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Conserved domains on  [gi|530405578|ref|XP_005254311|]
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MAX gene-associated protein isoform X26 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bHLHzip_MGA cd18911
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) and ...
 987-1051 2.17e-33

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) and similar proteins; MGA, also termed MAX dimerization protein 5 (MAD5), is a dual specificity T-box/ bHLHzip transcription factor that regulates the expression of both Max-network and T-box family target genes. It contains a Myc-like bHLHZip motif and requires heterodimerization with Max for binding to the preferred Myc-Max-binding site CACGTG. In addition to the bHLHZip domain, MGA harbors a second DNA-binding domain, the T-box or T-domain. It thus binds the preferred Brachyury-binding sequence and represses transcription of reporter genes containing promoter-proximal Brachyury-binding sites.


:

Pssm-ID: 381481  Cd Length: 65  Bit Score: 123.36  E-value: 2.17e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLT 1051
Cdd:cd18911     1 RRTHTANERRRRNEMRDLFEKLKRTLGLHNLPKVSKYYILKQAFEEIQGLTDQADRLIGQKTLLT 65
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 48-366 2.52e-05

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


The actual alignment was detected with superfamily member pfam17823:

Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 48.80  E-value: 2.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578    48 ASRKPRTLLPSTSNSKMASSSGTATNRP-GKNLKAfvPAKRPIAARPSPGGVFTQfvmskvgalqqkiPGVSTPQTLAGT 126
Cdd:pfam17823   65 AAPAPVTLTKGTSAAHLNSTEVTAEHTPhGTDLSE--PATREGAADGAASRALAA-------------AASSSPSSAAQS 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   127 QKFSIRPSPvmvvTPVVSSEPVQVCSPVTAAVTTTTPQVFLENTTA--VTPMTAISDVETKETTYSSGATTTGVVEVSET 204
Cdd:pfam17823  130 LPAAIAALP----SEAFSAPRAAACRANASAAPRAAIAAASAPHAAspAPRTAASSTTAASSTTAASSAPTTAASSAPAT 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   205 NTSTSVTSTQstatvnltkTTGITTPVASVAfpkslVASPSTITlPVASTASTSLVVVTAAAsssmVTTPTSSLGSVPII 284
Cdd:pfam17823  206 LTPARGISTA---------ATATGHPAAGTA-----LAAVGNSS-PAAGTVTAAVGTVTPAA----LATLAAAAGTVASA 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   285 LSGINGSPPVSQRPENAAQIPVATPQVSPNTVKRAGPRLLLIPVQqgspTLRPVSNTqlqghrmvlQPVRSPSGMNLFRH 364
Cdd:pfam17823  267 AGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVS----TDQPVHNT---------AGEPTPSPSNTTLE 333


                   ..
gi 530405578   365 PN 366
Cdd:pfam17823  334 PN 335
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 222-544 2.23e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   222 TKTTGITTPVASVAFPKSLVASPSTITLPVASTASTSLVVVTAAASSSMVTTPTSSLGSVPIILSGINGSPPVSQRPENA 301
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPP 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   302 AQ---IPVATPQVSPNTVK---------------RAGPRLLLIPV-----------QQGSPTLRPVSNTQLQGHRMVLQP 352
Cdd:pfam03154  249 LQpmtQPPPPSQVSPQPLPqpslhgqmppmphslQTGPSHMQHPVppqpfpltpqsSQSQVPPGPSPAAPGQSQQRIHTP 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   353 VRSPSGMNL------------FRHPNGQIVQLLPLHQLrgSNTQPNLQPVMFRNPGSV-MGIRLPAP------SKPSETP 413
Cdd:pfam03154  329 PSQSQLQSQqppreqplppapLSMPHIKPPPTTPIPQL--PNPQSHKHPPHLSGPSPFqMNSNLPPPpalkplSSLSTHH 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   414 PSSTSSSAFSVMNPVIQAVGSSSAVNVITQAPSLLSSGASFVSQAGTLTLRISPPEPQ-SFASktGSETKITYSSGGQPV 492
Cdd:pfam03154  407 PPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQhPFVP--GGPPPITPPSGPPTS 484

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530405578   493 GTASLIPLQSGSFALLQLPGqkPVPSSILQHVASLQMKRESqnPDQKDETNS 544
Cdd:pfam03154  485 TSSAMPGIQPPSSASVSSSG--PVPAAVSCPLPPVQIKEEA--LDEAEEPES 532
 
