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Conserved domains on  [gi|578826753|ref|XP_006720508|]
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MAX gene-associated protein isoform X16 [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 ...
 2018-2082 3.76e-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: 3.76e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578826753 2018 RRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLT 2082
Cdd:cd18911     1 RRTHTANERRRRNEMRDLFEKLKRTLGLHNLPKVSKYYILKQAFEEIQGLTDQADRLIGQKTLLT 65
MGA_dom super family cl24582
MGA, conserved domain; This domain can be found in the MAX gene-associated protein (Mga), ...
 584-625 1.13e-13

MGA, conserved domain; This domain can be found in the MAX gene-associated protein (Mga), which is a dual-specificity transcription factor that contains both a bHLHZip domain and a T-box domain and is able to bind to and regulate transcriptional targets through both E-box sites as well as T-box-binding elements (TBEs).


The actual alignment was detected with superfamily member pfam16059:

Pssm-ID: 464998  Cd Length: 51  Bit Score: 67.51  E-value: 1.13e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 578826753   584 RKRAPPCNNDFCRLGCVCSSLA-LEKRQPAHCRRPDCMFGCTC 625
Cdd:pfam16059    2 KDAKKPCDKDYCQLGCVCDSLAgTRPPKREHCGRADCVLGCVC 44
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 1062-1363 2.61e-07

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: 56.12  E-value: 2.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1062 STLSTVISKVASNAKVAasrkPRTLLPSTSNSKMASSSGTATNRPGKNLKAFVPAKRPIAARPSPGGVFTQFVMSKVGAL 1141
Cdd:pfam17823  128 QSLPAAIAALPSEAFSA----PRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAP 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1142 QQKIP--GVSTPQTLAGTQKFSIRPSPVMVVTPVVSSEPVQVCSPVTAAVTTTTPQVFLENTTAVTPMTAISDVETKETT 1219
Cdd:pfam17823  204 ATLTParGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRLSPA 283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1220 YSSGATTTGVVEVSETNTSTSVTSTQSTATVNLTKTTGITTPVasvafPKSLVASPSTitlpVASTASTSLVVVTaaasS 1299
Cdd:pfam17823  284 KHMPSDTMARNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPS-----PSNTTLEPNT----PKSVASTNLAVVT----T 350

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578826753  1300 SMVTTPTSSLGSVPIilsgingsPPVSQRPENAAQIPVATPQVSPNTVKRAGPRLLLIPVQQGS 1363
Cdd:pfam17823  351 TKAQAKEPSASPVPV--------LHTSMIPEVEATSPTTQPSPLLPTQGAAGPGILLAPEQVAT 406
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1253-1575 6.73e-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: 42.06  E-value: 6.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1253 TKTTGITTPVASVAFPKSLVASPSTITLPVASTASTSLVVVTAAASSSMVTTPTSSLGSVPIILSGINGSPPVSQRPENA 1332
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPP 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1333 AQ---IPVATPQVSPNTVK---------------RAGPRLLLIPV-----------QQGSPTLRPVSNTQLQGHRMVLQP 1383
Cdd:pfam03154  249 LQpmtQPPPPSQVSPQPLPqpslhgqmppmphslQTGPSHMQHPVppqpfpltpqsSQSQVPPGPSPAAPGQSQQRIHTP 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1384 VRSPSGMNL------------FRHPNGQIVQLLPLHQLrgSNTQPNLQPVMFRNPGSV-MGIRLPAP------SKPSETP 1444
Cdd:pfam03154  329 PSQSQLQSQqppreqplppapLSMPHIKPPPTTPIPQL--PNPQSHKHPPHLSGPSPFqMNSNLPPPpalkplSSLSTHH 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1445 PSSTSSSAFSVMNPVIQAVGSSSAVNVITQAPSLLSSGASFVSQAGTLTLRISPPEPQ-SFASktGSETKITYSSGGQPV 1523
Cdd:pfam03154  407 PPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQhPFVP--GGPPPITPPSGPPTS 484

