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Conserved domains on  [gi|4504385|ref|NP_001521|]
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hypoxia-inducible factor 1-alpha isoform 1 [Homo sapiens]

Protein Classification

PAS and HIF-1a_CTAD domain-containing protein (domain architecture ID 11512674)

protein containing domains HLH, PAS, HIF-1, and HIF-1a_CTAD

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
254-339 3.80e-20

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: 312074  Cd Length: 89  Bit Score: 87.78  E-value: 3.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385    254 YCDERITELMGYEPEELLGR--SIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNtKNSQ 331
Cdd:pfam08447   3 YWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRD-ENGK 81

                  ....*...
gi 4504385    332 PQCIVCVN 339
Cdd:pfam08447  82 PVRVIGVA 89
HIF-1a_CTAD pfam08778
HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) ...
789-825 4.22e-15

HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) is the regulatory subunit of the heterodimeric transcription factor HIF-1. It plays a key role in cellular response to low oxygen tension. This region corresponds to the C terminal transactivation domain.


:

Pssm-ID: 285931  Cd Length: 37  Bit Score: 72.03  E-value: 4.22e-15
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 4504385    789 ESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQV 825
Cdd:pfam08778   1 LSGLPQLTRYDCEVNAPLQGRSHLLQGEELLRALDQV 37
HIF-1 pfam11413
Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic ...
552-581 1.43e-10

Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic homeostatic responses to oxygen availability. In the presence of oxygen HIF-1 alpha is targeted for proteasomal degradation by pHVL, a ubiquitination complex.


:

Pssm-ID: 314369  Cd Length: 31  Bit Score: 58.86  E-value: 1.43e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 4504385    552 TQDT-DLDLEMLAPYIPMDDDFQLRSFDQLS 581
Cdd:pfam11413   1 TQDMeDLDLEMLAPYIPMDDDFQLNPIDPLE 31
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
93-148 7.64e-10

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: 57.41  E-value: 7.64e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 4504385      93 LKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREML 148
Cdd:smart00091   7 LESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEAL 62
HLH cd00083
Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription ...
15-68 1.33e-07

Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, dimerization creates a parallel, left-handed, four helix bundle; the basic region N-terminal to the first amphipathic helix mediates high-affinity DNA-binding; there are several groups of HLH proteins: those (E12/E47) which bind specific hexanucleotide sequences such as E-box (5-CANNTG-3) or StRE 5-ATCACCCCAC-3), those lacking the basic domain (Emc, Id) function as negative regulators since they fail to bind DNA, those (hairy, E(spl), deadpan) which repress transcription although they can bind specific hexanucleotide sequences such as N-box (5-CACGc/aG-3), those which have a COE domain (Collier/Olf-1/EBF) which is involved in both in dimerization and in DNA binding, and those which bind pentanucleotides ACGTG or GCGTG and have a PAS domain which allows the dimerization between PAS proteins, the binding of small molecules (e.g., dioxin), and interactions with non-PAS proteins.


:

Pssm-ID: 238036  Cd Length: 60  Bit Score: 50.68  E-value: 1.33e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 4504385   15 SERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNvSSHLDKASVMRLTISYLR 68
Cdd:cd00083   1 RKSRREAHNLRERRRRERINDAFDELRSLLPTLPP-SKKLSKAEILRKAVDYIK 53
 
Name Accession Description Interval E-value
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
254-339 3.80e-20

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: 312074  Cd Length: 89  Bit Score: 87.78  E-value: 3.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385    254 YCDERITELMGYEPEELLGR--SIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNtKNSQ 331
Cdd:pfam08447   3 YWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRD-ENGK 81

                  ....*...
gi 4504385    332 PQCIVCVN 339
Cdd:pfam08447  82 PVRVIGVA 89
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
239-338 2.23e-16

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  Cd Length: 103  Bit Score: 77.29  E-value: 2.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385  239 SKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVE 318
Cdd:cd00130   1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                        90       100
                ....*....|....*....|
gi 4504385  319 TQATVIYNTKNSQPQCIVCV 338
Cdd:cd00130  81 VSLTPIRDEGGEVIGLLGVV 100
HIF-1a_CTAD pfam08778
HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) ...
789-825 4.22e-15

HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) is the regulatory subunit of the heterodimeric transcription factor HIF-1. It plays a key role in cellular response to low oxygen tension. This region corresponds to the C terminal transactivation domain.


