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Conserved domains on  [gi|17531993|ref|NP_495912|]
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Mitochondrial import receptor subunit TOM40 homolog [Caenorhabditis elegans]

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 ...
16-301 2.91e-114

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: 330.71  E-value: 2.91e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993  16 TNPGSYEELHRKARDVFPTCFE-GAKLMVNKGLSSHFQVSHTLSLSAMN--TGYRFGATYVGTNQvgpaeaYPILLGDTD 92
Cdd:cd07305   2 PNPGTFEELHREVKEVFPLDFFdGFRLDVNKGLSPHFQVSHSLHLGSSSltSSYQFGATYVGDKQ------YPFLQGDID 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993  93 VNGNTTATILHQLG-IYRTKLQGQIQQGKLAGAQATIERKGRLSTLGLTLANIDLVNEAGILVGQFLRRLTPRLDVGTEM 171
Cdd:cd07305  76 NDGNLNARIIHQLGdRLRSKLQAQLQDSKFNMSQLELDYRGDDFTASLKLANPDILNETGIYVASYLQSVTPKLALGGEL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993 172 VYQYGkniPGGQISVLSYAARYTANHFIAAATLGASG-VHLTYYHKQNENLAFGVEFECNANVGEAVTTLAYQTELPeeG 250
Cdd:cd07305 156 VYQRV---PGNGISVLSYAARYTAGNWIASGQLGAQGgLHLSYYRKLSDKLQLGVELELNLRTRESTATLGYQYDFR--Q 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 17531993 251 VTMRASFDTNWTVGGVFEKRLsqQLPFTLALSGTLNHVKAAGKFGIGLIIG 301
Cdd:cd07305 231 SRFRGSIDSNGKVSAVLEKRL--PLPLSLLLSGELNHVKNDYKFGFGLTIG 279
 
Name Accession Description Interval E-value
Porin3_Tom40 cd07305
Translocase of outer mitochondrial membrane 40 (Tom40); Tom40 forms a channel in the ...
16-301 2.91e-114

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: 330.71  E-value: 2.91e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993  16 TNPGSYEELHRKARDVFPTCFE-GAKLMVNKGLSSHFQVSHTLSLSAMN--TGYRFGATYVGTNQvgpaeaYPILLGDTD 92
Cdd:cd07305   2 PNPGTFEELHREVKEVFPLDFFdGFRLDVNKGLSPHFQVSHSLHLGSSSltSSYQFGATYVGDKQ------YPFLQGDID 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993  93 VNGNTTATILHQLG-IYRTKLQGQIQQGKLAGAQATIERKGRLSTLGLTLANIDLVNEAGILVGQFLRRLTPRLDVGTEM 171
Cdd:cd07305  76 NDGNLNARIIHQLGdRLRSKLQAQLQDSKFNMSQLELDYRGDDFTASLKLANPDILNETGIYVASYLQSVTPKLALGGEL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993 172 VYQYGkniPGGQISVLSYAARYTANHFIAAATLGASG-VHLTYYHKQNENLAFGVEFECNANVGEAVTTLAYQTELPeeG 250
Cdd:cd07305 156 VYQRV---PGNGISVLSYAARYTAGNWIASGQLGAQGgLHLSYYRKLSDKLQLGVELELNLRTRESTATLGYQYDFR--Q 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 17531993 251 VTMRASFDTNWTVGGVFEKRLsqQLPFTLALSGTLNHVKAAGKFGIGLIIG 301
Cdd:cd07305 231 SRFRGSIDSNGKVSAVLEKRL--PLPLSLLLSGELNHVKNDYKFGFGLTIG 279
Porin_3 pfam01459
Eukaryotic porin;
17-297 2.04e-72

Eukaryotic porin;


Pssm-ID: 460220 [Multi-domain]  Cd Length: 269  Bit Score: 224.01  E-value: 2.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993    17 NPGSYEELHRKARDVFPTC--FEGAKLMVNK--GLSSHFQVSHTLSLSAMNTGYRFGATYV--GTNQVgpaeaypiLLGD 90
Cdd:pfam01459   1 NPGTYEDIGKEAKDLLNKDyhFDGAKLDVTTksGLGVAFQVSGSFSLGSGLSSGDFEAKYKdkGLTLT--------LKGD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993    91 TDVNGNTTATILHQLGI-YRTKLQGQIQQGKlAGAQATIERKGRLSTLGLTLANidlvNEAGILVGQFLRRLTpRLDVGT 169
Cdd:pfam01459  73 TDNDLSTTATVNEQLTPgLKTKLSTQFVPGK-KSGKLELDYKGDDFTASLKVGL----LAGPVVVGSYLQGVT-GLALGA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993   170 EMVYQYGKNIPGGQISVLSYAARytanHFIAAATLG--ASGVHLTYYHKQNENLAFGVEFECNANVGEAVTTLAYQTELP 247
Cdd:pfam01459 147 EASYDTASGKLTKYNAALGYTAR----DYIASLTLVnnGGVLTASYYHKVSEKLEVGAELTLNFSSNENTVTIGYKYDLD 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 17531993   248 eEGVTMRASFDTNWTVGGVFEKRLsqQLPFTLALSGTLNHVKAAGKFGIG 297
Cdd:pfam01459 223 -KSTTVKAKVNSNGKVGLLYEQKL--RPGVTLTLSAEVDHKKLNGAHKFG 269
3a0801s07tom40 TIGR00989
mitochondrial import receptor subunit Tom40; The mitochondrial protein translocase (MPT) ...
17-174 1.41e-09