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578826753  1524 GTASLIPLQSGSFALLQLPGqkPVPSSILQHVASLQMKRESqnPDQKDETNS 1575
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 ...
 2018-2082 3.76e-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: 3.76e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578826753 2018 RRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLT 2082
Cdd:cd18911     1 RRTHTANERRRRNEMRDLFEKLKRTLGLHNLPKVSKYYILKQAFEEIQGLTDQADRLIGQKTLLT 65
MGA_dom pfam16059
MGA, conserved domain; This domain can be found in the MAX gene-associated protein (Mga), ...
 584-625 1.13e-13

MGA, conserved domain; This domain can be found in the MAX gene-associated protein (Mga), which is a dual-specificity transcription factor that contains both a bHLHZip domain and a T-box domain and is able to bind to and regulate transcriptional targets through both E-box sites as well as T-box-binding elements (TBEs).


Pssm-ID: 464998  Cd Length: 51  Bit Score: 67.51  E-value: 1.13e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 578826753   584 RKRAPPCNNDFCRLGCVCSSLA-LEKRQPAHCRRPDCMFGCTC 625
Cdd:pfam16059    2 KDAKKPCDKDYCQLGCVCDSLAgTRPPKREHCGRADCVLGCVC 44
HLH pfam00010
Helix-loop-helix DNA-binding domain;
2017-2068 8.47e-09

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 53.62  E-value: 8.47e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 578826753  2017 YRRTHTANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLT 2068
Cdd:pfam00010    1 RREAHNERERRRRDRINDAFDELRELLpTLPPDKKLSKAEILRLAIEYIKHLQ 53
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 1062-1363 2.61e-07

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: 56.12  E-value: 2.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1062 STLSTVISKVASNAKVAasrkPRTLLPSTSNSKMASSSGTATNRPGKNLKAFVPAKRPIAARPSPGGVFTQFVMSKVGAL 1141
Cdd:pfam17823  128 QSLPAAIAALPSEAFSA----PRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAP 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1142 QQKIP--GVSTPQTLAGTQKFSIRPSPVMVVTPVVSSEPVQVCSPVTAAVTTTTPQVFLENTTAVTPMTAISDVETKETT 1219
Cdd:pfam17823  204 ATLTParGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRLSPA 283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1220 YSSGATTTGVVEVSETNTSTSVTSTQSTATVNLTKTTGITTPVasvafPKSLVASPSTitlpVASTASTSLVVVTaaasS 1299
Cdd:pfam17823  284 KHMPSDTMARNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPS-----PSNTTLEPNT----PKSVASTNLAVVT----T 350

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578826753  1300 SMVTTPTSSLGSVPIilsgingsPPVSQRPENAAQIPVATPQVSPNTVKRAGPRLLLIPVQQGS 1363
Cdd:pfam17823  351 TKAQAKEPSASPVPV--------LHTSMIPEVEATSPTTQPSPLLPTQGAAGPGILLAPEQVAT 406
HLH smart00353
helix loop helix domain;
2022-2073 1.29e-05

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 44.52  E-value: 1.29e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 578826753   2022 TANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLTDQADK 2073
Cdd:smart00353    1 NARERRRRRKINEAFDELRSLLpTLPKNKKLSKAEILRLAIEYIKSLQEELQK 53
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1253-1575 6.73e-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: 42.06  E-value: 6.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1253 TKTTGITTPVASVAFPKSLVASPSTITLPVASTASTSLVVVTAAASSSMVTTPTSSLGSVPIILSGINGSPPVSQRPENA 1332
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPP 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1333 AQ---IPVATPQVSPNTVK---------------RAGPRLLLIPV-----------QQGSPTLRPVSNTQLQGHRMVLQP 1383
Cdd:pfam03154  249 LQpmtQPPPPSQVSPQPLPqpslhgqmppmphslQTGPSHMQHPVppqpfpltpqsSQSQVPPGPSPAAPGQSQQRIHTP 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1384 VRSPSGMNL------------FRHPNGQIVQLLPLHQLrgSNTQPNLQPVMFRNPGSV-MGIRLPAP------SKPSETP 1444
Cdd:pfam03154  329 PSQSQLQSQqppreqplppapLSMPHIKPPPTTPIPQL--PNPQSHKHPPHLSGPSPFqMNSNLPPPpalkplSSLSTHH 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1445 PSSTSSSAFSVMNPVIQAVGSSSAVNVITQAPSLLSSGASFVSQAGTLTLRISPPEPQ-SFASktGSETKITYSSGGQPV 1523
Cdd:pfam03154  407 PPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQhPFVP--GGPPPITPPSGPPTS 484

