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Conserved domains on  [gi|24645243|ref|NP_731308|]
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tango, isoform A [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bHLH-PAS_ARNT cd18947
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ...
 9-74 2.47e-42

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor nuclear translocator (ARNT) and similar proteins; ARNT, also termed Class E basic helix-loop-helix protein 2 (bHLHe2), or Dioxin receptor, nuclear translocator, or hypoxia-inducible factor 1-beta (HIF1b), or HIF-1-beta, or HIF1-beta, is a member of bHLH-PAS transcription regulators that acts as the heterodimeric partner for bHLH-PAS proteins such as aryl hydrocarbon receptor (AhR), hypoxia-inducible factor (HIF), and single-minded (SIM). These bHLH-PAS transcription complexes are involved in transcriptional responses to xenobiotic, hypoxia, and developmental pathways. Heterodimerization of bHLH-PAS proteins with ARNT is mediated by contacts between both the bHLH and the tandem PAS domains. ARNT use bHLH and/or PAS domains to interact with several transcriptional coactivators. It is required for activity of the aryl hydrocarbon (dioxin) receptor.


:

Pssm-ID: 381517  Cd Length: 65  Bit Score: 146.86  E-value: 2.47e-42
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24645243   9 KERFAsRENHCEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMKALRGTGNTSS 74
Cdd:cd18947   1 KERFA-RENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTST 65
PAS_11 super family cl37882
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
 282-384 2.56e-27

PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), which binds to an LXXLL motif in the C-terminal region of STAT6 (Signal transducer and activator of transcription 6).


The actual alignment was detected with superfamily member pfam14598:

Pssm-ID: 464214 [Multi-domain]  Cd Length: 110  Bit Score: 106.22  E-value: 2.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243   282 QSEFITRHAMDGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLKQKGQMFSLLYRARAKNSEYVWL 361
Cdd:pfam14598   1 TEQFTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDLRTAKSHLREIIQTRGRATSPSYRLRLRDGDFLSV 80

                          90       100
                  ....*....|....*....|...
gi 24645243   362 RTQAYAFLNPYTDEVEYIVCTNS 384
Cdd:pfam14598  81 HTKSKLFLNQNSNQQPFIMCTHT 103
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 90-154 3.99e-12

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


:

Pssm-ID: 214512  Cd Length: 67  Bit Score: 61.65  E-value: 3.99e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24645243     90 HLILEAADGFLFVVSCDsGRVIYVSDSVTPVLNYTQSDWYGTSLYEHIHPDDREKIREQLSTQES 154
Cdd:smart00091   4 RAILESLPDGIFVLDLD-GRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
 
Name Accession Description Interval E-value
bHLH-PAS_ARNT cd18947
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ...
 9-74 2.47e-42

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor nuclear translocator (ARNT) and similar proteins; ARNT, also termed Class E basic helix-loop-helix protein 2 (bHLHe2), or Dioxin receptor, nuclear translocator, or hypoxia-inducible factor 1-beta (HIF1b), or HIF-1-beta, or HIF1-beta, is a member of bHLH-PAS transcription regulators that acts as the heterodimeric partner for bHLH-PAS proteins such as aryl hydrocarbon receptor (AhR), hypoxia-inducible factor (HIF), and single-minded (SIM). These bHLH-PAS transcription complexes are involved in transcriptional responses to xenobiotic, hypoxia, and developmental pathways. Heterodimerization of bHLH-PAS proteins with ARNT is mediated by contacts between both the bHLH and the tandem PAS domains. ARNT use bHLH and/or PAS domains to interact with several transcriptional coactivators. It is required for activity of the aryl hydrocarbon (dioxin) receptor.


Pssm-ID: 381517  Cd Length: 65  Bit Score: 146.86  E-value: 2.47e-42
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24645243   9 KERFAsRENHCEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMKALRGTGNTSS 74
Cdd:cd18947   1 KERFA-RENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTST 65
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
 282-384 2.56e-27

PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), which binds to an LXXLL motif in the C-terminal region of STAT6 (Signal transducer and activator of transcription 6).


Pssm-ID: 464214 [Multi-domain]  Cd Length: 110  Bit Score: 106.22  E-value: 2.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243   282 QSEFITRHAMDGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLKQKGQMFSLLYRARAKNSEYVWL 361
Cdd:pfam14598   1 TEQFTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDLRTAKSHLREIIQTRGRATSPSYRLRLRDGDFLSV 80

                          90       100
                  ....*....|....*....|...
gi 24645243   362 RTQAYAFLNPYTDEVEYIVCTNS 384
Cdd:pfam14598  81 HTKSKLFLNQNSNQQPFIMCTHT 103
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 283-380 3.26e-18

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 80.37  E-value: 3.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243 283 SEFITRHAMDGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLkQKGQMFSLLYRARAKNSEYVWLR 362
Cdd:cd00130   2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLL-SGGEPVTLEVRLRRKDGSVIWVL 80

                        90
                ....*....|....*...
gi 24645243 363 TQAYAFLNPYTDEVEYIV 380
Cdd:cd00130  81 VSLTPIRDEGGEVIGLLG 98
HLH pfam00010
Helix-loop-helix DNA-binding domain;
15-67 7.38e-13

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 63.25  E-value: 7.38e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24645243    15 RENHCEIERRRRNKMTAYITELSDMVPTcSALARKPDKLTILRMAVAHMKALR 67
Cdd:pfam00010   2 REAHNERERRRRDRINDAFDELRELLPT-LPPDKKLSKAEILRLAIEYIKHLQ 53
PAS COG2202
PAS domain [Signal transduction mechanisms];
280-382 1.77e-12

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 67.74  E-value: 1.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243 280 NNQSEFITRHAMDGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLKQKGQMFSLLYRARAKNSEYV 359
Cdd:COG2202 144 ENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWV 223

                        90       100
                ....*....|....*....|...
gi 24645243 360 WLRTQAYAFLNPytDEVEYIVCT 382
Cdd:COG2202 224 WVEASAVPLRDG--GEVIGVLGI 244
HLH smart00353
helix loop helix domain;
20-67 1.98e-12

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 62.24  E-value: 1.98e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 24645243     20 EIERRRRNKMTAYITELSDMVPTCSAlARKPDKLTILRMAVAHMKALR 67
Cdd:smart00353   2 ARERRRRRKINEAFDELRSLLPTLPK-NKKLSKAEILRLAIEYIKSLQ 48
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 90-154 3.99e-12

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 61.65  E-value: 3.99e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24645243     90 HLILEAADGFLFVVSCDsGRVIYVSDSVTPVLNYTQSDWYGTSLYEHIHPDDREKIREQLSTQES 154
Cdd:smart00091   4 RAILESLPDGIFVLDLD-GRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 280-339 6.20e-12

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 61.26  E-value: 6.20e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243    280 NNQSEFITRHAMDGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLK 339
Cdd:smart00091   8 ESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 87-192 9.40e-12

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 62.05  E-value: 9.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243    87 ELKHLILEAADGFLFVVScDSGRVIYVSDSVTPVLNYTQSDWYGTSLYEHIHPDDREKIREQLST-----QESQNAGRIL 161
Cdd:pfam00989   1 EDLRAILESLPDGIFVVD-EDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQallqgEESRGFEVSF 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 24645243   162 DLKSGTVKK-EGHQSSMRLSMGARRGFICRMR 192
Cdd:pfam00989  80 RVPDGRPRHvEVRASPVRDAGGEILGFLGVLR 111
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 96-192 1.54e-11

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 61.11  E-value: 1.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243  96 ADGFLFVVSCDsGRVIYVSDSVTPVLNYTQSDWYGTSLYEHIHPDDREKIREQLSTQESQNAGRILDLKsgTVKKEGHQS 175
Cdd:cd00130   1 LPDGVIVLDLD-GRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVR--LRRKDGSVI 77

                        90
                ....*....|....*..
gi 24645243 176 SMRLSMGARRGFICRMR 192
Cdd:cd00130  78 WVLVSLTPIRDEGGEVI 94
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 86-363 1.95e-09

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 60.37  E-value: 1.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243  86 QELKHLILEAADGflfVVSCD-SGRVIYVSDSVTPVLNYTQSDWYGTSLYEHIHPDD---REKIREQLSTQESqnagril 161
Cdd:COG5809  15 QRFRSLFENAPDA---ILILDlEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDekeLREILKLLKEGES------- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243 162 dlksgtvkkeghqssmrlsmgaRRGFICRMRVGNVNPESMVSghlnrlkqrnSLGPSRDGtNYAVVHCTGYIKNwpptdM 241
Cdd:COG5809  85 ----------------------RDELEFELRHKNGKRLEFSS----------KLSPIFDQ-NGDIEGMLAISRD-----I 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243 242 FPNMHMERDVDDMSSHCCLVAigrlqvtstaandmsgsNNQSEFITRHAMDGKFTFVDQRVLNILGYTPTELLGKICYDF 321
Cdd:COG5809 127 TERKRMEEALRESEEKFRLIF-----------------NHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILEL 189