Pssm-ID: 285931  Cd Length: 37  Bit Score: 72.03  E-value: 4.22e-15
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 4504385    789 ESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQV 825
Cdd:pfam08778   1 LSGLPQLTRYDCEVNAPLQGRSHLLQGEELLRALDQV 37
HIF-1 pfam11413
Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic ...
552-581 1.43e-10

Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic homeostatic responses to oxygen availability. In the presence of oxygen HIF-1 alpha is targeted for proteasomal degradation by pHVL, a ubiquitination complex.


Pssm-ID: 314369  Cd Length: 31  Bit Score: 58.86  E-value: 1.43e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 4504385    552 TQDT-DLDLEMLAPYIPMDDDFQLRSFDQLS 581
Cdd:pfam11413   1 TQDMeDLDLEMLAPYIPMDDDFQLNPIDPLE 31
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
93-148 7.64e-10

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: 57.41  E-value: 7.64e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 4504385      93 LKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREML 148
Cdd:smart00091   7 LESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEAL 62
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
96-150 1.48e-09

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  Cd Length: 103  Bit Score: 57.64  E-value: 1.48e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4504385   96 LDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTH 150
Cdd:cd00130   1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLEN 55
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
239-295 2.84e-08

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: 52.79  E-value: 2.84e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 4504385     239 SKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMF 295
Cdd:smart00091  10 LPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLL 66
HLH cd00083
Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription ...
15-68 1.33e-07

Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, dimerization creates a parallel, left-handed, four helix bundle; the basic region N-terminal to the first amphipathic helix mediates high-affinity DNA-binding; there are several groups of HLH proteins: those (E12/E47) which bind specific hexanucleotide sequences such as E-box (5-CANNTG-3) or StRE 5-ATCACCCCAC-3), those lacking the basic domain (Emc, Id) function as negative regulators since they fail to bind DNA, those (hairy, E(spl), deadpan) which repress transcription although they can bind specific hexanucleotide sequences such as N-box (5-CACGc/aG-3), those which have a COE domain (Collier/Olf-1/EBF) which is involved in both in dimerization and in DNA binding, and those which bind pentanucleotides ACGTG or GCGTG and have a PAS domain which allows the dimerization between PAS proteins, the binding of small molecules (e.g., dioxin), and interactions with non-PAS proteins.


Pssm-ID: 238036  Cd Length: 60  Bit Score: 50.68  E-value: 1.33e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 4504385   15 SERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNvSSHLDKASVMRLTISYLR 68
Cdd:cd00083   1 RKSRREAHNLRERRRRERINDAFDELRSLLPTLPP-SKKLSKAEILRKAVDYIK 53
HLH smart00353
helix loop helix domain;
23-68 3.50e-07

helix loop helix domain;


Pssm-ID: 197674  Cd Length: 53  Bit Score: 49.52  E-value: 3.50e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 4504385      23 RDAARSRRSKESEVFYELAHQLPlPHNVSSHLDKASVMRLTISYLR 68
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLP-TLPKNKKLSKAEILRLAIEYIK 45
PAS COG2202
PAS domain [Signal transduction mechanisms];
99-338 6.36e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 225112  Cd Length: 232  Bit Score: 48.31  E-value: 6.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385   99 FVMVLTDDGDMIYISDNVNKYMGLTQFELTGhsVFDFTHPCDHEEMREMLTHrngLVKKGKEQNTQRSFFLRMKCTLTSR 178
Cdd:COG2202   1 LILVLDRDGRIIYANEAAEELLGYSAEELLG--LLLALHPEDRDRLRELLRR---LLAGEELLSEELRLVRKDGEERWVE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385  179 GRTMNIKSATWKVLHCTGHIHVYDTNSNQPQCGYKKPPMTCLVlicEPIPHPsnieipldsktfLSRHSLDMKFSYCDER 258
Cdd:COG2202  76 LSAAPLRDGEGRVLGLLGLRDITERKRAEEALRESEERLRALL---EASPDG------------IWVLDEDGRILYANPA 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385  259 ITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMF--TKGQVTTGQYRMLAKRGGYV-WVETQATVIYNtkNSQPQCI 335
Cdd:COG2202 141 AEELLGYSPEEELGRGLSDLIHPEDEERRELELARALaeGRGGPLEIEYRVRRKDGERVrWILSRISPVRD--DGEIVGV 218

                ...
gi 4504385  336 VCV 338
Cdd:COG2202 219 VGI 221
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
95-180 3.97e-04