Name Accession Description Interval E-value
bHLHzip_MGA cd18911
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) and ...
 987-1051 2.17e-33

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) and similar proteins; MGA, also termed MAX dimerization protein 5 (MAD5), is a dual specificity T-box/ bHLHzip transcription factor that regulates the expression of both Max-network and T-box family target genes. It contains a Myc-like bHLHZip motif and requires heterodimerization with Max for binding to the preferred Myc-Max-binding site CACGTG. In addition to the bHLHZip domain, MGA harbors a second DNA-binding domain, the T-box or T-domain. It thus binds the preferred Brachyury-binding sequence and represses transcription of reporter genes containing promoter-proximal Brachyury-binding sites.


Pssm-ID: 381481  Cd Length: 65  Bit Score: 123.36  E-value: 2.17e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLT 1051
Cdd:cd18911     1 RRTHTANERRRRNEMRDLFEKLKRTLGLHNLPKVSKYYILKQAFEEIQGLTDQADRLIGQKTLLT 65
HLH pfam00010
Helix-loop-helix DNA-binding domain;
986-1037 3.57e-09

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 54.00  E-value: 3.57e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 530405578   986 YRRTHTANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLT 1037
Cdd:pfam00010    1 RREAHNERERRRRDRINDAFDELRELLpTLPPDKKLSKAEILRLAIEYIKHLQ 53
HLH smart00353
helix loop helix domain;
991-1042 7.37e-06

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 44.52  E-value: 7.37e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 530405578    991 TANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLTDQADK 1042
Cdd:smart00353    1 NARERRRRRKINEAFDELRSLLpTLPKNKKLSKAEILRLAIEYIKSLQEELQK 53
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 48-366 2.52e-05

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 48.80  E-value: 2.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578    48 ASRKPRTLLPSTSNSKMASSSGTATNRP-GKNLKAfvPAKRPIAARPSPGGVFTQfvmskvgalqqkiPGVSTPQTLAGT 126
Cdd:pfam17823   65 AAPAPVTLTKGTSAAHLNSTEVTAEHTPhGTDLSE--PATREGAADGAASRALAA-------------AASSSPSSAAQS 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   127 QKFSIRPSPvmvvTPVVSSEPVQVCSPVTAAVTTTTPQVFLENTTA--VTPMTAISDVETKETTYSSGATTTGVVEVSET 204
Cdd:pfam17823  130 LPAAIAALP----SEAFSAPRAAACRANASAAPRAAIAAASAPHAAspAPRTAASSTTAASSTTAASSAPTTAASSAPAT 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   205 NTSTSVTSTQstatvnltkTTGITTPVASVAfpkslVASPSTITlPVASTASTSLVVVTAAAsssmVTTPTSSLGSVPII 284
Cdd:pfam17823  206 LTPARGISTA---------ATATGHPAAGTA-----LAAVGNSS-PAAGTVTAAVGTVTPAA----LATLAAAAGTVASA 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   285 LSGINGSPPVSQRPENAAQIPVATPQVSPNTVKRAGPRLLLIPVQqgspTLRPVSNTqlqghrmvlQPVRSPSGMNLFRH 364
Cdd:pfam17823  267 AGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVS----TDQPVHNT---------AGEPTPSPSNTTLE 333


                   ..
gi 530405578   365 PN 366
Cdd:pfam17823  334 PN 335
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 222-544 2.23e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   222 TKTTGITTPVASVAFPKSLVASPSTITLPVASTASTSLVVVTAAASSSMVTTPTSSLGSVPIILSGINGSPPVSQRPENA 301
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPP 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   302 AQ---IPVATPQVSPNTVK---------------RAGPRLLLIPV-----------QQGSPTLRPVSNTQLQGHRMVLQP 352
Cdd:pfam03154  249 LQpmtQPPPPSQVSPQPLPqpslhgqmppmphslQTGPSHMQHPVppqpfpltpqsSQSQVPPGPSPAAPGQSQQRIHTP 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   353 VRSPSGMNL------------FRHPNGQIVQLLPLHQLrgSNTQPNLQPVMFRNPGSV-MGIRLPAP------SKPSETP 413
Cdd:pfam03154  329 PSQSQLQSQqppreqplppapLSMPHIKPPPTTPIPQL--PNPQSHKHPPHLSGPSPFqMNSNLPPPpalkplSSLSTHH 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   414 PSSTSSSAFSVMNPVIQAVGSSSAVNVITQAPSLLSSGASFVSQAGTLTLRISPPEPQ-SFASktGSETKITYSSGGQPV 492
Cdd:pfam03154  407 PPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQhPFVP--GGPPPITPPSGPPTS 484