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 24645243 322 FHPEDQSHMKESFDQVLKQKGQMfSLLYRARAKNSEYVWLRT 363
Cdd:COG5809 190 IHSDDQENVAAFISQLLKDGGIA-QGEVRFWTKDGRWRLLEA 230
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 292-362 1.05e-07

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 50.75  E-value: 1.05e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24645243   292 DGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLKQKGQMFSLLYRARAKNSEYVWLR 362
Cdd:TIGR00229  22 EGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRRKDGSEIWVE 92
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 290-362 4.99e-04

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 43.51  E-value: 4.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24645243   290 AMDGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLKQKGQMFSLLYRARAKNSEYVWLR 362
Cdd:PRK09776  300 GTEGQWLQVNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLLSGEINSYSMEKRYYRRDGEVVWAL 372
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 83-174 7.04e-04

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 42.65  E-value: 7.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243  83 LTDQELKH-LILEAADGFLFVVSCDsGRVIYVSDSVTPVLNYTQSDWYGTSLYEHIHPDDREK----IREQLSTQESQNA 157
Cdd:COG5809 136 LRESEEKFrLIFNHSPDGIIVTDLD-GRIIYANPAACKLLGISIEELIGKSILELIHSDDQENvaafISQLLKDGGIAQG 214

                        90       100
                ....*....|....*....|....*..
gi 24645243 158 ----------GRILDLKSGTVKKEGHQ 174
Cdd:COG5809 215 evrfwtkdgrWRLLEASGAPIKKNGEV 241
 
Name Accession Description Interval E-value
bHLH-PAS_ARNT cd18947
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ...
 9-74 2.47e-42

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor nuclear translocator (ARNT) and similar proteins; ARNT, also termed Class E basic helix-loop-helix protein 2 (bHLHe2), or Dioxin receptor, nuclear translocator, or hypoxia-inducible factor 1-beta (HIF1b), or HIF-1-beta, or HIF1-beta, is a member of bHLH-PAS transcription regulators that acts as the heterodimeric partner for bHLH-PAS proteins such as aryl hydrocarbon receptor (AhR), hypoxia-inducible factor (HIF), and single-minded (SIM). These bHLH-PAS transcription complexes are involved in transcriptional responses to xenobiotic, hypoxia, and developmental pathways. Heterodimerization of bHLH-PAS proteins with ARNT is mediated by contacts between both the bHLH and the tandem PAS domains. ARNT use bHLH and/or PAS domains to interact with several transcriptional coactivators. It is required for activity of the aryl hydrocarbon (dioxin) receptor.


Pssm-ID: 381517  Cd Length: 65  Bit Score: 146.86  E-value: 2.47e-42
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24645243   9 KERFAsRENHCEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMKALRGTGNTSS 74
Cdd:cd18947   1 KERFA-RENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTST 65
bHLH-PAS_ARNT_like cd11437
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ...
 14-71 5.16e-31

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor nuclear translocator (ARNT) family; The ARNT family of bHLH-PAS transcription regulators includes ARNT, ARNT-like proteins (ARNTL and ARNTL2), and Drosophila melanogaster protein cycle. They act as the heterodimeric partner for bHLH-PAS proteins such as aryl hydrocarbon receptor (AhR), hypoxia-inducible factor (HIF), and single-minded (SIM). These bHLH-PAS transcription complexes are involved in transcriptional responses to xenobiotic, hypoxia, and developmental pathways. Heterodimerization of bHLH-PAS proteins with ARNT is mediated by contacts between both the bHLH and the tandem PAS domains. ARNT use bHLH and/or PAS domains to interact with several transcriptional coactivators. It is required for activity of the aryl hydrocarbon (dioxin) receptor. ARNTL, also termed Basic-helix-loop-helix-PAS protein MOP3, or brain and muscle ARNT-like 1 (BMAL1), or Class E basic helix-loop-helix protein 5 (bHLHe5), or member of PAS protein 3, or PAS domain-containing protein 3 (PASD3), or bHLH-PAS protein JAP3, is a member of the bHLH-PAS transcription factor family that forms heterodimers with another bHLH-PAS protein, CLOCK (circadian locomotor output cycle kaput), which regulates circadian rhythm. ARNTL-CLOCK heterodimer complex activates transcription from E-box (CANNTG) elements found in the promoter of circadian responsive genes. ARNTL is highly homologous to ARNT. ARNTL2, also termed Basic-helix-loop-helix-PAS protein MOP9, or brain and muscle ARNT-like 2 (BMAL2), or CYCLE-like factor (CLIF), or Class E basic helix-loop-helix protein 6 (bHLHe6), or member of PAS protein 9, or PAS domain-containing protein 9 (PASD9), is a neuronal bHLH-PAS transcriptional factor, regulating cell cycle progression and preventing cell death, whose sustained expression might ensure brain neuron survival. It also plays important roles in tumor angiogenesis. Protein cycle, also termed brain and muscle ARNT-like 1 (BMAL1), or MOP3, is a putative bHLH-PAS transcription factor involved in the generation of biological rhythms in Drosophila. It activates cycling transcription of Period (PER) and Timeless (TIM) by binding to the E-box (5'-CACGTG-3') present in their promoters.


Pssm-ID: 381443  Cd Length: 58  Bit Score: 115.21  E-value: 5.16e-31
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24645243  14 SRENHCEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMKALRGTGN 71
Cdd:cd11437   1 SRSNHSEIEKRRRDKMNAYIQELSALVPACNAMSRKLDKLTVLRMAVQHLKSLRGTGS 58
bHLH-PAS_cycle_like cd19726
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein ...
 14-75 3.23e-28

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster protein cycle and similar proteins; Protein cycle, also termed brain and muscle ARNT-like 1 (BMAL1), or MOP3, is a putative bHLH-PAS transcription factor involved in the generation of biological rhythms in Drosophila. It activates cycling transcription of Period (PER) and Timeless (TIM) by binding to the E-box (5'-CACGTG-3') present in their promoters.


Pssm-ID: 381569  Cd Length: 62  Bit Score: 107.18  E-value: 3.23e-28
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24645243  14 SRENHCEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMKALRGTGNTSSD 75
Cdd:cd19726   1 RRQNHSEIEKRRRDKMNTYITELSSMIPMCNAMSRKLDKLTVLRMAVQHMKTLRGSLTSYTE 62
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
 282-384 2.56e-27

PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), which binds to an LXXLL motif in the C-terminal region of STAT6 (Signal transducer and activator of transcription 6).


Pssm-ID: 464214 [Multi-domain]  Cd Length: 110  Bit Score: 106.22  E-value: 2.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243   282 QSEFITRHAMDGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLKQKGQMFSLLYRARAKNSEYVWL 361
Cdd:pfam14598   1 TEQFTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDLRTAKSHLREIIQTRGRATSPSYRLRLRDGDFLSV 80

                          90       100
                  ....*....|....*....|...
gi 24645243   362 RTQAYAFLNPYTDEVEYIVCTNS 384
Cdd:pfam14598  81 HTKSKLFLNQNSNQQPFIMCTHT 103
bHLH-PAS_ARNTL_PASD3 cd11438
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ...
 14-71 4.08e-23

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor nuclear translocator-like protein 1 (ARNTL) and similar proteins; ARNTL, also termed Basic-helix-loop-helix-PAS protein MOP3, or brain and muscle ARNT-like 1 (BMAL1), or Class E basic helix-loop-helix protein 5 (bHLHe5), or member of PAS protein 3, or PAS domain-containing protein 3 (PASD3), or bHLH-PAS protein JAP3, is a member of the bHLH-PAS transcription factor family that forms heterodimers with another bHLH-PAS protein, CLOCK (circadian locomotor output cycle kaput), which regulates circadian rhythm. ARNTL-CLOCK heterodimer complex activates transcription from E-box (CANNTG) elements found in the promoter of circadian responsive genes. ARNTL is highly homologous to ARNT.


Pssm-ID: 381444  Cd Length: 64  Bit Score: 92.86  E-value: 4.08e-23
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24645243  14 SRENHCEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMKALRGTGN 71
Cdd:cd11438   7 AREAHSQIEKRRRDKMNSFIDELASLVPTCNAMSRKLDKLTVLRMAVQHMKTLRGATN 64
bHLH-PAS_ARNTL2_PASD9 cd11469
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor ...
 15-72 5.85e-21

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in aryl hydrocarbon receptor nuclear translocator-like protein 2 (ARNTL2) and similar proteins; ARNTL2, also termed Basic-helix-loop-helix-PAS protein MOP9, or brain and muscle ARNT-like 2 (BMAL2), or CYCLE-like factor (CLIF), or Class E basic helix-loop-helix protein 6 (bHLHe6), or member of PAS protein 9, or PAS domain-containing protein 9 (PASD9), is a neuronal bHLH-PAS transcriptional factor, regulating cell cycle progression and preventing cell death, whose sustained expression might ensure brain neuron survival. It also plays important roles in tumor angiogenesis. ARNT-2 heterodimerize with other bHLH-PAS proteins such as aryl hydrocarbon receptor (AhR), hypoxia-inducible factor (HIF), and single-minded (SIM).


