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Conserved domains on  [gi|193083122|ref|NP_001122389|]
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mitochondrial import receptor subunit TOM40 homolog [Homo sapiens]

Protein Classification

mitochondrial import receptor subunit TOM40 family protein( domain architecture ID 10163980)

mitochondrial import receptor subunit TOM40 family protein is a porin similar to translocase of outer mitochondrial membrane 40 (Tom40) which forms channels in the mitochondrial outer membrane and functions as a transport channel for unfolded protein chains

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Porin3_Tom40 cd07305
Translocase of outer mitochondrial membrane 40 (Tom40); Tom40 forms a channel in the ...
77-361 1.08e-131

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 [Multi-domain]  Cd Length: 279  Bit Score: 377.70  E-value: 1.08e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122  77 LPNPGTFEECHRKCKELFPIQME-GVKLTVNKGLSNHFQVNHTVALSTIGE-SNYHFGVTYVGTKQlspteaFPVLVGDM 154
Cdd:cd07305    1 LPNPGTFEELHREVKEVFPLDFFdGFRLDVNKGLSPHFQVSHSLHLGSSSLtSSYQFGATYVGDKQ------YPFLQGDI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122 155 DNSGSLNAQVIHQLGPGLRSKMAIQTQQSKFVNWQVDGEYRGSDFTAAVTLGNPDVLVGSGILVAHYLQSITPCLALGGE 234
Cdd:cd07305   75 DNDGNLNARIIHQLGDRLRSKLQAQLQDSKFNMSQLELDYRGDDFTASLKLANPDILNETGIYVASYLQSVTPKLALGGE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122 235 LVYHRRPGEEGTVMSLAGKYTLNNWLATVTLGQAGM-HATYYHKASDQLQVGVEFEASTRMQDTSVSFGYQLDLPKAnlL 313
Cdd:cd07305  155 LVYQRVPGNGISVLSYAARYTAGNWIASGQLGAQGGlHLSYYRKLSDKLQLGVELELNLRTRESTATLGYQYDFRQS--R 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 193083122 314 FKGSVDSNWIVGATLEKKlPPLPLTLALGAFLNHRKNKFQCGFGLTIG 361
Cdd:cd07305  233 FRGSIDSNGKVSAVLEKR-LPLPLSLLLSGELNHVKNDYKFGFGLTIG 279
 
Name Accession Description Interval E-value
Porin3_Tom40 cd07305
Translocase of outer mitochondrial membrane 40 (Tom40); Tom40 forms a channel in the ...
77-361 1.08e-131

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 [Multi-domain]  Cd Length: 279  Bit Score: 377.70  E-value: 1.08e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122  77 LPNPGTFEECHRKCKELFPIQME-GVKLTVNKGLSNHFQVNHTVALSTIGE-SNYHFGVTYVGTKQlspteaFPVLVGDM 154
Cdd:cd07305    1 LPNPGTFEELHREVKEVFPLDFFdGFRLDVNKGLSPHFQVSHSLHLGSSSLtSSYQFGATYVGDKQ------YPFLQGDI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122 155 DNSGSLNAQVIHQLGPGLRSKMAIQTQQSKFVNWQVDGEYRGSDFTAAVTLGNPDVLVGSGILVAHYLQSITPCLALGGE 234
Cdd:cd07305   75 DNDGNLNARIIHQLGDRLRSKLQAQLQDSKFNMSQLELDYRGDDFTASLKLANPDILNETGIYVASYLQSVTPKLALGGE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122 235 LVYHRRPGEEGTVMSLAGKYTLNNWLATVTLGQAGM-HATYYHKASDQLQVGVEFEASTRMQDTSVSFGYQLDLPKAnlL 313
Cdd:cd07305  155 LVYQRVPGNGISVLSYAARYTAGNWIASGQLGAQGGlHLSYYRKLSDKLQLGVELELNLRTRESTATLGYQYDFRQS--R 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 193083122 314 FKGSVDSNWIVGATLEKKlPPLPLTLALGAFLNHRKNKFQCGFGLTIG 361
Cdd:cd07305  233 FRGSIDSNGKVSAVLEKR-LPLPLSLLLSGELNHVKNDYKFGFGLTIG 279
Porin_3 pfam01459
Eukaryotic porin;
79-357 3.39e-73