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530405578   493 GTASLIPLQSGSFALLQLPGqkPVPSSILQHVASLQMKRESqnPDQKDETNS 544
Cdd:pfam03154  485 TSSAMPGIQPPSSASVSSSG--PVPAAVSCPLPPVQIKEEA--LDEAEEPES 532
 
Name Accession Description Interval E-value
bHLHzip_MGA cd18911
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) and ...
 987-1051 2.17e-33

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) and similar proteins; MGA, also termed MAX dimerization protein 5 (MAD5), is a dual specificity T-box/ bHLHzip transcription factor that regulates the expression of both Max-network and T-box family target genes. It contains a Myc-like bHLHZip motif and requires heterodimerization with Max for binding to the preferred Myc-Max-binding site CACGTG. In addition to the bHLHZip domain, MGA harbors a second DNA-binding domain, the T-box or T-domain. It thus binds the preferred Brachyury-binding sequence and represses transcription of reporter genes containing promoter-proximal Brachyury-binding sites.


Pssm-ID: 381481  Cd Length: 65  Bit Score: 123.36  E-value: 2.17e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLT 1051
Cdd:cd18911     1 RRTHTANERRRRNEMRDLFEKLKRTLGLHNLPKVSKYYILKQAFEEIQGLTDQADRLIGQKTLLT 65
bHLHzip_MGA_like cd19682
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) ...
 987-1051 1.66e-21

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) family; The MGA family includes MGA, Schizosaccharomyces pombe ESC1 (spESC1) and similar proteins. MGA, also termed MAX dimerization protein 5 (MAD5), is a dual specificity T-box/ bHLHzip transcription factor that regulates the expression of both Max-network and T-box family target genes. It contains a Myc-like bHLHZip motif and requires heterodimerization with Max for binding to the preferred Myc-Max-binding site CACGTG. In addition to the bHLHZip domain, MGA harbors a second DNA-binding domain, the T-box or T-domain. It thus binds the preferred Brachyury-binding sequence and represses transcription of reporter genes containing promoter-proximal Brachyury-binding sites. spESC1 is a bHLHzip protein with homology to human MyoD and Myf-5 myogenic differentiation inducers. It is involved in the sexual differentiation process.


Pssm-ID: 381525 [Multi-domain]  Cd Length: 65  Bit Score: 89.64  E-value: 1.66e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLT 1051
Cdd:cd19682     1 RLRHKKRERERRSELRELFDKLKQLLGLDSDEKASKLAVLTEAIEEIQQLKREEDELQKEKARLT 65
bHLHzip_Myc cd11400
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a ...
 987-1064 7.61e-10

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a member of the bHLHzip family of transcription factors that play important roles in the control of normal cell proliferation, growth, survival and differentiation. All Myc isoforms contain two independently functioning polypeptide chain regions: N-terminal transactivating residues and a C-terminal bHLHzip segment. The bHLHzip family of bHLH transcription factors are characterized by a highly conserved N-terminal basic region that may bind DNA at a consensus hexanucleotide sequence known as the E-box (CANNTG) followed by HLH and leucine zipper motifs that may interact with other proteins to form homo- and heterodimers. Myc heterodimerizes with Max enabling specific binding to E-box DNA sequences in the promoters of target genes. The Myc proto-oncoprotein family includes at least five different functional members: c-, N-, L-, S- and B-Myc (which is lacking the bHLH domain).


Pssm-ID: 381406 [Multi-domain]  Cd Length: 80  Bit Score: 56.79  E-value: 7.61e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLTRKRNILIRKVSSL 1064
Cdd:cd11400     2 RRLHNVLERQRRNDLKNSFEKLRDLVpELADNEKASKVVILKKATEYIKQLQQEEKKLEKEKDKLKARNEQLRKKLERL 80
bHLHzip_spESC1_like cd19690
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Schizosaccharomyces pombe ESC1 (spESC1) ...
 987-1043 1.07e-09

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Schizosaccharomyces pombe ESC1 (spESC1) and similar proteins; spESC1 is a bHLHzip protein with homology to human MyoD and Myf-5 myogenic differentiation inducers. It is involved in the sexual differentiation process.