Pssm-ID: 381475  Cd Length: 60  Bit Score: 86.62  E-value: 5.85e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24645243  15 RENHCEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMKALRGTGNT 72
Cdd:cd11469   2 REAHSQTEKRRRDKMNNLIEELSAMIPQCNPMARKLDKLTVLRMAVQHLKSLKGSTSS 59
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 295-383 1.01e-18

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 81.23  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243   295 FTFVDQRVLNILGYTPTELLGKI--CYDFFHPEDQSHMKESFDQVLKqKGQMFSLLYRARAKNSEYVWLRTQAYAFLNPy 372
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGesWLDLVHPDDRERVREALWEALK-GGEPYSGEYRIRRKDGEYRWVEARARPIRDE- 78

                          90
                  ....*....|.
gi 24645243   373 TDEVEYIVCTN 383
Cdd:pfam08447  79 NGKPVRVIGVA 89
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 283-380 3.26e-18

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 80.37  E-value: 3.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243 283 SEFITRHAMDGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLkQKGQMFSLLYRARAKNSEYVWLR 362
Cdd:cd00130   2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLL-SGGEPVTLEVRLRRKDGSVIWVL 80

                        90
                ....*....|....*...
gi 24645243 363 TQAYAFLNPYTDEVEYIV 380
Cdd:cd00130  81 VSLTPIRDEGGEVIGLLG 98
bHLH_PAS cd11391
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain family; bHLH-PAS domain has been found ...
 15-64 3.61e-17

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain family; bHLH-PAS domain has been found in a large group of bHLH transcription regulators that are involved in gene expression responding to environmental change and controlling aspects of neural development, including proteins from aryl hydrocarbon receptor nuclear translocator (ARNT) family, hypoxia-inducible factor (HIF) family, aryl hydrocarbon receptor (AhR) family, neuronal PAS domain-containing protein (NPAS) family, Circadian locomotor output cycles protein kaput (CLOCK)-like family, and single-minded (SIM) family. bHLH-PAS transcriptional regulatory factors have a bHLH DNA-binding domain followed by two PAS domains and a C-terminal activation or repression domain. bHLH-PAS family members can be divided into class I and class II based on their dimerization partner. bHLH-PAS class I factors include AhR, HIF and SIM. The best characterized bHLH-PAS Class II protein is the ubiquitous ARNT. Some members of bHLH-PAS family act as transcriptional coactivators (such as NCoA) that lack the ability to dimerize and bind DNA.


Pssm-ID: 381397 [Multi-domain]  Cd Length: 55  Bit Score: 75.69  E-value: 3.61e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24645243  15 RENHCEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMK 64
Cdd:cd11391   1 REKSREAAKKRRDKENAEISELASLLPLPPAVGSKLDKLSVLRLAVAYLR 50
HLH pfam00010
Helix-loop-helix DNA-binding domain;
15-67 7.38e-13

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 63.25  E-value: 7.38e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24645243    15 RENHCEIERRRRNKMTAYITELSDMVPTcSALARKPDKLTILRMAVAHMKALR 67
Cdd:pfam00010   2 REAHNERERRRRDRINDAFDELRELLPT-LPPDKKLSKAEILRLAIEYIKHLQ 53
PAS COG2202
PAS domain [Signal transduction mechanisms];
280-382 1.77e-12

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 67.74  E-value: 1.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243 280 NNQSEFITRHAMDGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLKQKGQMFSLLYRARAKNSEYV 359
Cdd:COG2202 144 ENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWV 223

                        90       100
                ....*....|....*....|...
gi 24645243 360 WLRTQAYAFLNPytDEVEYIVCT 382
Cdd:COG2202 224 WVEASAVPLRDG--GEVIGVLGI 244
HLH smart00353
helix loop helix domain;
20-67 1.98e-12

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 62.24  E-value: 1.98e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 24645243     20 EIERRRRNKMTAYITELSDMVPTCSAlARKPDKLTILRMAVAHMKALR 67
Cdd:smart00353   2 ARERRRRRKINEAFDELRSLLPTLPK-NKKLSKAEILRLAIEYIKSLQ 48
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 90-154 3.99e-12

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 61.65  E-value: 3.99e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24645243     90 HLILEAADGFLFVVSCDsGRVIYVSDSVTPVLNYTQSDWYGTSLYEHIHPDDREKIREQLSTQES 154
Cdd:smart00091   4 RAILESLPDGIFVLDLD-GRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 280-339 6.20e-12

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 61.26  E-value: 6.20e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243    280 NNQSEFITRHAMDGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLK 339
Cdd:smart00091   8 ESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 87-192 9.40e-12

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 62.05  E-value: 9.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243    87 ELKHLILEAADGFLFVVScDSGRVIYVSDSVTPVLNYTQSDWYGTSLYEHIHPDDREKIREQLST-----QESQNAGRIL 161
Cdd:pfam00989   1 EDLRAILESLPDGIFVVD-EDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQallqgEESRGFEVSF 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 24645243   162 DLKSGTVKK-EGHQSSMRLSMGARRGFICRMR 192
Cdd:pfam00989  80 RVPDGRPRHvEVRASPVRDAGGEILGFLGVLR 111
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 96-192 1.54e-11

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 61.11  E-value: 1.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243  96 ADGFLFVVSCDsGRVIYVSDSVTPVLNYTQSDWYGTSLYEHIHPDDREKIREQLSTQESQNAGRILDLKsgTVKKEGHQS 175
Cdd:cd00130   1 LPDGVIVLDLD-GRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVR--LRRKDGSVI 77

                        90
                ....*....|....*..
gi 24645243 176 SMRLSMGARRGFICRMR 192
Cdd:cd00130  78 WVLVSLTPIRDEGGEVI 94
PAS COG2202
PAS domain [Signal transduction mechanisms];
280-382 3.23e-10

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 61.19  E-value: 3.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243 280 NNQSEFITRHAMDGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLKQkGQMFSLLYRARAKNSEYV 359
Cdd:COG2202  18 ESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAG-GGVWRGELRNRRKDGSLF 96

                        90       100
                ....*....|....*....|...
gi 24645243 360 WLRTQAYAFLNPyTDEVEYIVCT 382
Cdd:COG2202  97 WVELSISPVRDE-DGEITGFVGI 118
bHLH_SF cd00083
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
 22-67 6.43e-10

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: 54.83  E-value: 6.43e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 24645243  22 ERRRRNKMTAYITELSDMVPTCSALaRKPDKLTILRMAVAHMKALR 67
Cdd:cd00083   1 ERRRRDKINDAFEELKRLLPELPDS-KKLSKASILQKAVEYIRELQ 45
bHLH-O_HERP_like cd11389
basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES) ...
 18-70 8.05e-10

basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES)-related repressor protein (HERP)-like family; The HERP-like family includes bHLH-O transcriptional regulators that are related to the Drosophila hairy and Enhancer-of-split proteins. They contain a basic helix-loop-helix (bHLH) domain with an invariant glycine residue in its basic region, an orange domain in the central region and YXXW sequence motif at its C-terminal region. HERP proteins (HEY1, HEY2 and HEYL) act as downstream effectors of Notch signaling. They are involved in cardiovascular development and have roles in somitogenesis, myogenesis and gliogenesis. Hairy and enhancer of split-related protein HELT is a transcriptional repressor expressed in the developing central nervous system. It binds preferentially to the canonical E box sequence 5'-CACGCG-3' and regulates neuronal differentiation and/or identity. Differentially expressed in chondrocytes proteins, DEC1 and DEC2, are widely expressed in both embryonic and adult tissues and have been implicated in apoptosis, cell proliferation, and circadian rhythms, as well as malignancy in various cancers. Drosophila melanogaster protein clockwork orange (Cwo) is also included in this family. It is involved in the regulation of Drosophila circadian rhythms. It functions as both an activator and a repressor of clock gene expression.