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: 307226  Cd Length: 113  Bit Score: 40.86  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385     95 ALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLT--------HRNGLVKKGKEQNTQRS 166
Cdd:pfam00989   9 SLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRqallqgeeSRGFEVSFRVPDGRPRH 88
                          90
                  ....*....|....
gi 4504385    167 FFLRMKCTLTSRGR 180
Cdd:pfam00989  89 VEVRASPVRDAGGE 102
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
101-168 4.21e-03

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  Cd Length: 124  Bit Score: 38.04  E-value: 4.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504385    101 MVLTD-DGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRnglvkKGKEQNTQRSFF 168
Cdd:TIGR00229  16 IIVIDlEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERR-----LEGEPEPVSEER 79
 
Name Accession Description Interval E-value
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
254-339 3.80e-20

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: 312074  Cd Length: 89  Bit Score: 87.78  E-value: 3.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385    254 YCDERITELMGYEPEELLGR--SIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNtKNSQ 331
Cdd:pfam08447   3 YWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRD-ENGK 81

                  ....*...
gi 4504385    332 PQCIVCVN 339
Cdd:pfam08447  82 PVRVIGVA 89
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
242-343 1.45e-17

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: 317051  Cd Length: 112  Bit Score: 81.18  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385    242 FLSRHSLDMKFSYCD---ERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMF-TKGQVTTGQYRMLAKRGGYVWV 317
Cdd:pfam14598   3 FTTRHDMDGKIISIDtssLRASFSLGLEKDELVGRSIYDLCHPQDLRTAKSHLREVIdSNGRATSSSYRLRLRDGDFVYV 82
                          90       100
                  ....*....|....*....|....*.
gi 4504385    318 ETQATVIYNTKNSQPQCIVCVNYVVS 343
Cdd:pfam14598  83 HTKSKLFRNQKTNEQDFIMCTHTILR 108
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
239-338 2.23e-16

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  Cd Length: 103  Bit Score: 77.29  E-value: 2.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385  239 SKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVE 318
Cdd:cd00130   1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                        90       100
                ....*....|....*....|
gi 4504385  319 TQATVIYNTKNSQPQCIVCV 338
Cdd:cd00130  81 VSLTPIRDEGGEVIGLLGVV 100
HIF-1a_CTAD pfam08778
HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) ...
789-825 4.22e-15

HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) is the regulatory subunit of the heterodimeric transcription factor HIF-1. It plays a key role in cellular response to low oxygen tension. This region corresponds to the C terminal transactivation domain.


Pssm-ID: 285931  Cd Length: 37  Bit Score: 72.03  E-value: 4.22e-15
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 4504385    789 ESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQV 825
Cdd:pfam08778   1 LSGLPQLTRYDCEVNAPLQGRSHLLQGEELLRALDQV 37
HIF-1 pfam11413
Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic ...
552-581 1.43e-10

Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic homeostatic responses to oxygen availability. In the presence of oxygen HIF-1 alpha is targeted for proteasomal degradation by pHVL, a ubiquitination complex.


Pssm-ID: 314369  Cd Length: 31  Bit Score: 58.86  E-value: 1.43e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 4504385    552 TQDT-DLDLEMLAPYIPMDDDFQLRSFDQLS 581
Cdd:pfam11413   1 TQDMeDLDLEMLAPYIPMDDDFQLNPIDPLE 31
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
93-148 7.64e-10

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: 57.41  E-value: 7.64e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 4504385      93 LKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREML 148
Cdd:smart00091   7 LESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEAL 62
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
96-150 1.48e-09

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  Cd Length: 103  Bit Score: 57.64  E-value: 1.48e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4504385   96 LDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTH 150
Cdd:cd00130   1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLEN 55
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
239-295 2.84e-08

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: 52.79  E-value: 2.84e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 4504385     239 SKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMF 295
Cdd:smart00091  10 LPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLL 66
HLH cd00083
Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription ...
15-68 1.33e-07

Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, dimerization creates a parallel, left-handed, four helix bundle; the basic region N-terminal to the first amphipathic helix mediates high-affinity DNA-binding; there are several groups of HLH proteins: those (E12/E47) which bind specific hexanucleotide sequences such as E-box (5-CANNTG-3) or StRE 5-ATCACCCCAC-3), those lacking the basic domain (Emc, Id) function as negative regulators since they fail to bind DNA, those (hairy, E(spl), deadpan) which repress transcription although they can bind specific hexanucleotide sequences such as N-box (5-CACGc/aG-3), those which have a COE domain (Collier/Olf-1/EBF) which is involved in both in dimerization and in DNA binding, and those which bind pentanucleotides ACGTG or GCGTG and have a PAS domain which allows the dimerization between PAS proteins, the binding of small molecules (e.g., dioxin), and interactions with non-PAS proteins.