Pssm-ID: 381533  Cd Length: 65  Bit Score: 55.93  E-value: 1.07e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKL 1043
Cdd:cd19690     1 RVSHKLAERKRRKEMKELFEDLRDALPQERGTKASKWEILTKAISYIQQLKRHIREL 57
HLH pfam00010
Helix-loop-helix DNA-binding domain;
986-1037 3.57e-09

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 54.00  E-value: 3.57e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 530405578   986 YRRTHTANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLT 1037
Cdd:pfam00010    1 RREAHNERERRRRDRINDAFDELRELLpTLPPDKKLSKAEILRLAIEYIKHLQ 53
bHLH_SF cd00083
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
 994-1036 9.76e-08

basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators that are found in organisms from yeast to humans. Members of the bHLH superfamily have two highly conserved and functionally distinct regions. The basic part is at the amino end of the bHLH that may bind DNA to a consensus hexanucleotide sequence known as the E box (CANNTG). Different families of bHLH proteins recognize different E-box consensus sequences. At the carboxyl-terminal end of the region is the HLH region that interacts with other proteins to form homo- and heterodimers. bHLH proteins function as a diverse set of regulatory factors because they recognize different DNA sequences and dimerize with different proteins. The bHLH proteins can be divided to cell-type specific and widely expressed proteins. The cell-type specific members of bHLH superfamily are involved in cell-fate determination and act in neurogenesis, cardiogenesis, myogenesis, and hematopoiesis.


Pssm-ID: 381392 [Multi-domain]  Cd Length: 46  Bit Score: 49.83  E-value: 9.76e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 530405578  994 ERRRRGEMRDLFEKLKITLGLLH-SSKVSKSLILTRAFSEIQGL 1036
Cdd:cd00083     1 ERRRRDKINDAFEELKRLLPELPdSKKLSKASILQKAVEYIREL 44
bHLHzip_L-Myc cd11457
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in L-Myc and similar proteins; L-Myc, ...
 987-1066 1.33e-06

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in L-Myc and similar proteins; L-Myc, also termed Class E basic helix-loop-helix protein 38 (bHLHe38), or protein L-Myc-1, or V-myc myelocytomatosis viral oncogene homolog, is a bHLHZip oncoprotein belonging to the Myc oncogene protein family. It binds DNA as a heterodimer with MAX. L-Myc is co-expressed with another Myc family member and has weaker transformation/transactivation activities. L-Myc knockout mouse did not exhibit any phenotypic abnormalities.


Pssm-ID: 381463 [Multi-domain]  Cd Length: 89  Bit Score: 47.87  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLTRKRNILIRKVSSLS 1065
Cdd:cd11457     8 RKNHNFLERKRRNDLRSRFLALRDEVpGLASCSKTPKVVILSKATEYLRGLVSAERRMAAEKRQLKSRQQQLLRRIAQLK 87


                  .
gi 530405578 1066 G 1066
Cdd:cd11457    88 G 88
bHLHzip_Mlx_like cd11404
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, ...
 987-1054 3.81e-06

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, also termed Class D basic helix-loop-helix protein 13 (bHLHd13), or Max-like bHLHZip protein, or protein BigMax, or transcription factor-like protein 4, is a Max-like bHLHZip transcription regulator that interacts with the Max network of transcription factors. It forms a sequence-specific DNA-binding protein complex with some member of Mad family (Mad1 and Mad4) and Mondo family but not the Myc family and bind the E-box DNA to control transcription. The family also includes Saccharomyces cerevisiae INO4, which is a bHLH transcriptional activator of phospholipid synthetic genes (such as INO1, CHO1/PSS, CHO2/PEM1, OPI3/PEM2, etc.). It is required for de-repression of phospholipid biosynthetic gene expression in response to inositol deprivation in yeast.