Pssm-ID: 381395 [Multi-domain]  Cd Length: 55  Bit Score: 54.64  E-value: 8.05e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24645243  18 HCEIERRRRNKMTAYITELSDMVPTCSALAR--KPDKLTILRMAVAHMKALRGTG 70
Cdd:cd11389   1 HKVIEKRRRDRINESLAELRRLVPEARKSKGsgKLEKAEILEMTLQHLKALQSST 55
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 86-363 1.95e-09

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 60.37  E-value: 1.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243  86 QELKHLILEAADGflfVVSCD-SGRVIYVSDSVTPVLNYTQSDWYGTSLYEHIHPDD---REKIREQLSTQESqnagril 161
Cdd:COG5809  15 QRFRSLFENAPDA---ILILDlEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDekeLREILKLLKEGES------- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243 162 dlksgtvkkeghqssmrlsmgaRRGFICRMRVGNVNPESMVSghlnrlkqrnSLGPSRDGtNYAVVHCTGYIKNwpptdM 241
Cdd:COG5809  85 ----------------------RDELEFELRHKNGKRLEFSS----------KLSPIFDQ-NGDIEGMLAISRD-----I 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243 242 FPNMHMERDVDDMSSHCCLVAigrlqvtstaandmsgsNNQSEFITRHAMDGKFTFVDQRVLNILGYTPTELLGKICYDF 321
Cdd:COG5809 127 TERKRMEEALRESEEKFRLIF-----------------NHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILEL 189

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 24645243 322 FHPEDQSHMKESFDQVLKQKGQMfSLLYRARAKNSEYVWLRT 363
Cdd:COG5809 190 IHSDDQENVAAFISQLLKDGGIA-QGEVRFWTKDGRWRLLEA 230
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 292-382 9.45e-08

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 50.15  E-value: 9.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243   292 DGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQShmkESFDQVLKQKGQMFSLLYRARAKNSEYVWLRTQAYAFLNP 371
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDS---ERLREALREGKAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|.
gi 24645243   372 yTDEVEYIVCT 382
Cdd:pfam13426  78 -GGELVGIIAI 87
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 292-362 1.05e-07

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 50.75  E-value: 1.05e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24645243   292 DGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLKQKGQMFSLLYRARAKNSEYVWLR 362
Cdd:TIGR00229  22 EGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRRKDGSEIWVE 92
bHLHzip_USF_MITF cd11387
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in USF/MITF family; The USF (upstream ...
 17-67 2.75e-07

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in USF/MITF family; The USF (upstream stimulatory factor)/MITF (microphthalmia-associated transcription factor) family includes two bHLHzip transcription factor subfamilies. USFs are ubiquitously expressed and key regulators of a wide number of gene regulation networks, including the stress and immune responses, cell cycle and proliferation, lipid and glucid metabolism. USFs recruit chromatin remodeling enzymes and interact with co-activators and the members of the transcription pre-initiation complex. USFs interact with high affinity to E-box regulatory elements. The MITF (also known as microphthalmia-TFE, or MiT) subfamily comprises four genes in mammals (MITF, TFE3, TFEB, and TFEC); each gene has different functions. MITF is involved in neural crest melanocytes development as well as the pigmented retinal epithelium. TFEB is required for vascularization of the mouse placenta. TFE3 is involved in B cell function. TFEC regulates gene expression in macrophages. The MITF subfamily proteins can form homodimers or heterodimers with each other but not with other bHLH or bHLHzip proteins.


Pssm-ID: 381393 [Multi-domain]  Cd Length: 58  Bit Score: 47.63  E-value: 2.75e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 24645243  17 NHCEIERRRRNKMTAYITELSDMVPTC--SALARKPDKLTILRMAVAHMKALR 67
Cdd:cd11387   1 SHNAVERRRRDNINEKIQELGSLVPPSrlETKDLKPNKGSILSKAVEYIRELQ 53
bHLHzip_scCBP1 cd11398
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae ...
 15-66 4.66e-07

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae centromere-binding protein 1 (CBP-1) and similar proteins; CBP-1, also termed centromere promoter factor 1 (CPF1), or centromere-binding factor 1 (CBF1), is a bHLHzip protein that is required for chromosome stability and methionine prototrophy. It binds as a homodimer to the centromere DNA elements I (CDEI, GTCACATG) region of the centromere that is required for optimal centromere function.


Pssm-ID: 381404 [Multi-domain]  Cd Length: 89  Bit Score: 48.10  E-value: 4.66e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24645243  15 RENHCEIERRRRNKMTAYITELSDMVPtcsALARKPDKLTILRMAVAHMKAL 66
Cdd:cd11398   8 RDNHKEVERRRRENINEGINELAALVP---GNAREKNKGAILARAVEYIQEL 56
bHLHzip_USF2 cd18923
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in upstream stimulatory factor 2 (USF2) ...
 7-79 4.69e-07

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in upstream stimulatory factor 2 (USF2) and similar proteins; USF2, also termed Class B basic helix-loop-helix protein 12 (bHLHb12), or major late transcription factor 2, or FOS-interacting protein (FIP), or upstream transcription factor 2, is a bHLHzip transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.


Pssm-ID: 381493  Cd Length: 80  Bit Score: 47.77  E-value: 4.69e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24645243   7 QDKERfasRENHCEIERRRRNKMTAYITELSDMVPTCSALARK--PDKLTILRMAVAHMKALRGTgNTSSDGTYK 79
Cdd:cd18923   4 RDERR---RAQHNEVERRRRDKINNWIVQLSKIIPDCNTDNSKtgASKGGILSKACDYIRELRQT-NQRMQETYK 74
bHLH_SOHLH_like cd19683
basic helix-loop-helix (bHLH) domain found in the spermatogenesis- and oogenesis-specific ...
 14-68 5.26e-07

basic helix-loop-helix (bHLH) domain found in the spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein (SOHLH) family and similar proteins; The SOHLH family includes two bHLH transcription factors, SOHLH1 and SOHLH2. They are specifically in spermatogonia and oocytes and essential for early spermatogonial and oocyte differentiation. The family also includes transcription factor-like 5 protein (TCFL5) and similar proteins. TCFL5, also termed Cha transcription factor, or HPV-16 E2-binding protein 1 (E2BP-1), is a bHLH transcription factor that plays a crucial role in spermatogenesis. It regulates cell proliferation or differentiation of cells through binding to a specific DNA sequence like other bHLH molecules.


Pssm-ID: 381526  Cd Length: 58  Bit Score: 46.96  E-value: 5.26e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24645243  14 SRENHCEIERRRRNKMTAYITELSDMVPTCSalaRKPDKLTILRMAVAHMKALRG 68
Cdd:cd19683   2 SRERHNAKERQRRERIKIACDQLRKLVPGCS---RKTDKATVFEFTVAYIKFLRE 53
bHLHzip_USF1 cd18924
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in upstream stimulatory factor 1 (USF1) ...
 7-67 6.64e-07

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in upstream stimulatory factor 1 (USF1) and similar proteins; USF1, also termed Class B basic helix-loop-helix protein 11 (bHLHb11), or major late transcription factor 1, is a bHLHzip transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters. It is ubiquitously expressed and involved in the transcription activation of various functional genes implicated in lipid and glucose metabolism, stress response, immune response, cell cycle control and tumour suppression. USF-1 recruits chromatin remodeling enzymes and interact with co-activators and the members of the transcription pre-initiation complex. Genetic polymorphisms of USF1 are associated with some metabolic and cardiovascular diseases, like diabetes, atherosclerosis, coronary artery calcifications and familial combined hyperlipidaemia (FCHL).


Pssm-ID: 381494  Cd Length: 65  Bit Score: 46.99  E-value: 6.64e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24645243   7 QDKERfasRENHCEIERRRRNKMTAYITELSDMVPTCSALARKP--DKLTILRMAVAHMKALR 67
Cdd:cd18924   1 RDEKR---RAQHNEVERRRRDKINNWIVQLSKIIPDCSMESTKSgqSKGGILSKACDYIQELR 60
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 285-382 8.74e-07

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 47.80  E-value: 8.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243   285 FITRHamDGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLKQKGQMFSLLYRARAKNSEYVWLRTQ 364
Cdd:pfam00989  15 FVVDE--DGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRVPDGRPRHVEVR 92

                          90
                  ....*....|....*...
gi 24645243   365 AYAFLNPyTDEVEYIVCT 382
Cdd:pfam00989  93 ASPVRDA-GGEILGFLGV 109
bHLHzip_USF cd11396
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in upstream stimulatory factors, USF1, ...
 18-67 8.82e-07

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in upstream stimulatory factors, USF1, USF2 and similar proteins; Upstream stimulatory factor 1 and 2 (USF-1 and USF-2) are members of bHLHzip transcription factor family. USFs are ubiquitously expressed and key regulators of a wide number of gene regulation networks, including the stress and immune responses, cell cycle and proliferation, lipid and glucid metabolism. USFs recruit chromatin remodeling enzymes and interact with co-activators and the members of the transcription pre-initiation complex. USFs interact with high affinity to E-box regulatory elements.


