKFG 271
Porin3 cd07303
Eukaryotic porin family that forms channels in the mitochondrial outer membrane; The porin ...
6-281 2.81e-95

Eukaryotic porin family that forms channels in the mitochondrial outer membrane; The porin family 3 contains two sub-families that play vital roles in the mitochondrial outer membrane, a translocase for unfolded pre-proteins (Tom40) and the voltage-dependent anion channel (VDAC) that regulates the flux of mostly anionic metabolites through the outer mitochondrial membrane.


Pssm-ID: 132765  Cd Length: 274  Bit Score: 285.71  E-value: 2.81e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306   6 TYVDLGKSARDIFTKGYgFGLIKLDLKTRSENglEFKSSGSANTET----SKVAGTLETKYKWAEHGLTFTEKWNTDNTL 81
Cdd:cd07303   1 TYAELGKSARDLFTKGY-GGGIKLDVKTKSEL--EFTSSGSANTETiestTKVGGSLETKYRWSPYGLTFTEKWNTDNTL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306  82 GTEITLEDQLTKGLKLTFDSSFSPNTGKKSGKIKSSYQRehINLGCDVDYDINGTAVHGALVLGLDGWLAGYQMTFEAGR 161
Cdd:cd07303  78 GLEITVEDQLSRGLKSTFDSSFSPNTGKKNAKIKTGYKR--INLGCDVDFDIAGPLIRGALVLGYEGWLAGYQMVFETVS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306 162 nRITQSNFAVGYKTD--EFQLHTNVNDGTEFGGSIYQKVNDNLETAVNLAWTAGNSNTRFGIAAKYQIDSDAAFSAKVNN 239
Cdd:cd07303 156 -RVTQSNFAVGYKTDynEFQAHTNVNDGTEFGGSIYHKVNDKLEVGVNLAATAGNSNTRFGIAAKYQVDPDACFSASVNN 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 47777306 240 SSLVGLGYTQTLKPGIKLTLSALLDGKNinaGGHKMGLGLEF 281
Cdd:cd07303 235 SSLVGLGYTQTLKPGIKLTLSALLDHKA---GGHKLGLGLEF 273
Porin3_Tom40 cd07305
Translocase of outer mitochondrial membrane 40 (Tom40); Tom40 forms a channel in the ...
162-282 3.73e-08

Translocase of outer mitochondrial membrane 40 (Tom40); Tom40 forms a channel in the mitochondrial outer membrane with a pore about 1.5 to 2.5 nanometers wide. It functions as a transport channel for unfolded protein chains and forms a complex with Tom5, Tom6, Tom7, and Tom22. The primary receptors Tom20 and Tom70 recruit the unfolded precursor protein from the mitochondrial-import stimulating factor (MSF) or cytosolic Hsc70. The precursor passes through the Tom40 channel and through another channel in the inner membrane, formed by Tim23, to be finally translocated into the mitochondrial matrix. The process depends on a proton motive force across the inner membrane and requires a contact site where the outer and inner membranes come close. Tom40 is also involved in inserting outer membrane proteins into the membrane, most likely not via a lateral opening in the pore, but by transfering precursor proteins to an outer membrane sorting and assembly machinery.


Pssm-ID: 132766  Cd Length: 279  Bit Score: 53.37  E-value: 3.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47777306 162 NRITQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNDNLETAVNLAWTAGNSNTRFGIAAKYQIdSDAAFSAKVNNSS 241
Cdd:cd07305 163 NGISVLSYAARYTAGNWIASGQLGAQGGLHLSYYRKLSDKLQLGVELELNLRTRESTATLGYQYDF-RQSRFRGSIDSNG 241
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 47777306 242 LVGLGYTQTLKPGIKLTLSALLDGKNINAgghKMGLGLEFE 282
Cdd:cd07305 242 KVSAVLEKRLPLPLSLLLSGELNHVKNDY---KFGFGLTIG 279
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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