Pssm-ID: 381410 [Multi-domain]  Cd Length: 70  Bit Score: 46.14  E-value: 3.81e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLTRKR 1054
Cdd:cd11404     3 RLNHVRSEKKRRELIKKGYDELCALVPGLDPQKRTKADILQKAADWIQELKEENEKLEEQLDELKEAA 70
HLH smart00353
helix loop helix domain;
991-1042 7.37e-06

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 44.52  E-value: 7.37e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 530405578    991 TANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLTDQADK 1042
Cdd:smart00353    1 NARERRRRRKINEAFDELRSLLpTLPKNKKLSKAEILRLAIEYIKSLQEELQK 53
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 48-366 2.52e-05

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 48.80  E-value: 2.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578    48 ASRKPRTLLPSTSNSKMASSSGTATNRP-GKNLKAfvPAKRPIAARPSPGGVFTQfvmskvgalqqkiPGVSTPQTLAGT 126
Cdd:pfam17823   65 AAPAPVTLTKGTSAAHLNSTEVTAEHTPhGTDLSE--PATREGAADGAASRALAA-------------AASSSPSSAAQS 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   127 QKFSIRPSPvmvvTPVVSSEPVQVCSPVTAAVTTTTPQVFLENTTA--VTPMTAISDVETKETTYSSGATTTGVVEVSET 204
Cdd:pfam17823  130 LPAAIAALP----SEAFSAPRAAACRANASAAPRAAIAAASAPHAAspAPRTAASSTTAASSTTAASSAPTTAASSAPAT 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   205 NTSTSVTSTQstatvnltkTTGITTPVASVAfpkslVASPSTITlPVASTASTSLVVVTAAAsssmVTTPTSSLGSVPII 284
Cdd:pfam17823  206 LTPARGISTA---------ATATGHPAAGTA-----LAAVGNSS-PAAGTVTAAVGTVTPAA----LATLAAAAGTVASA 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   285 LSGINGSPPVSQRPENAAQIPVATPQVSPNTVKRAGPRLLLIPVQqgspTLRPVSNTqlqghrmvlQPVRSPSGMNLFRH 364
Cdd:pfam17823  267 AGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVS----TDQPVHNT---------AGEPTPSPSNTTLE 333


                   ..
gi 530405578   365 PN 366
Cdd:pfam17823  334 PN 335
bHLHzip_N-Myc_like cd11456
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in N-Myc and similar proteins; N-Myc, ...
 987-1061 3.01e-05

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in N-Myc and similar proteins; N-Myc, also termed Class E basic helix-loop-helix protein 37 (bHLHe37), is a bHLHZip proto-oncogene protein that positively regulates the transcription of MYCNOS in neuroblastoma cells. It is also essential during embryonic development. N-Myc has a critical role in regulating the switch between proliferation and differentiation of progenitor cells. It binds DNA as a heterodimer with MAX. The family also includes S-Myc, encoded by rat or mouse intronless myc gene, which has apoptosis-inducing activity.


Pssm-ID: 381462 [Multi-domain]  Cd Length: 87  Bit Score: 44.12  E-value: 3.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLTRKRNILIRKV 1061
Cdd:cd11456     6 RRNHNILERQRRNDLRSSFLTLRDHVpELVKNEKAAKVVILKKATEYVHSLQAEEQKLLLEKEKLQARQQQLLKKI 81
bHLHzip_Max cd11406
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max and similar proteins; Max, ...
 987-1034 1.53e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max and similar proteins; Max, also termed Class D basic helix-loop-helix protein 4 (bHLHd4), or Myc-associated factor X, is a bHLHZip transcription regulator that forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a transcriptional repressor. Max homodimer bind DNA but is transcriptionally inactive. Targeted deletion of max results in early embryonic lethality in mice.


Pssm-ID: 381412  Cd Length: 69  Bit Score: 41.57  E-value: 1.53e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQ 1034
Cdd:cd11406     2 RAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILKKATEYIQ 49
bHLHzip_Mad4 cd18929
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 4 (Mad4) and ...
 986-1065 1.93e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 4 (Mad4) and similar proteins; Mad4, also termed Max dimerization protein 4, or Max dimerizer 4 (MXD4), or Class C basic helix-loop-helix protein 12 (bHLHc12), or Max-interacting transcriptional repressor MAD4, is a bHLHZip Max-interacting transcriptional repressor that suppresses c-myc dependent transformation and is expressed during neural and epidermal differentiation. It is regulated by a transcriptional repressor complex that contains Miz-1 and c-Myc.