Pssm-ID: 381402  Cd Length: 58  Bit Score: 46.14  E-value: 8.82e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24645243  18 HCEIERRRRNKMTAYITELSDMVPTCSALARK--PDKLTILRMAVAHMKALR 67
Cdd:cd11396   2 HNEVERRRRDKINNWIVKLAKIVPDCEKDNSKqgQSKGGILSKACDYIQELR 53
bHLHzip_SREBP_like cd11395
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
 14-66 1.16e-06

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein (SREBP) family and similar proteins; The SREBP family includes SREBP1 and SREBP2, which are bHLHzip transcriptional activator of genes encoding proteins essential for cholesterol biosynthesis/uptake and fatty acid biosynthesis. SREBP1 and SREBP2 are principally found in the liver and in adipocytes and made up of an N-terminal transcription factor portion (composed of an activation domain, a bHLHzip domain, and a nuclear localization signal), a hydrophobic region containing two membrane spanning regions, and a C-terminal regulatory segment. They recognize a symmetric sterol regulatory element (TCACNCCAC) instead of E-box. The family also includes Saccharomyces cerevisiae transcription factor HMS1 (also termed high-copy MEP suppressor protein 1) and serine-rich protein TYE7. HMS1 is a putative bHLHzip transcription factor involved in exit from mitosis and pseudohyphal differentiation. TYE7, also termed basic-helix-loop-helix protein SGC1, is a putative bHLHzip transcription activator required for Ty1-mediated glycolytic gene expression. TYE7 N-terminal is extremely rich in serine residues. It binds DNA on E-box motifs, 5'-CANNTG-3'. TYE7 is not essential for growth.


Pssm-ID: 381401 [Multi-domain]  Cd Length: 87  Bit Score: 46.94  E-value: 1.16e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24645243  14 SRENHCEIERRRRNKMTAYITELSDMVPTCS--------------ALARKPDKLTILRMAVAHMKAL 66
Cdd:cd11395   3 KRLPHNAIEKRYRSNLNTKIERLRDAIPSLRspegksddgglgglAPTTKLSKATILTKAIEYIRHL 69
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 110-162 2.25e-06

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 46.18  E-value: 2.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 24645243   110 VIYVSDSVTPVLNYTQSDWYGT--SLYEHIHPDDREKIREQLstQESQNAGRILD 162
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREAL--WEALKGGEPYS 53
bHLH-O_HEYL cd11447
basic helix-loop-helix-orange (bHLH-O) domain found in hairy/enhancer-of-split related with ...
 21-72 2.40e-06

basic helix-loop-helix-orange (bHLH-O) domain found in hairy/enhancer-of-split related with YRPW motif-like protein (HEYL) and similar proteins; HEYL, also termed Class B basic helix-loop-helix protein 33 (bHLHb33), or hairy-related transcription factor 3 (HRT-3), is a bHLH-O transcriptional repressor that is strongly expressed in the presomitic mesoderm, the somites, the peripheral nervous system and smooth muscle of all arteries and is a downstream effector of the Notch and transforming growth factor-beta pathways. It promotes neuronal differentiation by activating proneural genes and inhibiting other hairy and enhancer of split (HES) and hairy/enhancer-of-split related with YRPW motif protein (HEY) proteins. HEYL also functions as a tumor suppressor involved in the progression of human cancers.


Pssm-ID: 381453 [Multi-domain]  Cd Length: 74  Bit Score: 45.47  E-value: 2.40e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24645243  21 IERRRRNKMTAYITELSDMVPTC--SALARKPDKLTILRMAVAHMKALRGTGNT 72
Cdd:cd11447  16 IEKRRRDRINSSLSELRRLVPTAfeKQGSSKLEKAEILQMTVDHLKMLHATGGA 69
bHLH-O_HERP cd11407
basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES) ...
 21-70 5.61e-06

basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES)-related repressor protein (HERP) family; HERP (also called Hey/Hesr/HRT/CHF/gridlock) proteins corresponds to a family of bHLH-O transcriptional repressors that are related to the Drosophila hairy and Enhancer-of-split proteins and act as downstream effectors of Notch signaling. They contain a basic helix-loop-helix (bHLH) domain with an invariant glycine residue in its basic region, an orange domain in the central region and YXXW sequence motif at its C-terminal region. HERP proteins are involved in cardiovascular development and have roles in somitogenesis, myogenesis and gliogenesis.


Pssm-ID: 381413 [Multi-domain]  Cd Length: 59  Bit Score: 43.95  E-value: 5.61e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24645243  21 IERRRRNKMTAYITELSDMVPTcsALAR----KPDKLTILRMAVAHMKALRGTG 70
Cdd:cd11407   8 IEKRRRDRINNSLAELRRLVPT--AFEKqgsaKLEKAEILQMTVDHLKMLHSKG 59
bHLH-PAS_dCLOCK cd19735
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster ...
 2-83 6.88e-06

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Drosophila melanogaster Circadian locomotor output cycles protein kaput (dCLOCK) and similar proteins; dCLOCK, also termed dPAS1, is a bHLH-PAS Circadian regulator that acts as a transcription factor and generates a rhythmic output with a period of about 24 hours.


Pssm-ID: 381578  Cd Length: 80  Bit Score: 44.40  E-value: 6.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243   2 DEANIQDKERFASrenhceiERRRRNKMTAYITELSDMVptcSALARKPDKLTILRMAVAHMKalrgTGNTSSDGT---- 77
Cdd:cd19735   5 EKDTIKRKSRNLS-------EKKRRDQFNVLINELCSMV---STSNRKMDKSTVLKSTIAFLK----NHNEVTMQShqqe 70

                        90
                ....*....|
gi 24645243  78 ----YKPSFL 83
Cdd:cd19735  71 iqedWKPSFL 80
bHLH-PAS_NCoA3_SRC3 cd18949
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in nuclear receptor coactivator 3 ...
 19-75 8.35e-06

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in nuclear receptor coactivator 3 (NCoA-3) and similar proteins; NCoA-3, also termed ACTR, or amplified in breast cancer 1 protein (AIB-1), or CBP-interacting protein (pCIP), or Class E basic helix-loop-helix protein 42 (bHLHe42), or receptor-associated coactivator 3 (RAC-3), or steroid receptor coactivator protein 3 (SRC-3), or thyroid hormone receptor activator molecule 1 (TRAM-1), is a bHLH-PAS steroid/nuclear receptor-associated coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. It also plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin.


Pssm-ID: 381519  Cd Length: 73  Bit Score: 43.87  E-value: 8.35e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24645243  19 CEIERRRRNKMTAYITELSDMVPT----CSALARKPDKLTILRMAVAHMKALRGTGNTSSD 75
Cdd:cd18949   3 CSGEKRRREQESKYIEELAELISAnlsdIDNFNVKPDKCAILKETVRQIRQIKEQGKSSSN 63
bHLHzip_MITF_like cd11397
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the microphthalmia-associated ...
 9-67 1.06e-05

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the microphthalmia-associated transcription factor family (MITF) family; The MITF (also known as microphthalmia-TFE, or MiT) family is a small family that contain a basic helix loop helix domain associated with a leucine zipper (bHLHZip). The MITF family comprises four genes in mammals (MITF, TFE3, TFEB, and TFEC); each gene has different functions. MITF is involved in neural crest melanocytes development as well as the pigmented retinal epithelium. TFEB is required for vascularization of the mouse placenta. TFE3 is involved in B cell function. TFEC regulates gene expression in macrophages. The MITF family can form homodimers or heterodimers with each other but not with other bHLH or bHLHzip proteins.


Pssm-ID: 381403  Cd Length: 69  Bit Score: 43.44  E-value: 1.06e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24645243   9 KERfASRENHCEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMKALR 67
Cdd:cd11397   1 KDR-QKKDNHNMIERRRRFNINDRIKELGTLLPKSNDPDMRWNKGTILKASVDYIRKLQ 58
bHLHzip_TFEB cd18927
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor EB (TFEB) and ...
 3-67 1.50e-05

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor EB (TFEB) and similar proteins; TFEB, also termed Class E basic helix-loop-helix protein 35 (bHLHe35), is a bHLHzip transcription factor that is required for vascularization of the mouse placenta. It specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Its efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFE3 or MITF.


Pssm-ID: 381497  Cd Length: 91  Bit Score: 43.81  E-value: 1.50e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24645243   3 EANIQDKERfASRENHCEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMKALR 67
Cdd:cd18927   1 EARALAKER-QKKDNHNLIERRRRFNINDRIKELGTLIPKTNDLDVRWNKGTILKASVDYIKRMQ 64
bHLH-O_HELT cd11408
basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split-related ...
 17-70 2.11e-05

basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split-related protein HELT and similar proteins; HELT, also termed HES/HEY-like transcription factor, is a bHLH-O transcriptional repressor expressed in the developing central nervous system. It binds preferentially to the canonical E box sequence 5'-CACGCG-3' and regulates neuronal differentiation and/or identity. HELT could homodimerize and heterodimerize with other bHLH-O protein such as HES-5 or HEY-2 and bound to E box to repress gene transcription.