Pssm-ID: 238036  Cd Length: 60  Bit Score: 50.68  E-value: 1.33e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 4504385   15 SERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNvSSHLDKASVMRLTISYLR 68
Cdd:cd00083   1 RKSRREAHNLRERRRRERINDAFDELRSLLPTLPP-SKKLSKAEILRKAVDYIK 53
HLH smart00353
helix loop helix domain;
23-68 3.50e-07

helix loop helix domain;


Pssm-ID: 197674  Cd Length: 53  Bit Score: 49.52  E-value: 3.50e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 4504385      23 RDAARSRRSKESEVFYELAHQLPlPHNVSSHLDKASVMRLTISYLR 68
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLP-TLPKNKKLSKAEILRLAIEYIK 45
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
302-343 5.43e-07

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 48.72  E-value: 5.43e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 4504385     302 TGQYRMLAKRGGYVWVETQATVIYNTKNsQPQCIVCVNYVVS 343
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDG-EVEGILGVVRDIT 41
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
251-338 3.20e-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: 307226  Cd Length: 113  Bit Score: 47.41  E-value: 3.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385    251 KFSYCDERITELMGYEPEELLGRSIYEYYHALDS----DHLTKTHHDMftkGQVTTGQYRMLAKRGGYVWVETQATVIYN 326
Cdd:pfam00989  22 RILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDaevaELLRQALLQG---EESRGFEVSFRVPDGRPRHVEVRASPVRD 98
                          90
                  ....*....|..
gi 4504385    327 tKNSQPQCIVCV 338
Cdd:pfam00989  99 -AGGEILGFLGV 109
PAS COG2202
PAS domain [Signal transduction mechanisms];
99-338 6.36e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 225112  Cd Length: 232  Bit Score: 48.31  E-value: 6.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385   99 FVMVLTDDGDMIYISDNVNKYMGLTQFELTGhsVFDFTHPCDHEEMREMLTHrngLVKKGKEQNTQRSFFLRMKCTLTSR 178
Cdd:COG2202   1 LILVLDRDGRIIYANEAAEELLGYSAEELLG--LLLALHPEDRDRLRELLRR---LLAGEELLSEELRLVRKDGEERWVE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385  179 GRTMNIKSATWKVLHCTGHIHVYDTNSNQPQCGYKKPPMTCLVlicEPIPHPsnieipldsktfLSRHSLDMKFSYCDER 258
Cdd:COG2202  76 LSAAPLRDGEGRVLGLLGLRDITERKRAEEALRESEERLRALL---EASPDG------------IWVLDEDGRILYANPA 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385  259 ITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMF--TKGQVTTGQYRMLAKRGGYV-WVETQATVIYNtkNSQPQCI 335
Cdd:COG2202 141 AEELLGYSPEEELGRGLSDLIHPEDEERRELELARALaeGRGGPLEIEYRVRRKDGERVrWILSRISPVRD--DGEIVGV 218

                ...
gi 4504385  336 VCV 338
Cdd:COG2202 219 VGI 221
PAS_9 pfam13426
PAS domain;
249-350 3.14e-04

PAS domain;


Pssm-ID: 315989  Cd Length: 102  Bit Score: 41.29  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385    249 DMKFSYCDERITELMGYEPEELLGRSIYEYYHalDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNTK 328
Cdd:pfam13426  10 DGRIIYVNPAALRLLGYTREELLGKSLTDLFG--EPEDAERLREALREGRKVRELEVVLVRKDGEPFPVLVSASPIKDDG 87
                          90       100
                  ....*....|....*....|..
gi 4504385    329 NsqpqcivcvNYVVSGIIQHDL 350
Cdd:pfam13426  88 G---------ELVGIIAILRDI 100
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
95-180 3.97e-04

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: 307226  Cd Length: 113  Bit Score: 40.86  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504385     95 ALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLT--------HRNGLVKKGKEQNTQRS 166
Cdd:pfam00989   9 SLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRqallqgeeSRGFEVSFRVPDGRPRH 88
                          90
                  ....*....|....
gi 4504385    167 FFLRMKCTLTSRGR 180
Cdd:pfam00989  89 VEVRASPVRDAGGE 102
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
101-168 4.21e-03

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  Cd Length: 124  Bit Score: 38.04  E-value: 4.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504385    101 MVLTD-DGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRnglvkKGKEQNTQRSFF 168
Cdd:TIGR00229  16 IIVIDlEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERR-----LEGEPEPVSEER 79
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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