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578826753  1524 GTASLIPLQSGSFALLQLPGqkPVPSSILQHVASLQMKRESqnPDQKDETNS 1575
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 ...
 2018-2082 3.76e-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: 3.76e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578826753 2018 RRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLT 2082
Cdd:cd18911     1 RRTHTANERRRRNEMRDLFEKLKRTLGLHNLPKVSKYYILKQAFEEIQGLTDQADRLIGQKTLLT 65
bHLHzip_MGA_like cd19682
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) ...
 2018-2082 2.82e-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: 89.26  E-value: 2.82e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578826753 2018 RRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLT 2082
Cdd:cd19682     1 RLRHKKRERERRSELRELFDKLKQLLGLDSDEKASKLAVLTEAIEEIQQLKREEDELQKEKARLT 65
MGA_dom pfam16059
MGA, conserved domain; This domain can be found in the MAX gene-associated protein (Mga), ...
 584-625 1.13e-13

MGA, conserved domain; This domain can be found in the MAX gene-associated protein (Mga), which is a dual-specificity transcription factor that contains both a bHLHZip domain and a T-box domain and is able to bind to and regulate transcriptional targets through both E-box sites as well as T-box-binding elements (TBEs).


Pssm-ID: 464998  Cd Length: 51  Bit Score: 67.51  E-value: 1.13e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 578826753   584 RKRAPPCNNDFCRLGCVCSSLA-LEKRQPAHCRRPDCMFGCTC 625
Cdd:pfam16059    2 KDAKKPCDKDYCQLGCVCDSLAgTRPPKREHCGRADCVLGCVC 44
bHLHzip_Myc cd11400
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a ...
 2018-2095 1.31e-09

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: 1.31e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578826753 2018 RRTHTANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLTRKRNILIRKVSSL 2095
Cdd:cd11400     2 RRLHNVLERQRRNDLKNSFEKLRDLVpELADNEKASKVVILKKATEYIKQLQQEEKKLEKEKDKLKARNEQLRKKLERL 80
bHLHzip_spESC1_like cd19690
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Schizosaccharomyces pombe ESC1 (spESC1) ...
 2018-2074 1.58e-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: 1.58e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578826753 2018 RRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKL 2074
Cdd:cd19690     1 RVSHKLAERKRRKEMKELFEDLRDALPQERGTKASKWEILTKAISYIQQLKRHIREL 57
HLH pfam00010
Helix-loop-helix DNA-binding domain;
2017-2068 8.47e-09

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 53.62  E-value: 8.47e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 578826753  2017 YRRTHTANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLT 2068
Cdd:pfam00010    1 RREAHNERERRRRDRINDAFDELRELLpTLPPDKKLSKAEILRLAIEYIKHLQ 53
bHLH_SF cd00083
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
 2025-2067 1.83e-07

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: 49.44  E-value: 1.83e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 578826753 2025 ERRRRGEMRDLFEKLKITLGLLH-SSKVSKSLILTRAFSEIQGL 2067
Cdd:cd00083     1 ERRRRDKINDAFEELKRLLPELPdSKKLSKASILQKAVEYIREL 44
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 1062-1363 2.61e-07

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: 56.12  E-value: 2.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1062 STLSTVISKVASNAKVAasrkPRTLLPSTSNSKMASSSGTATNRPGKNLKAFVPAKRPIAARPSPGGVFTQFVMSKVGAL 1141
Cdd:pfam17823  128 QSLPAAIAALPSEAFSA----PRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAP 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1142 QQKIP--GVSTPQTLAGTQKFSIRPSPVMVVTPVVSSEPVQVCSPVTAAVTTTTPQVFLENTTAVTPMTAISDVETKETT 1219
Cdd:pfam17823  204 ATLTParGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRLSPA 283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1220 YSSGATTTGVVEVSETNTSTSVTSTQSTATVNLTKTTGITTPVasvafPKSLVASPSTitlpVASTASTSLVVVTaaasS 1299
Cdd:pfam17823  284 KHMPSDTMARNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPS-----PSNTTLEPNT----PKSVASTNLAVVT----T 350