Pssm-ID: 381499 [Multi-domain]  Cd Length: 88  Bit Score: 41.92  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578  986 YRRTHTANERRRRGEMRDLFEKLK--ITLGLLHSSKVSKSLiLTRAFSEIQGLTDQADKLIGQKNLLTRKRNILIRKVSS 1063
Cdd:cd18929     2 NRSSHNELEKHRRAKLRLYLEQLKqlVPLGPDSTRHTTLSL-LKRAKMHIKKLEEQDRKALNIKEQLQREHRYLKRRLEQ 80


                  ..
gi 530405578 1064 LS 1065
Cdd:cd18929    81 LS 82
bHLHzip_USF3 cd18910
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in basic helix-loop-helix ...
 984-1044 5.13e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in basic helix-loop-helix domain-containing protein USF3 and similar proteins; USF3, also termed upstream transcription factor 3, is a bHLHzip protein that is involved in the negative regulation of epithelial-mesenchymal transition, the process by which epithelial cells lose their polarity and adhesion properties to become mesenchymal cells with enhanced migration and invasive properties.


Pssm-ID: 381480  Cd Length: 65  Bit Score: 39.98  E-value: 5.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530405578  984 AYYRRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKLI 1044
Cdd:cd18910     3 EKKRESHNEVERRRKDKINAGINKIGELLPDRDAKKQSKNMILEQAYKYIVELKKKNDKLL 63
bHLHzip_c-Myc cd11458
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in c-Myc and similar proteins; c-Myc, ...
 987-1064 9.79e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in c-Myc and similar proteins; c-Myc, also termed Myc proto-oncogene protein, or Class E basic helix-loop-helix protein 39 (bHLHe39), or transcription factor p64, a bHLHZip proto-oncogene protein that functions as a transcription factor, which binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. It activates the transcription of growth-related genes.


Pssm-ID: 381464 [Multi-domain]  Cd Length: 84  Bit Score: 39.86  E-value: 9.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLTRKRNILIRKVSSL 1064
Cdd:cd11458     6 RRTHNVLERQRRNELKLSFFALRDQIpEVANNEKAPKVVILKKATEYILSMQADEQRLISEKEQLRRRREQLKHRLEQL 84
bHLHzip_Mad cd11401
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Mad family; Members of the Mad ...
 987-1061 1.25e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Mad family; Members of the Mad family (Mad1, Mxi, Mad3, and Mad4) bear the bHLHzip domain (also known as basic-helix-loop-helix-leucine-zipper or bHLH-LZ domain), which mediates heterodimerization to Max and the sequence-specific DNA binding ability to E-box DNA. Mad family proteins can repress transcription at the E-box through their interaction with co-repressors. Mad family proteins antagonize Myc function in transactivation and transformation and they are growth/tumor suppressors. The developmental phenotypes of the individual Mad family member knockout mice are relatively mild- all these mice have been shown to be viable and normal.


Pssm-ID: 381407 [Multi-domain]  Cd Length: 76  Bit Score: 39.12  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLK------------ITLGLlhsskvsksliLTRAFSEIQGLTDQADKLIGQKNLLTRKR 1054
Cdd:cd11401     1 RSTHNELEKNRRAHLRLCLERLKelvplgpdatrhTTLSL-----------LTKAKAYIKNLEDKEKRQRQQKEQLRREQ 69


                  ....*..
gi 530405578 1055 NILIRKV 1061
Cdd:cd11401    70 RELKRRL 76
bHLHzip_MLXIP_like cd11405
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP), ...
 987-1056 1.86e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP), MLX-interacting protein-like (MLXIPL) and similar proteins; The family includes MLXIP and MLXIPL. MLXIP, also termed Class E basic helix-loop-helix protein 36 (bHLHe36), or transcriptional activator MondoA, is a bHLHZip transcriptional activator that binds DNA as a heterodimer with Mlx. It binds to the canonical E box sequence 5'-CACGTG-3' and plays a role in transcriptional activation of glycolytic target genes. MLXIP is most highly expressed in skeletal muscle and functions as an indirect glucose sensor, by sensing glucose 6-phosphate and shuttling between the nucleus and the cytoplasm. MLXIPL, also termed carbohydrate-responsive element-binding protein (ChREBP), or Class D basic helix-loop-helix protein 14 (bHLHd14), or MLX interactor, or WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), is a bHLHZip transcriptional factor integral to the regulation of glycolysis and lipogenesis in the liver. It forms heterodimers with the bHLHZip protein Mlx to bind the DNA sequence 5'-CACGTG-3'.