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: 56.05  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993    17 NPGSYEELHRK-ARDVFPT--CFEGAKLMVNKGLSSH--FQVSHTLSL-SAMNTGYRFGATYvGTNQVgpaeaypILLGD 90
Cdd:TIGR00989   3 NPGTIENLAKEvSRDTLLSnyMFTGLRADVTKAFSLAplFQVSHQFAMgSQRLPPYAFSALF-GTNQL-------FAQGN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993    91 TDVNGNTTATILHQLGIYR-TKLQGQIQQGKLAGAQATIERKGRLSTLGLTLANIDLVNEA--GILVGQFLRRLTPRLDV 167
Cdd:TIGR00989  75 LDNDGAVSTRLNYRWGDRTiSKVQFQISGGQPDMCQFEHDHLGDDFSASLKAINPSFLEKGltGIFVGSYLQSVTPRLGL 154

                  ....*..
gi 17531993   168 GTEMVYQ 174
Cdd:TIGR00989 155 GLEALWQ 161
 
Name Accession Description Interval E-value
Porin3_Tom40 cd07305
Translocase of outer mitochondrial membrane 40 (Tom40); Tom40 forms a channel in the ...
16-301 2.91e-114

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: 330.71  E-value: 2.91e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993  16 TNPGSYEELHRKARDVFPTCFE-GAKLMVNKGLSSHFQVSHTLSLSAMN--TGYRFGATYVGTNQvgpaeaYPILLGDTD 92
Cdd:cd07305   2 PNPGTFEELHREVKEVFPLDFFdGFRLDVNKGLSPHFQVSHSLHLGSSSltSSYQFGATYVGDKQ------YPFLQGDID 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993  93 VNGNTTATILHQLG-IYRTKLQGQIQQGKLAGAQATIERKGRLSTLGLTLANIDLVNEAGILVGQFLRRLTPRLDVGTEM 171
Cdd:cd07305  76 NDGNLNARIIHQLGdRLRSKLQAQLQDSKFNMSQLELDYRGDDFTASLKLANPDILNETGIYVASYLQSVTPKLALGGEL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993 172 VYQYGkniPGGQISVLSYAARYTANHFIAAATLGASG-VHLTYYHKQNENLAFGVEFECNANVGEAVTTLAYQTELPeeG 250
Cdd:cd07305 156 VYQRV---PGNGISVLSYAARYTAGNWIASGQLGAQGgLHLSYYRKLSDKLQLGVELELNLRTRESTATLGYQYDFR--Q 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 17531993 251 VTMRASFDTNWTVGGVFEKRLsqQLPFTLALSGTLNHVKAAGKFGIGLIIG 301
Cdd:cd07305 231 SRFRGSIDSNGKVSAVLEKRL--PLPLSLLLSGELNHVKNDYKFGFGLTIG 279
Porin_3 pfam01459
Eukaryotic porin;
17-297 2.04e-72

Eukaryotic porin;


Pssm-ID: 460220 [Multi-domain]  Cd Length: 269  Bit Score: 224.01  E-value: 2.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993    17 NPGSYEELHRKARDVFPTC--FEGAKLMVNK--GLSSHFQVSHTLSLSAMNTGYRFGATYV--GTNQVgpaeaypiLLGD 90
Cdd:pfam01459   1 NPGTYEDIGKEAKDLLNKDyhFDGAKLDVTTksGLGVAFQVSGSFSLGSGLSSGDFEAKYKdkGLTLT--------LKGD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993    91 TDVNGNTTATILHQLGI-YRTKLQGQIQQGKlAGAQATIERKGRLSTLGLTLANidlvNEAGILVGQFLRRLTpRLDVGT 169
Cdd:pfam01459  73 TDNDLSTTATVNEQLTPgLKTKLSTQFVPGK-KSGKLELDYKGDDFTASLKVGL----LAGPVVVGSYLQGVT-GLALGA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993   170 EMVYQYGKNIPGGQISVLSYAARytanHFIAAATLG--ASGVHLTYYHKQNENLAFGVEFECNANVGEAVTTLAYQTELP 247
Cdd:pfam01459 147 EASYDTASGKLTKYNAALGYTAR----DYIASLTLVnnGGVLTASYYHKVSEKLEVGAELTLNFSSNENTVTIGYKYDLD 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 17531993   248 eEGVTMRASFDTNWTVGGVFEKRLsqQLPFTLALSGTLNHVKAAGKFGIG 297
Cdd:pfam01459 223 -KSTTVKAKVNSNGKVGLLYEQKL--RPGVTLTLSAEVDHKKLNGAHKFG 269
Porin3 cd07303
Eukaryotic porin family that forms channels in the mitochondrial outer membrane; The porin ...
20-301 2.04e-40