Pssm-ID: 381414 [Multi-domain]  Cd Length: 56  Bit Score: 42.28  E-value: 2.11e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24645243  17 NHCEIERRRRNKMTAYITELSDMVPtcSALAR----KPDKLTILRMAVAHMKALRGTG 70
Cdd:cd11408   1 SHKVIEKRRRDRINRCLNELGKTVP--MALAKqtsgKLEKAEILEMTVQYLRALHSAD 56
bHLH-O_ESMB_like cd19741
basic helix-loop-helix-orange (bHLH-O) domain found in Drosophila melanogaster enhancer of ...
 21-67 2.88e-05

basic helix-loop-helix-orange (bHLH-O) domain found in Drosophila melanogaster enhancer of split mbeta protein (ESMB) and similar proteins; ESMB, also termed E(spl)mbeta, or HLH-mbeta, or split locus enhancer protein mA, is a bHLH-O transcriptional repressor of genes that require a bHLH protein for their transcription. It is involved in the neural-epidermal lineage decision during early neurogenesis. The family also includes Enhancer of split m7 protein (also known as E(spl)m7), which acts as a transcriptional repressor that participates in the control of cell fate choice by uncommitted neuroectodermal cells in the embryo.


Pssm-ID: 381584 [Multi-domain]  Cd Length: 69  Bit Score: 42.37  E-value: 2.88e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 24645243  21 IERRRRNKMTAYITELSDMVPTCSALARKPD----KLTILRMAVAHMKALR 67
Cdd:cd19741  15 LERKRRARINKCLDELKDLMVEALATEAENVskleKADILELTVRHLKKLR 65
bHLH_AtbHLH_like cd11393
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana genes coding transcription ...
 18-67 3.69e-05

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana genes coding transcription factors and similar proteins; bHLH proteins are the second largest class of plant transcription factors that regulate transcription of genes that are involve in many essential physiological and developmental process. bHLH proteins are transcriptional regulators that are found in organisms from yeast to humans. The Arabidopsis bHLH proteins that have been characterized so far have roles in regulation of fruit dehiscence, cell development (carpel, anther and epidermal), phytochrome signaling, flavonoid biosynthesis, hormone signaling and stress responses.


Pssm-ID: 381399 [Multi-domain]  Cd Length: 53  Bit Score: 41.40  E-value: 3.69e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24645243  18 HCEIERRRRNKMTAYITELSDMVPTCsalaRKPDKLTILRMAVAHMKALR 67
Cdd:cd11393   1 HSIAERKRREKINERIRALRSLVPNG----GKTDKASILDEAIEYIKFLQ 46
bHLHzip_Mlx_like cd11404
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, ...
 15-66 4.87e-05

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: 41.90  E-value: 4.87e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24645243  15 RENHCEIERRRRNKMTAYITELSDMVPTCSalARKPDKLTILRMAVAHMKAL 66
Cdd:cd11404   3 RLNHVRSEKKRRELIKKGYDELCALVPGLD--PQKRTKADILQKAADWIQEL 52
bHLHzip_USF3 cd18910
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in basic helix-loop-helix ...
 15-67 6.75e-05

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: 41.13  E-value: 6.75e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 24645243  15 RENHCEIERRRRNKMTAYITELSDMVPTCSalARKPDKLTILRMAVAHMKALR 67
Cdd:cd18910   6 RESHNEVERRRKDKINAGINKIGELLPDRD--AKKQSKNMILEQAYKYIVELK 56
bHLHzip_TFE3 cd18928
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor E3 (TFE3) and ...
 3-75 8.53e-05

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor E3 (TFE3) and similar proteins; TFE3, also termed Class E basic helix-loop-helix protein 33 (bHLHe33), is a bHLHzip transcription factor that is involved in B cell function. It specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Its efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFEB or MITF.


Pssm-ID: 381498 [Multi-domain]  Cd Length: 91  Bit Score: 41.57  E-value: 8.53e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24645243   3 EANIQDKERfASRENHCEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMKALRGTGNTSSD 75
Cdd:cd18928   1 EAKAFLKER-QKKDNHNLIERRRRFNINDRIKELGTLIPKSTDPEMRWNKGTILKASVDYIRKLQKEQQRSKE 72
bHLH-O_HEY2 cd18920
basic helix-loop-helix-orange (bHLH-O) domain found in hairy/enhancer-of-split related with ...
 21-70 1.33e-04

basic helix-loop-helix-orange (bHLH-O) domain found in hairy/enhancer-of-split related with YRPW motif protein 2 (HEY2) and similar proteins; HEY2, also termed cardiovascular helix-loop-helix factor 1 (CHF-1), or Class B basic helix-loop-helix protein 32 (bHLHb32), or HES-related repressor protein 2, or hairy and enhancer of split-related protein 2 (HESR-2), or hairy-related transcription factor 2 (HRT-2), or protein gridlock homolog, is a bHLH-O transcriptional repressor expressed preferentially in the developing and adult cardiovascular system. As a downstream effector of Notch signaling, HEY2 may be required for cardiovascular development. It also plays an important role in neurologic development, as well as in the progression of human cancers.


Pssm-ID: 381490 [Multi-domain]  Cd Length: 82  Bit Score: 40.89  E-value: 1.33e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24645243  21 IERRRRNKMTAYITELSDMVPTC--SALARKPDKLTILRMAVAHMKALRGTG 70
Cdd:cd18920  17 IEKRRRDRINNSLSELRRLVPTAfeKQGSAKLEKAEILQMTVDHLKMLQATG 68
bHLH-O_HERP_HES cd19685
basic helix-loop-helix-orange (bHLH-O) domain found in HERP/HES-like family; The HERP/HES-like ...
 21-67 1.60e-04

basic helix-loop-helix-orange (bHLH-O) domain found in HERP/HES-like family; The HERP/HES-like family includes bHLH-O transcriptional regulators that are related to the Drosophila hairy and Enhancer-of-split (HES) proteins. The HERP (HES-related repressor protein) subfamily proteins contain a basic helix-loop-helix (bHLH) domain with an invariant glycine residue in its basic region, an orange domain in the central region and YXXW sequence motif at its C-terminal region. Hairy and enhancer of split (HES)-related repressor protein (HERP) proteins (HEY1, HEY2 and HEYL) act as downstream effectors of Notch signaling. They are involved in cardiovascular development and have roles in somitogenesis, myogenesis and gliogenesis. Hairy and enhancer of split-related protein HELT is a transcriptional repressor expressed in the developing central nervous system. It binds preferentially to the canonical E box sequence 5'-CACGCG-3' and regulates neuronal differentiation and/or identity. Differentially expressed in chondrocytes proteins, DEC1 and DEC2, are widely expressed in both embryonic and adult tissues and have been implicated in apoptosis, cell proliferation, and circadian rhythms, as well as malignancy in various cancers. Drosophila melanogaster protein clockwork orange (Cwo) is also included in this subfamily. It is involved in the regulation of Drosophila circadian rhythms. It functions as both an activator and a repressor of clock gene expression. The HES subfamily proteins contain a basic helix-loop-helix (bHLH) domain with an invariant proline residue in its basic region, an orange domain in the central region and a conserved tetrapeptide motif, WRPW, at its C-terminal region. They form heterodimers or homodimers via their HLH domain and bind DNA to repress gene transcription that play an essential role in development of both compartment and boundary cells of the central nervous system.


Pssm-ID: 381528 [Multi-domain]  Cd Length: 52  Bit Score: 39.72  E-value: 1.60e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 24645243  21 IERRRRNKMTAYITELSDMVPTCSAL--ARKPDKLTILRMAVAHMKALR 67
Cdd:cd19685   1 SEKRRRQRINDKLNQLKELLPPNLSKqsRSKLSKAEILEMAITELRRLQ 49
bHLH_TCFL5 cd18909
basic helix-loop-helix (bHLH) domain found in transcription factor-like 5 protein (TCFL5) and ...
 15-68 3.00e-04

basic helix-loop-helix (bHLH) domain found in transcription factor-like 5 protein (TCFL5) and similar proteins; TCFL5, also termed Cha transcription factor, or HPV-16 E2-binding protein 1 (E2BP-1), is a bHLH transcription factor that plays a crucial role in spermatogenesis. It regulates cell proliferation or differentiation of cells through binding to a specific DNA sequence like other bHLH molecules.