Pssm-ID: 381411 [Multi-domain]  Cd Length: 74  Bit Score: 38.41  E-value: 1.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLK---ITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLtrKRNI 1056
Cdd:cd11405     4 RLSHISAEQKRRFNIKSGFDTLQsliPSLGQNPNQKVSKAAMLQKAAEYIKSLKRERQQMQEEAEQL--RQEI 74
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 222-544 2.23e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   222 TKTTGITTPVASVAFPKSLVASPSTITLPVASTASTSLVVVTAAASSSMVTTPTSSLGSVPIILSGINGSPPVSQRPENA 301
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPP 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   302 AQ---IPVATPQVSPNTVK---------------RAGPRLLLIPV-----------QQGSPTLRPVSNTQLQGHRMVLQP 352
Cdd:pfam03154  249 LQpmtQPPPPSQVSPQPLPqpslhgqmppmphslQTGPSHMQHPVppqpfpltpqsSQSQVPPGPSPAAPGQSQQRIHTP 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   353 VRSPSGMNL------------FRHPNGQIVQLLPLHQLrgSNTQPNLQPVMFRNPGSV-MGIRLPAP------SKPSETP 413
Cdd:pfam03154  329 PSQSQLQSQqppreqplppapLSMPHIKPPPTTPIPQL--PNPQSHKHPPHLSGPSPFqMNSNLPPPpalkplSSLSTHH 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405578   414 PSSTSSSAFSVMNPVIQAVGSSSAVNVITQAPSLLSSGASFVSQAGTLTLRISPPEPQ-SFASktGSETKITYSSGGQPV 492
Cdd:pfam03154  407 PPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQhPFVP--GGPPPITPPSGPPTS 484

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530405578   493 GTASLIPLQSGSFALLQLPGqkPVPSSILQHVASLQMKRESqnPDQKDETNS 544
Cdd:pfam03154  485 TSSAMPGIQPPSSASVSSSG--PVPAAVSCPLPPVQIKEEA--LDEAEEPES 532
bHLHzip_Mlx cd19687
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) and similar ...
 987-1053 4.04e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) and similar proteins; Mlx, also termed Class D basic helix-loop-helix protein 13 (bHLHd13), or Max-like bHLHZip protein, or protein BigMax, or transcription factor-like protein 4, is a Max-like bHLHZip transcription regulator that interacts with the Max network of transcription factors. It forms a sequence-specific DNA-binding protein complex with some member of Mad family (Mad1 and Mad4) and Mondo family but not the Myc family and bind the E-box DNA to control transcription.


Pssm-ID: 381530 [Multi-domain]  Cd Length: 76  Bit Score: 37.79  E-value: 4.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLKITLGLLH------SSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLtRK 1053
Cdd:cd19687     3 REAHTQAEQKRRDAIKKGYDDLQDIVPTCQqqddigSQKLSKATILQRSIDYIQFLHQQKKKQEEELSAL-RK 74
bHLH_ScINO2_like cd11388
basic helix-loop-helix (bHLH) domain found in Saccharomyces cerevisiae protein INO2 and ...
 987-1043 6.50e-03

basic helix-loop-helix (bHLH) domain found in Saccharomyces cerevisiae protein INO2 and similar proteins; INO2 is a positive regulatory factor required for depression of the co-regulated phospholipid biosynthetic enzymes in Saccharomyces cerevisiae. It is also involved in the expression of ITR1.


Pssm-ID: 381394  Cd Length: 68  Bit Score: 36.95  E-value: 6.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLkitLGLLH------SSKVSKSLILTRAFSEIQGLTDQADKL 1043
Cdd:cd11388     4 KWKHVEAEKKRRNQIKKGFEDL---INLINyprnnnEKRISKSELLNKAVDDIRGLLKANEQL 63
bHLHzip_Mad1 cd18931
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max-associated protein 1 (Mad1) ...
 987-1064 7.62e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max-associated protein 1 (Mad1) and similar proteins; Mad1, also termed Max dimerization protein 1 (MXD1), or Max dimerizer 1, or protein MAD, is a bHLHZip transcriptional repressor that binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. It thus antagonizes MYC transcriptional activity by competing for MAX.


Pssm-ID: 381501 [Multi-domain]  Cd Length: 80  Bit Score: 36.91  E-value: 7.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530405578  987 RRTHTANERRRRGEMRDLFEKLKITLGL-LHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLTRKRNILIRKVSSL 1064
Cdd:cd18931     2 RSTHNEMEKNRRAHLRLCLEKLKMLVPLgPESNRHTTLSLLMKAKLHIKKLEDSDRKAVHQIDQLQREQRHLKRQLEKL 80
 
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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