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: 142.03  E-value: 2.04e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993  20 SYEELHRKARDVFPT-CFEGAKLMVNKGLSSHFQVSHTLSLSAMNTGYRFGATYVGTNQVGPAEAYPILLGDTDVNGNTT 98
Cdd:cd07303   1 TYAELGKSARDLFTKgYGGGIKLDVKTKSELEFTSSGSANTETIESTTKVGGSLETKYRWSPYGLTFTEKWNTDNTLGLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993  99 ATILHQLGI-YRTKLQGQIQQgKLAGAQATIERKGRLSTLGltlANIDLVNeAGILVGQFLRRLTPRLDVGTEMVYQYGK 177
Cdd:cd07303  81 ITVEDQLSRgLKSTFDSSFSP-NTGKKNAKIKTGYKRINLG---CDVDFDI-AGPLIRGALVLGYEGWLAGYQMVFETVS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993 178 NiPGGQISVLSYAARYtaNHFIAAATLG-ASGVHLTYYHKQNENLAFGVEFECNANVGEAVTTLAYQTELPEEGVtMRAS 256
Cdd:cd07303 156 R-VTQSNFAVGYKTDY--NEFQAHTNVNdGTEFGGSIYHKVNDKLEVGVNLAATAGNSNTRFGIAAKYQVDPDAC-FSAS 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 17531993 257 FDTNWTVGGVFEKRLsqQLPFTLALSGTLNHVKAAGKFGIGLIIG 301
Cdd:cd07303 232 VNNSSLVGLGYTQTL--KPGIKLTLSALLDHKAGGHKLGLGLEFQ 274
3a0801s07tom40 TIGR00989
mitochondrial import receptor subunit Tom40; The mitochondrial protein translocase (MPT) ...
17-174 1.41e-09

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: 56.05  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993    17 NPGSYEELHRK-ARDVFPT--CFEGAKLMVNKGLSSH--FQVSHTLSL-SAMNTGYRFGATYvGTNQVgpaeaypILLGD 90
Cdd:TIGR00989   3 NPGTIENLAKEvSRDTLLSnyMFTGLRADVTKAFSLAplFQVSHQFAMgSQRLPPYAFSALF-GTNQL-------FAQGN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993    91 TDVNGNTTATILHQLGIYR-TKLQGQIQQGKLAGAQATIERKGRLSTLGLTLANIDLVNEA--GILVGQFLRRLTPRLDV 167
Cdd:TIGR00989  75 LDNDGAVSTRLNYRWGDRTiSKVQFQISGGQPDMCQFEHDHLGDDFSASLKAINPSFLEKGltGIFVGSYLQSVTPRLGL 154

                  ....*..
gi 17531993   168 GTEMVYQ 174
Cdd:TIGR00989 155 GLEALWQ 161
Porin3_VDAC cd07306
Voltage-dependent anion channel of the outer mitochondrial membrane; The voltage-dependent ...
18-300 2.07e-07

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: 51.06  E-value: 2.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993  18 PGSYEELHRKARDVFptcfegaklmvNKGLssHFQVsHTLSLSAM-NTGYRFGATYVGTNQVGPAEA-----YPILLGDT 91
Cdd:cd07306   1 PPTYFDIGKSAKDLL-----------TKGY--NFGA-WKLDVKTKtPNGVEFTSTGSKKPDTGKVSGsleakYKIKGLTL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993  92 DVNGNTTATILHQLGIyrtklQGQIQQGKLAGAQATI-----ERKGRLST------LGLTLAnIDLVN----EAGILVG- 155
Cdd:cd07306  67 TQKWNTDNVLLTEITI-----EDLLAPGLKLTLDTTFppntgKKSGKLKAgykhdpININAD-VDLNKgplvGASAVLGy 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531993 156 -QFLrrltprldVGTEMVYqygkNIPGGQISVLSYAARYTANHFIAAATLG-ASGVHLTYYHKQNENLAFGVEFECNANV 233
Cdd:cd07306 141 kGFL--------LGAEVVY----DTAKSKFTKYNFALGYTNGDFELSLKLNnGKTLRGSYFHKVSPRLAVGAKVTWYSGT 208
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17531993 234 GEAVTTLAYQTELpEEGVTMRASFDTNWTVGGVFEKRLSQQLPFTLALS-GTLNHVKAAGKFGIGLII 300
Cdd:cd07306 209 NETTFAVGGQYAL-DPDALVKAKVNNDGQLGLSYQHKLRPGVTLTLSAGfDAKNLNQGGHKFGLSLSL 275
 
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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