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578826753  1300 SMVTTPTSSLGSVPIilsgingsPPVSQRPENAAQIPVATPQVSPNTVKRAGPRLLLIPVQQGS 1363
Cdd:pfam17823  351 TKAQAKEPSASPVPV--------LHTSMIPEVEATSPTTQPSPLLPTQGAAGPGILLAPEQVAT 406
bHLHzip_L-Myc cd11457
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in L-Myc and similar proteins; L-Myc, ...
 2018-2097 2.35e-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: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753 2018 RRTHTANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLTRKRNILIRKVSSLS 2096
Cdd:cd11457     8 RKNHNFLERKRRNDLRSRFLALRDEVpGLASCSKTPKVVILSKATEYLRGLVSAERRMAAEKRQLKSRQQQLLRRIAQLK 87


                  .
gi 578826753 2097 G 2097
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, ...
 2018-2085 6.50e-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: 6.50e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578826753 2018 RRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLTRKR 2085
Cdd:cd11404     3 RLNHVRSEKKRRELIKKGYDELCALVPGLDPQKRTKADILQKAADWIQELKEENEKLEEQLDELKEAA 70
HLH smart00353
helix loop helix domain;
2022-2073 1.29e-05

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 44.52  E-value: 1.29e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 578826753   2022 TANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLTDQADK 2073
Cdd:smart00353    1 NARERRRRRKINEAFDELRSLLpTLPKNKKLSKAEILRLAIEYIKSLQEELQK 53
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 1079-1397 2.21e-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: 49.96  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1079 ASRKPRTLLPSTSNSKMASSSGTATNRP-GKNLKAfvPAKRPIAARPSPGGVFTQfvmskvgalqqkiPGVSTPQTLAGT 1157
Cdd:pfam17823   65 AAPAPVTLTKGTSAAHLNSTEVTAEHTPhGTDLSE--PATREGAADGAASRALAA-------------AASSSPSSAAQS 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1158 QKFSIRPSPvmvvTPVVSSEPVQVCSPVTAAVTTTTPQVFLENTTA--VTPMTAISDVETKETTYSSGATTTGVVEVSET 1235
Cdd:pfam17823  130 LPAAIAALP----SEAFSAPRAAACRANASAAPRAAIAAASAPHAAspAPRTAASSTTAASSTTAASSAPTTAASSAPAT 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1236 NTSTSVTSTQstatvnltkTTGITTPVASVAfpkslVASPSTITlPVASTASTSLVVVTAAAsssmVTTPTSSLGSVPII 1315
Cdd:pfam17823  206 LTPARGISTA---------ATATGHPAAGTA-----LAAVGNSS-PAAGTVTAAVGTVTPAA----LATLAAAAGTVASA 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1316 LSGINGSPPVSQRPENAAQIPVATPQVSPNTVKRAGPRLLLIPVQqgspTLRPVSNTqlqghrmvlQPVRSPSGMNLFRH 1395
Cdd:pfam17823  267 AGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVS----TDQPVHNT---------AGEPTPSPSNTTLE 333


                   ..
gi 578826753  1396 PN 1397
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, ...
 2018-2092 4.24e-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: 4.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578826753 2018 RRTHTANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLTRKRNILIRKV 2092
Cdd:cd11456     6 RRNHNILERQRRNDLRSSFLTLRDHVpELVKNEKAAKVVILKKATEYVHSLQAEEQKLLLEKEKLQARQQQLLKKI 81
bHLHzip_Max cd11406
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in protein Max and similar proteins; Max, ...
 2018-2065 2.89e-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: 41.18  E-value: 2.89e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578826753 2018 RRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQ 2065
Cdd:cd11406     2 RAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILKKATEYIQ 49
bHLHzip_Mad4 cd18929
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-associated protein 4 (Mad4) and ...
 2017-2096 3.19e-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: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753 2017 YRRTHTANERRRRGEMRDLFEKLK--ITLGLLHSSKVSKSLiLTRAFSEIQGLTDQADKLIGQKNLLTRKRNILIRKVSS 2094
Cdd:cd18929     2 NRSSHNELEKHRRAKLRLYLEQLKqlVPLGPDSTRHTTLSL-LKRAKMHIKKLEEQDRKALNIKEQLQREHRYLKRRLEQ 80