Pssm-ID: 381479  Cd Length: 60  Bit Score: 39.15  E-value: 3.00e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24645243  15 RENHCEIERRRRNKMTAYITELSDMVPTCSAlarKPDKLTILRMAVAHMKALRG 68
Cdd:cd18909   3 RERHNRMERDRRRRIRICCDELNLLVPFCNA---ETDKATTLQWTTAFLKYIQE 53
bHLH-O_HEY1 cd19748
basic helix-loop-helix-orange (bHLH-O) domain found in hairy/enhancer-of-split related with ...
 21-70 3.34e-04

basic helix-loop-helix-orange (bHLH-O) domain found in hairy/enhancer-of-split related with YRPW motif protein 1 (HEY1) and similar proteins; HEY1, also termed cardiovascular helix-loop-helix factor 2 (CHF-2), or Class B basic helix-loop-helix protein 31 (bHLHb31), or HES-related repressor protein 1, or hairy and enhancer of split-related protein 1 (HESR-1), or hairy-related transcription factor 1 (HRT-1), is a bHLH-O transcriptional repressor that acts as an essential downstream effector of the Notch signaling pathway and may play a fundamental role in vascular development. HEY1 also participates several cancer-related pathways. It acts as a positive regulator of the tumor suppressor p53.


Pssm-ID: 381591 [Multi-domain]  Cd Length: 71  Bit Score: 39.55  E-value: 3.34e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24645243  21 IERRRRNKMTAYITELSDMVPTC-----SAlarKPDKLTILRMAVAHMKALRGTG 70
Cdd:cd19748  16 IEKRRRDRINNSLSELRRLVPSAfekqgSA---KLEKAEILQMTVDHLKMLHAAG 67
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 290-362 4.99e-04

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 43.51  E-value: 4.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24645243   290 AMDGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQSHMKESFDQVLKQKGQMFSLLYRARAKNSEYVWLR 362
Cdd:PRK09776  300 GTEGQWLQVNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLLSGEINSYSMEKRYYRRDGEVVWAL 372
bHLHzip_L-Myc cd11457
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in L-Myc and similar proteins; L-Myc, ...
 8-66 5.88e-04

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: 39.39  E-value: 5.88e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24645243   8 DKERFASRENHCEIERRRRNKMTAYITELSDMVPTCSALARKPdKLTILRMAVAHMKAL 66
Cdd:cd11457   1 DTEDVAKRKNHNFLERKRRNDLRSRFLALRDEVPGLASCSKTP-KVVILSKATEYLRGL 58
bHLH-PAS_SRC cd11439
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in steroid receptor coactivator ...
 17-67 6.88e-04

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in steroid receptor coactivator (SRC) family; The SRC family of coactivators includes SRC-1 (NcoA-1/p160), SRC-2(TIF2/GRIP1/NcoA-2) and SRC-3(NcoA-3/pCIP/RAC3/ACTR/pCIP/AIB1/TRAM1), which are critical mediators of steroid receptor action. They contain bHLH-PAS domain at the N-terminal that is followed by receptor interacting domain and C-terminal transcriptional activation domain. SRC coactivators interact with nuclear receptors in a ligand-dependent manner and enhance transcriptional activation by the receptor via histone acetylation/methylation.


Pssm-ID: 381445  Cd Length: 58  Bit Score: 38.18  E-value: 6.88e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24645243  17 NHCEIERRRRNKMTAYITEL--------SDMvptcSALARKPDKLTILRMAVAHMKALR 67
Cdd:cd11439   1 NKCLNEKRRREQENKYIEELaelisasiSDM----DSLSVKPDKCAILQETVKQIRQIK 55
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 83-174 7.04e-04

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 42.65  E-value: 7.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243  83 LTDQELKH-LILEAADGFLFVVSCDsGRVIYVSDSVTPVLNYTQSDWYGTSLYEHIHPDDREK----IREQLSTQESQNA 157
Cdd:COG5809 136 LRESEEKFrLIFNHSPDGIIVTDLD-GRIIYANPAACKLLGISIEELIGKSILELIHSDDQENvaafISQLLKDGGIAQG 214

                        90       100
                ....*....|....*....|....*..
gi 24645243 158 ----------GRILDLKSGTVKKEGHQ 174
Cdd:COG5809 215 evrfwtkdgrWRLLEASGAPIKKNGEV 241
bHLH_AtPIF_like cd11445
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana phytochrome interacting ...
 14-66 7.75e-04

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana phytochrome interacting factors (PIFs) and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as PIFs, ALC, PIL1, SPATULA, and UNE10. PIFs (PIF1, PIF3, PIF4, PIF5, PIF6 and PIF7) have been shown to control light-regulated gene expression. They directly bind to the photoactivated phytochromes and are degraded in response to light signals. ALC, also termed AtbHLH73, or protein ALCATRAZ, or EN 98, is required for the dehiscence of fruit, especially for the separation of the valve cells from the replum. It promotes the differentiation of a strip of labile non-lignified cells sandwiched between layers of lignified cells. PIL1, also termed AtbHLH124, or protein phytochrome interacting factor 3-like 1, or EN 110, is involved in responses to transient and long-term shade. It is required for the light-mediated inhibition of hypocotyl elongation and necessary for rapid light-induced expression of the photomorphogenesis- and circadian-related gene APRR9. PIL1 seems to play a role in multiple PHYB responses, such as flowering transition and petiole elongation. SPATULA, also termed AtbHLH24, or EN 99, plays a role in floral organogenesis. It promotes the growth of carpel margins and of pollen tract tissues derived from them. UNE10, also termed AtbHLH16, or protein UNFERTILIZED EMBRYO SAC 10, or EN 99, is required during the fertilization of ovules by pollen.


Pssm-ID: 381451  Cd Length: 64  Bit Score: 38.12  E-value: 7.75e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 24645243  14 SRENHCEIERRRRNKMTAYITELSDMVPTCSalarKPDKLTILRMAVAHMKAL 66
Cdd:cd11445   2 AAEVHNLSERRRRDRINEKMKALQELIPNCN----KTDKASMLDEAIEYLKSL 50
bHLHzip_MITF cd18926
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in microphthalmia-associated ...
 3-67 8.06e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in microphthalmia-associated transcription factor (MITF) and similar proteins; MITF, also termed Class E basic helix-loop-helix protein 32 (bHLHe32), is a bHLHzip transcription factor that is involved in neural crest melanocytes development as well as the pigmented retinal epithelium. It regulates the expression of genes with essential roles in cell differentiation, proliferation and survival. It binds to M-boxes (5'-TCATGTG-3') and symmetrical DNA sequences (E-boxes) (5'-CACGTG-3') found in the promoters of target genes, such as BCL2 and tyrosinase (TYR).


Pssm-ID: 381496  Cd Length: 104  Bit Score: 39.30  E-value: 8.06e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24645243   3 EANIQDKERfASRENHCEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMKALR 67
Cdd:cd18926   3 EARALAKER-QKKDNHNLIERRRRFNINDRIKELGTLIPKSNDPDMRWNKGTILKASVDYIRKLQ 66
bHLHzip_Myc cd11400
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a ...
 15-67 9.80e-04

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: 38.30  E-value: 9.80e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24645243  15 RENHCEIERRRRNKMTAYITELSDMVPtcsALARKPD--KLTILRMAVAHMKALR 67
Cdd:cd11400   2 RRLHNVLERQRRNDLKNSFEKLRDLVP---ELADNEKasKVVILKKATEYIKQLQ 53
bHLH-O_Cwo_like cd11440
basic helix-loop-helix-orange (bHLH-O) domain found in Drosophila melanogaster protein ...
 17-67 1.26e-03

basic helix-loop-helix-orange (bHLH-O) domain found in Drosophila melanogaster protein clockwork orange (Cwo) and similar proteins; Cwo is a bHLH-O transcriptional regulator involved in the regulation of Drosophila circadian rhythms. It functions as both an activator and a repressor of clock gene expression.


Pssm-ID: 381446 [Multi-domain]  Cd Length: 60  Bit Score: 37.46  E-value: 1.26e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24645243  17 NHCEIERRRRNKMTAYITELSDMVPTcsALARKP----DKLTILRMAVAHMKALR 67
Cdd:cd11440   5 SHRIIEKRRRDRMNNCLADLSRLIPP--TYLKKGrgriEKTEIIEMAIKHIKHLQ 57
bHLH_AtNAI1_like cd11452
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein NAI1 and similar ...
 16-67 1.37e-03

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein NAI1 and similar proteins; NAI1, also termed AtbHLH20, or EN 27, is a bHLH transcription activator that regulates the expression of at least NAI2, PYK10 and PBP1. It is required for and mediates the formation of endoplasmic reticulum bodies (ER bodies). It plays a role in the symbiotic interactions with the endophytes of the Sebacinaceae fungus family, such as Piriformospora indica and Sebacina.


