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Conserved domains on  [gi|326807022|ref|NP_071907|]
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hypoxia-inducible factor 3-alpha isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAS_11 super family cl37882
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
 172-279 4.14e-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).


The actual alignment was detected with superfamily member pfam14598:

Pssm-ID: 464214 [Multi-domain]  Cd Length: 110  Bit Score: 77.33  E-value: 4.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326807022  172 FLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALD-SDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQ 250
Cdd:pfam14598   4 FTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDlRTAKSHLREIIQTRGRATSPSYRLRLRDGDFLSVHTK 83

                          90       100
                  ....*....|....*....|....*....
gi 326807022  251 ATVVSGGRGPQSESIVCVHFLISqvEETG 279
Cdd:pfam14598  84 SKLFLNQNSNQQPFIMCTHTILR--EENA 110
HIF-1 pfam11413
Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic ...
 409-440 9.15e-12

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: 463274  Cd Length: 32  Bit Score: 59.62  E-value: 9.15e-12
                          10        20        30
                  ....*....|....*....|....*....|..
gi 326807022  409 IAQDADALDLEMLAPYISMDDDFQLNASEQLP 440
Cdd:pfam11413   1 TTQDMEDLDLEMLAPYIPMDDDFQLNPIIPEE 32
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 51-101 4.90e-03

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: 36.84  E-value: 4.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 326807022  51 PQLELIGHSIFDFIHPCDQEELQDALtpQQTLSRRKveaPTERCFSLRMKS 101
Cdd:cd00130   28 SPEELIGKSLLDLIHPEDREELRERL--ENLLSGGE---PVTLEVRLRRKD 73
 
Name Accession Description Interval E-value
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
 172-279 4.14e-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: 464214 [Multi-domain]  Cd Length: 110  Bit Score: 77.33  E-value: 4.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326807022  172 FLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALD-SDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQ 250
Cdd:pfam14598   4 FTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDlRTAKSHLREIIQTRGRATSPSYRLRLRDGDFLSVHTK 83

                          90       100
                  ....*....|....*....|....*....
gi 326807022  251 ATVVSGGRGPQSESIVCVHFLISqvEETG 279
Cdd:pfam14598  84 SKLFLNQNSNQQPFIMCTHTILR--EENA 110
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 172-269 1.39e-15

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: 72.67  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326807022 172 FLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQA 251
Cdd:cd00130    4 GVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSL 83

                         90
                 ....*....|....*...
gi 326807022 252 TVVSGGRGPQSESIVCVH 269
Cdd:cd00130   84 TPIRDEGGEVIGLLGVVR 101
HIF-1 pfam11413
Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic ...
 409-440 9.15e-12

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: 463274  Cd Length: 32  Bit Score: 59.62  E-value: 9.15e-12
                          10        20        30
                  ....*....|....*....|....*....|..
gi 326807022  409 IAQDADALDLEMLAPYISMDDDFQLNASEQLP 440
Cdd:pfam11413   1 TTQDMEDLDLEMLAPYIPMDDDFQLNPIIPEE 32
PAS COG2202
PAS domain [Signal transduction mechanisms];
178-293 3.66e-07

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 51.95  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326807022 178 LDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQATVVSGG 257
Cdd:COG2202   29 LDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDE 108

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 326807022 258 RGpQSESIVCVHFLIS---QVEETgvvlsLEQTEQHSRR 293
Cdd:COG2202  109 DG-EITGFVGIARDITerkRAEEA-----LRESEERLRL 141
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 172-226 6.77e-07

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: 46.62  E-value: 6.77e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 326807022   172 FLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLS 226
Cdd:smart00091  13 GIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 51-101 4.90e-03

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: 36.84  E-value: 4.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 326807022  51 PQLELIGHSIFDFIHPCDQEELQDALtpQQTLSRRKveaPTERCFSLRMKS 101
Cdd:cd00130   28 SPEELIGKSLLDLIHPEDREELRERL--ENLLSGGE---PVTLEVRLRRKD 73
 