                  ..
gi 578826753 2095 LS 2096
Cdd:cd18929    81 LS 82
bHLHzip_USF3 cd18910
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in basic helix-loop-helix ...
 2015-2075 1.12e-03

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: 39.59  E-value: 1.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578826753 2015 AYYRRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKLI 2075
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, ...
 2018-2095 1.23e-03

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: 1.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578826753 2018 RRTHTANERRRRGEMRDLFEKLKITL-GLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLTRKRNILIRKVSSL 2095
Cdd:cd11458     6 RRTHNVLERQRRNELKLSFFALRDQIpEVANNEKAPKVVILKKATEYILSMQADEQRLISEKEQLRRRREQLKHRLEQL 84
bHLHzip_MLXIP_like cd11405
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP), ...
 2018-2087 2.26e-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: 38.79  E-value: 2.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578826753 2018 RRTHTANERRRRGEMRDLFEKLK---ITLGLLHSSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLtrKRNI 2087
Cdd:cd11405     4 RLSHISAEQKRRFNIKSGFDTLQsliPSLGQNPNQKVSKAAMLQKAAEYIKSLKRERQQMQEEAEQL--RQEI 74
bHLHzip_Mad cd11401
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Mad family; Members of the Mad ...
 2018-2092 2.46e-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: 38.73  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753 2018 RRTHTANERRRRGEMRDLFEKLK------------ITLGLlhsskvsksliLTRAFSEIQGLTDQADKLIGQKNLLTRKR 2085
Cdd:cd11401     1 RSTHNELEKNRRAHLRLCLERLKelvplgpdatrhTTLSL-----------LTKAKAYIKNLEDKEKRQRQQKEQLRREQ 69


                  ....*..
gi 578826753 2086 NILIRKV 2092
Cdd:cd11401    70 RELKRRL 76
bHLHzip_Mlx cd19687
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) and similar ...
 2018-2084 5.57e-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: 5.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578826753 2018 RRTHTANERRRRGEMRDLFEKLKITLGLLH------SSKVSKSLILTRAFSEIQGLTDQADKLIGQKNLLtRK 2084
Cdd:cd19687     3 REAHTQAEQKRRDAIKKGYDDLQDIVPTCQqqddigSQKLSKATILQRSIDYIQFLHQQKKKQEEELSAL-RK 74
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1253-1575 6.73e-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: 42.06  E-value: 6.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1253 TKTTGITTPVASVAFPKSLVASPSTITLPVASTASTSLVVVTAAASSSMVTTPTSSLGSVPIILSGINGSPPVSQRPENA 1332
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPP 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1333 AQ---IPVATPQVSPNTVK---------------RAGPRLLLIPV-----------QQGSPTLRPVSNTQLQGHRMVLQP 1383
Cdd:pfam03154  249 LQpmtQPPPPSQVSPQPLPqpslhgqmppmphslQTGPSHMQHPVppqpfpltpqsSQSQVPPGPSPAAPGQSQQRIHTP 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1384 VRSPSGMNL------------FRHPNGQIVQLLPLHQLrgSNTQPNLQPVMFRNPGSV-MGIRLPAP------SKPSETP 1444
Cdd:pfam03154  329 PSQSQLQSQqppreqplppapLSMPHIKPPPTTPIPQL--PNPQSHKHPPHLSGPSPFqMNSNLPPPpalkplSSLSTHH 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578826753  1445 PSSTSSSAFSVMNPVIQAVGSSSAVNVITQAPSLLSSGASFVSQAGTLTLRISPPEPQ-SFASktGSETKITYSSGGQPV 1523
Cdd:pfam03154  407 PPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQhPFVP--GGPPPITPPSGPPTS 484

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578826753  1524 GTASLIPLQSGSFALLQLPGqkPVPSSILQHVASLQMKRESqnPDQKDETNS 1575
Cdd:pfam03154  485 TSSAMPGIQPPSSASVSSSG--PVPAAVSCPLPPVQIKEEA--LDEAEEPES 532
 
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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