Pssm-ID: 381458 [Multi-domain]  Cd Length: 75  Bit Score: 37.83  E-value: 1.37e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24645243  16 ENHCEIERRRRNKMTAYITELSDMVPTCsalaRKPDKLTILRMAVAHMKALR 67
Cdd:cd11452   4 QDHILAERKRREKLSQRFIALSALVPGL----KKMDKASVLGDAIKHIKQLQ 51
bHLH-PAS_CLOCK_like cd11441
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output ...
 22-64 1.64e-03

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output cycles protein kaput (CLOCK) and similar proteins; The family includes CLOCK, neuronal PAS domain-containing protein 2 (NPAS2) and non-mammalian circadian clock protein PASD1. CLOCK, also termed Class E basic helix-loop-helix protein 8 (bHLHe8), is a transcriptional activator which forms a core component of the circadian clock. NPAS2, also termed neuronal PAS2, or basic-helix-loop-helix-PAS protein MOP4, or Class E basic helix-loop-helix protein 9 (bHLHe9), or member of PAS protein 4, or PAS domain-containing protein 4, is a transcriptional activator which forms a core component of the circadian clock. PASD1 is evolutionarily related to Circadian locomotor output cycles protein kaput (CLOCK)and functions as a suppressor of the biological clock that drives the daily circadian rhythms of cells throughout the body.


Pssm-ID: 381447  Cd Length: 54  Bit Score: 36.95  E-value: 1.64e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24645243  22 ERRRRNKMTAYITELSDMVPTCSalaRKPDKLTILRMAVAHMK 64
Cdd:cd11441   8 EKKRRDQFNVLINELASMLPGRG---RKMDKSTVLKKTIAFLR 47
bHLHzip_TFEC cd18925
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor EC (TFEC) and ...
 9-67 1.74e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor EC (TFEC) and similar proteins; TFEC, also termed Class E basic helix-loop-helix protein 34 (bHLHe34), or transcription factor EC-like (TFEC-L), is a bHLHzip transcriptional regulator that acts as a repressor or an activator and regulates gene expression in macrophages. It plays an important role in the niche to expand hematopoietic progenitors through the modulation of several cytokines.


Pssm-ID: 381495  Cd Length: 85  Bit Score: 37.75  E-value: 1.74e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24645243   9 KERfASRENHCEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMKALR 67
Cdd:cd18925   1 KER-QKKDNHNLIERRRRYNINYRIKELGTLIPKSNDPDMRWNKGTILKASVEYIKWLQ 58
bHLH_AtAIG1_like cd11455
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein AIG1 and similar ...
 7-69 1.78e-03

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein AIG1 and similar proteins; AIG1, also termed AtbHLH32, or EN 54, or protein target of MOOPTEROS 5, is a transcription factor required for MONOPTEROS-dependent root initiation in embryo.


Pssm-ID: 381461  Cd Length: 80  Bit Score: 37.66  E-value: 1.78e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24645243   7 QDKERFASReNHCEIERRRRNKMTAYITELSDMVPTCSalarKPDKLTILRMAVAHMKALRGT 69
Cdd:cd11455   1 EDKALAASK-SHSEAERRRRERINSHLATLRTLLPNLS----KTDKASLLAEVVQHVKELKRQ 58
bHLH_O_HES cd11410
basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES) ...
 21-67 2.36e-03

basic helix-loop-helix-orange (bHLH-O) domain found in hairy and enhancer of split (HES) family; The HES family includes bHLH-O transcriptional regulators that are related to the Drosophila hairy and Enhancer-of-split (HES) proteins. They contain a basic helix-loop-helix (bHLH) domain with an invariant proline residue in its basic region, an orange domain in the central region and a conserved tetrapeptide motif, WRPW, at its C-terminal region. HES family proteins form heterodimers or homodimers via their HLH domain and bind DNA to repress gene transcription that play an essential role in development of both compartment and boundary cells of the central nervous system.


Pssm-ID: 381416 [Multi-domain]  Cd Length: 54  Bit Score: 36.29  E-value: 2.36e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 24645243  21 IERRRRNKMTAYITELSDMVPTCSAL----ARKPDKLTILRMAVAHMKALR 67
Cdd:cd11410   1 MEKKRRARINKSLEQLKTLVLEALNKdntrYSKLEKADILEMTVKYLKQLQ 51
bHLH-O_ESM5_like cd18916
basic helix-loop-helix-orange (bHLH-O) domain found in Drosophila melanogaster Enhancer of ...
 21-71 3.98e-03

basic helix-loop-helix-orange (bHLH-O) domain found in Drosophila melanogaster Enhancer of split proteins, E(spl)m5, E(spl)m8 and similar proteins; The family includes two bHLH-O transcriptional repressors, E(spl)m5 and E(spl)m8, which participate in the control of cell fate choice by uncommitted neuroectodermal cells in the embryo. They bind DNA on N-box motifs, 5'-CACNAG-3'.


Pssm-ID: 381486 [Multi-domain]  Cd Length: 59  Bit Score: 35.97  E-value: 3.98e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 24645243  21 IERRRRNKMTAYITELSDMVPTCSAL--ARKPDKLTILRMAVAHMKALRGTGN 71
Cdd:cd18916   7 LERQRRARINKCLSELKTLVAECSGDdgCLRMDKAEMLETAVAFMRQQQTAKN 59
PAS COG2202
PAS domain [Signal transduction mechanisms];
86-149 4.17e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 39.62  E-value: 4.17e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24645243  86 QELKHLILEAADGFLFVVSCDsGRVIYVSDSVTPVLNYTQSDWYGTSLYEHIHPDDREKIREQL 149
Cdd:COG2202 136 EERLRLLVENAPDGIFVLDLD-GRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELL 198
bHLHzip_scHMS1_like cd11399
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae transcription ...
 18-68 4.22e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae transcription factor HMS1 and similar proteins; HMS1, also termed high-copy MEP suppressor protein 1, is a putative bHLHzip transcription factor involved in exit from mitosis and pseudohyphal differentiation.


Pssm-ID: 381405 [Multi-domain]  Cd Length: 96  Bit Score: 37.07  E-value: 4.22e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243  18 HCEIERRRRNKMTAYITELSDMVPTC-------------------SALARKPDKLTILRMAVAHMKALRG 68
Cdd:cd11399   7 HNMIEKRYRSNINDRIAELRDSVPALreayksargededeedlggLTPATKLNKATILSKATEYIRHLEK 76
bHLH_ScINO2_like cd11388
basic helix-loop-helix (bHLH) domain found in Saccharomyces cerevisiae protein INO2 and ...
 14-67 6.71e-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: 35.79  E-value: 6.71e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24645243  14 SRENHCEIERRRRNKMTAYITELSDMVPTCSALARKP-DKLTILRMAVAHMKALR 67
Cdd:cd11388   3 KKWKHVEAEKKRRNQIKKGFEDLINLINYPRNNNEKRiSKSELLNKAVDDIRGLL 57
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
292-371 8.26e-03

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 39.06  E-value: 8.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645243 292 DGKFTFVDQRVLNILGYTPTELLGKICYDFFHPEDQshMKESFDQVLKQKGQMFSLLYRARAKNSEYVWLRTQAYAFLNP 371
Cdd:COG3852  26 DGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSP--LRELLERALAEGQPVTEREVTLRRKDGEERPVDVSVSPLRDA 103
bHLH-PAS_HIF cd11433
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor (HIF) ...
 23-64 9.17e-03

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in hypoxia-inducible factor (HIF) family; The HIF family contains bHLH-PAS transcription regulators involved in oxygen homeostasis, including HIF1a, HIF2a, and HIF3a. They have been implicated in development, postnatal physiology as well as disease pathogenesis. HIF1a, also termed HIF-1-alpha, or HIF1-alpha, or ARNT-interacting protein, or Basic-helix-loop-helix-PAS protein MOP1, or Class E basic helix-loop-helix protein 78 (bHLHe78), or Member of PAS protein 1, or PAS domain-containing protein 8 (PASD8), functions as a master transcriptional regulator of the adaptive response to hypoxia. HIF2a, also termed HIF-2-alpha, or HIF2-alpha, or endothelial PAS domain-containing protein 1 (EPAS-1), or Basic-helix-loop-helix-PAS protein MOP2, or Class E basic helix-loop-helix protein 73 (bHLHe73), or Member of PAS protein 2, or PAS domain-containing protein 2 (PASD2), or HIF-1-alpha-like factor (HLF), is a bHLH-PAS transcription factor involved in the induction of oxygen regulated genes. HIF3a, also termed HIF-3-alpha, or HIF3-alpha, or endothelial PAS domain-containing protein 1 (EPAS-1), or Basic-helix-loop-helix-PAS protein MOP7, or Class E basic helix-loop-helix protein 17 (bHLHe17), or Member of PAS protein 7, or PAS domain-containing protein 7 (PASD7), or HIF3-alpha-1, or inhibitory PAS domain protein (IPAS), is a bHLH-PAS transcriptional regulator in adaptive response to low oxygen tension. It plays a role in the regulation of hypoxia-inducible gene expression.


Pssm-ID: 381439  Cd Length: 58  Bit Score: 34.91  E-value: 9.17e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24645243  23 RRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVAHMK 64
Cdd:cd11433  10 RCRRGKESEIFYELAHQLPLPHSVSSQLDKASIMRLTISYLK 51
 
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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