Eukaryotic porin;


Pssm-ID: 460220 [Multi-domain]  Cd Length: 269  Bit Score: 228.25  E-value: 3.39e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122   79 NPGTFEECHRKCKELFP--IQMEGVKLTVNK--GLSNHFQVNHTVALSTiGESNYHFGVTYV--GTKQlspteafpVLVG 152
Cdd:pfam01459   1 NPGTYEDIGKEAKDLLNkdYHFDGAKLDVTTksGLGVAFQVSGSFSLGS-GLSSGDFEAKYKdkGLTL--------TLKG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122  153 DMDNSGSLNAQVIHQLGPGLRSKMAIQTQQSKFvNWQVDGEYRGSDFTAAVTLGNpdvlVGSGILVAHYLQSITpCLALG 232
Cdd:pfam01459  72 DTDNDLSTTATVNEQLTPGLKTKLSTQFVPGKK-SGKLELDYKGDDFTASLKVGL----LAGPVVVGSYLQGVT-GLALG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122  233 GELVYHRR---PGEEGTVMSLAGKytlnNWLATVTLGQAG--MHATYYHKASDQLQVGVEFEASTRMQDTSVSFGYQLDL 307
Cdd:pfam01459 146 AEASYDTAsgkLTKYNAALGYTAR----DYIASLTLVNNGgvLTASYYHKVSEKLEVGAELTLNFSSNENTVTIGYKYDL 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 193083122  308 PKANlLFKGSVDSNWIVGATLEKKlPPLPLTLALGAFLNHRKNKFQCGFG 357
Cdd:pfam01459 222 DKST-TVKAKVNSNGKVGLLYEQK-LRPGVTLTLSAEVDHKKLNGAHKFG 269
3a0801s07tom40 TIGR00989
mitochondrial import receptor subunit Tom40; The mitochondrial protein translocase (MPT) ...
77-237 1.59e-15

mitochondrial import receptor subunit Tom40; The mitochondrial protein translocase (MPT) family, which brings nuclearly encoded preproteins into mitochondria, is very complex with 19 currently identified protein constituents.These proteins include several chaperone proteins, four proteins of the outer membrane translocase (Tom) import receptor, five proteins of the Tom channel complex, five proteins of the inner membrane translocase (Tim) and three "motor" proteins. This family is specific for the Tom40 proteins. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130062  Cd Length: 161  Bit Score: 73.38  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122   77 LPNPGTFEECHRKC-KELFPIQ--MEGVKLTVNKGLSNH--FQVNHTVALSTIGESNYHFGVTYvGTKQLspteafpVLV 151
Cdd:TIGR00989   1 LSNPGTIENLAKEVsRDTLLSNymFTGLRADVTKAFSLAplFQVSHQFAMGSQRLPPYAFSALF-GTNQL-------FAQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122  152 GDMDNSGSLNAQVIHQLGPGLRSKMAIQTQQSKFVNWQVDGEYRGSDFTAAVTLGNPDVLVG--SGILVAHYLQSITPCL 229
Cdd:TIGR00989  73 GNLDNDGAVSTRLNYRWGDRTISKVQFQISGGQPDMCQFEHDHLGDDFSASLKAINPSFLEKglTGIFVGSYLQSVTPRL 152

                  ....*...
gi 193083122  230 ALGGELVY 237
Cdd:TIGR00989 153 GLGLEALW 160
 
Name Accession Description Interval E-value
Porin3_Tom40 cd07305
Translocase of outer mitochondrial membrane 40 (Tom40); Tom40 forms a channel in the ...
77-361 1.08e-131

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 [Multi-domain]  Cd Length: 279  Bit Score: 377.70  E-value: 1.08e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122  77 LPNPGTFEECHRKCKELFPIQME-GVKLTVNKGLSNHFQVNHTVALSTIGE-SNYHFGVTYVGTKQlspteaFPVLVGDM 154
Cdd:cd07305    1 LPNPGTFEELHREVKEVFPLDFFdGFRLDVNKGLSPHFQVSHSLHLGSSSLtSSYQFGATYVGDKQ------YPFLQGDI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122 155 DNSGSLNAQVIHQLGPGLRSKMAIQTQQSKFVNWQVDGEYRGSDFTAAVTLGNPDVLVGSGILVAHYLQSITPCLALGGE 234
Cdd:cd07305   75 DNDGNLNARIIHQLGDRLRSKLQAQLQDSKFNMSQLELDYRGDDFTASLKLANPDILNETGIYVASYLQSVTPKLALGGE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122 235 LVYHRRPGEEGTVMSLAGKYTLNNWLATVTLGQAGM-HATYYHKASDQLQVGVEFEASTRMQDTSVSFGYQLDLPKAnlL 313
Cdd:cd07305  155 LVYQRVPGNGISVLSYAARYTAGNWIASGQLGAQGGlHLSYYRKLSDKLQLGVELELNLRTRESTATLGYQYDFRQS--R 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 193083122 314 FKGSVDSNWIVGATLEKKlPPLPLTLALGAFLNHRKNKFQCGFGLTIG 361
Cdd:cd07305  233 FRGSIDSNGKVSAVLEKR-LPLPLSLLLSGELNHVKNDYKFGFGLTIG 279
Porin3 cd07303
Eukaryotic porin family that forms channels in the mitochondrial outer membrane; The porin ...
82-361 2.92e-111

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 [Multi-domain]  Cd Length: 274  Bit Score: 325.38  E-value: 2.92e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122  82 TFEECHRKCKELFPIQME-GVKLTVNKGLSNHFQVNHTVALSTIgESNYHFGVTYVGTKQLSPTEAFPVLVGDMDNSGSL 160
Cdd:cd07303    1 TYAELGKSARDLFTKGYGgGIKLDVKTKSELEFTSSGSANTETI-ESTTKVGGSLETKYRWSPYGLTFTEKWNTDNTLGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122 161 NAQVIHQLGPGLRSKMAIQTQQ-SKFVNWQVDGEYRGSDFTAAVTLGNpdvlvgSGILVAHYLQSITPCLALGGELVYHR 239
Cdd:cd07303   80 EITVEDQLSRGLKSTFDSSFSPnTGKKNAKIKTGYKRINLGCDVDFDI------AGPLIRGALVLGYEGWLAGYQMVFET 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122 240 --RPGEEGTVMSLAGKYtlNNWLATVTLGQ-AGMHATYYHKASDQLQVGVEFEASTRMQDTSVSFGYQLDLPKaNLLFKG 316
Cdd:cd07303  154 vsRVTQSNFAVGYKTDY--NEFQAHTNVNDgTEFGGSIYHKVNDKLEVGVNLAATAGNSNTRFGIAAKYQVDP-DACFSA 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 193083122 317 SVDSNWIVGATLEKKLPPLPLTLALgAFLNHRKNKFQCGFGLTIG 361
Cdd:cd07303  231 SVNNSSLVGLGYTQTLKPGIKLTLS-ALLDHKAGGHKLGLGLEFQ 274
Porin_3 pfam01459
Eukaryotic porin;
79-357 3.39e-73

Eukaryotic porin;


Pssm-ID: 460220 [Multi-domain]  Cd Length: 269  Bit Score: 228.25  E-value: 3.39e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122   79 NPGTFEECHRKCKELFP--IQMEGVKLTVNK--GLSNHFQVNHTVALSTiGESNYHFGVTYV--GTKQlspteafpVLVG 152
Cdd:pfam01459   1 NPGTYEDIGKEAKDLLNkdYHFDGAKLDVTTksGLGVAFQVSGSFSLGS-GLSSGDFEAKYKdkGLTL--------TLKG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122  153 DMDNSGSLNAQVIHQLGPGLRSKMAIQTQQSKFvNWQVDGEYRGSDFTAAVTLGNpdvlVGSGILVAHYLQSITpCLALG 232
Cdd:pfam01459  72 DTDNDLSTTATVNEQLTPGLKTKLSTQFVPGKK-SGKLELDYKGDDFTASLKVGL----LAGPVVVGSYLQGVT-GLALG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122  233 GELVYHRR---PGEEGTVMSLAGKytlnNWLATVTLGQAG--MHATYYHKASDQLQVGVEFEASTRMQDTSVSFGYQLDL 307
Cdd:pfam01459 146 AEASYDTAsgkLTKYNAALGYTAR----DYIASLTLVNNGgvLTASYYHKVSEKLEVGAELTLNFSSNENTVTIGYKYDL 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 193083122  308 PKANlLFKGSVDSNWIVGATLEKKlPPLPLTLALGAFLNHRKNKFQCGFG 357
Cdd:pfam01459 222 DKST-TVKAKVNSNGKVGLLYEQK-LRPGVTLTLSAEVDHKKLNGAHKFG 269
3a0801s07tom40 TIGR00989
mitochondrial import receptor subunit Tom40; The mitochondrial protein translocase (MPT) ...
77-237 1.59e-15

mitochondrial import receptor subunit Tom40; The mitochondrial protein translocase (MPT) family, which brings nuclearly encoded preproteins into mitochondria, is very complex with 19 currently identified protein constituents.These proteins include several chaperone proteins, four proteins of the outer membrane translocase (Tom) import receptor, five proteins of the Tom channel complex, five proteins of the inner membrane translocase (Tim) and three "motor" proteins. This family is specific for the Tom40 proteins. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130062  Cd Length: 161  Bit Score: 73.38  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122   77 LPNPGTFEECHRKC-KELFPIQ--MEGVKLTVNKGLSNH--FQVNHTVALSTIGESNYHFGVTYvGTKQLspteafpVLV 151
Cdd:TIGR00989   1 LSNPGTIENLAKEVsRDTLLSNymFTGLRADVTKAFSLAplFQVSHQFAMGSQRLPPYAFSALF-GTNQL-------FAQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122  152 GDMDNSGSLNAQVIHQLGPGLRSKMAIQTQQSKFVNWQVDGEYRGSDFTAAVTLGNPDVLVG--SGILVAHYLQSITPCL 229
Cdd:TIGR00989  73 GNLDNDGAVSTRLNYRWGDRTISKVQFQISGGQPDMCQFEHDHLGDDFSASLKAINPSFLEKglTGIFVGSYLQSVTPRL 152

                  ....*...
gi 193083122  230 ALGGELVY 237
Cdd:TIGR00989 153 GLGLEALW 160
Porin3_VDAC cd07306
Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent ...
176-307 3.43e-05

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 [Multi-domain]  Cd Length: 276  Bit Score: 44.89  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083122 176 MAIQTQQSKFVNWQVDGEYRGSDFTAAVTLGNPDVLVGSgilvahYLQSITPCLALGGELvyHRRPGEEGTVMSLAGKYT 255
Cdd:cd07306  149 VVYDTAKSKFTKYNFALGYTNGDFELSLKLNNGKTLRGS------YFHKVSPRLAVGAKV--TWYSGTNETTFAVGGQYA 220
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193083122 256 LNNwLATV-----TLGQAGMhaTYYHKASDQLQVGVEFEASTRM-QDTSVSFGYQLDL 307
Cdd:cd07306  221 LDP-DALVkakvnNDGQLGL--SYQHKLRPGVTLTLSAGFDAKNlNQGGHKFGLSLSL 275
Porin3_VDAC cd07306
Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent ...
272-331 4.00e-03

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 [Multi-domain]  Cd Length: 276  Bit Score: 38.73  E-value: 4.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193083122 272 ATYYHKASDQLQVGVEFEASTRMQDTSVSFG--YQLDlpkANLLFKGSVDSNWIVGATLEKK 331
Cdd:cd07306  186 GSYFHKVSPRLAVGAKVTWYSGTNETTFAVGgqYALD---PDALVKAKVNNDGQLGLSYQHK 244
 
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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