Name Accession Description Interval E-value
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
 172-279 4.14e-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: 464214 [Multi-domain]  Cd Length: 110  Bit Score: 77.33  E-value: 4.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326807022  172 FLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALD-SDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQ 250
Cdd:pfam14598   4 FTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDlRTAKSHLREIIQTRGRATSPSYRLRLRDGDFLSVHTK 83

                          90       100
                  ....*....|....*....|....*....
gi 326807022  251 ATVVSGGRGPQSESIVCVHFLISqvEETG 279
Cdd:pfam14598  84 SKLFLNQNSNQQPFIMCTHTILR--EENA 110
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 182-269 8.37e-17

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: 75.45  E-value: 8.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326807022  182 FTYCDDRIAEVAGYSPDDLIG--CSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQATVVSGGRG 259
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80

                          90
                  ....*....|
gi 326807022  260 pQSESIVCVH 269
Cdd:pfam08447  81 -KPVRVIGVA 89
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 172-269 1.39e-15

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: 72.67  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326807022 172 FLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQA 251
Cdd:cd00130    4 GVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSL 83

                         90
                 ....*....|....*...
gi 326807022 252 TVVSGGRGPQSESIVCVH 269
Cdd:cd00130   84 TPIRDEGGEVIGLLGVVR 101
HIF-1 pfam11413
Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic ...
 409-440 9.15e-12

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: 463274  Cd Length: 32  Bit Score: 59.62  E-value: 9.15e-12
                          10        20        30
                  ....*....|....*....|....*....|..
gi 326807022  409 IAQDADALDLEMLAPYISMDDDFQLNASEQLP 440
Cdd:pfam11413   1 TTQDMEDLDLEMLAPYIPMDDDFQLNPIIPEE 32
PAS COG2202
PAS domain [Signal transduction mechanisms];
178-293 3.66e-07

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 51.95  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326807022 178 LDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQATVVSGG 257
Cdd:COG2202   29 LDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDE 108

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 326807022 258 RGpQSESIVCVHFLIS---QVEETgvvlsLEQTEQHSRR 293
Cdd:COG2202  109 DG-EITGFVGIARDITerkRAEEA-----LRESEERLRL 141
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 172-226 6.77e-07

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: 46.62  E-value: 6.77e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 326807022   172 FLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLS 226
Cdd:smart00091  13 GIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 181-269 5.21e-05

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: 42.79  E-value: 5.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326807022  181 KFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLL-SKGQAVTGQYRFLARSGGYLWTQTQATVVSGGRG 259
Cdd:pfam00989  22 RILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALlQGEESRGFEVSFRVPDGRPRHVEVRASPVRDAGG 101

                          90
                  ....*....|
gi 326807022  260 pQSESIVCVH 269
Cdd:pfam00989 102 -EILGFLGVL 110
PAS COG2202
PAS domain [Signal transduction mechanisms];
176-261 5.73e-05

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 45.02  E-value: 5.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326807022 176 HSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLSKG-QAVTGQYRFLARSGGYLWTQTQATVV 254
Cdd:COG2202  153 LDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGrESYELELRLKDGDGRWVWVEASAVPL 232


                 ....*..
gi 326807022 255 SGGRGPQ 261
Cdd:COG2202  233 RDGGEVI 239
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 232-274 1.07e-03

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: 37.16  E-value: 1.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 326807022   232 TGQYRFLARSGGYLWTQTQATVVSGGRGpQSESIVCVHFLISQ 274
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDG-EVEGILGVVRDITE 42
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 51-101 4.90e-03

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: 36.84  E-value: 4.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 326807022  51 PQLELIGHSIFDFIHPCDQEELQDALtpQQTLSRRKveaPTERCFSLRMKS 101
Cdd:cd00130   28 SPEELIGKSLLDLIHPEDREELRERL--ENLLSGGE---PVTLEVRLRRKD 73
 
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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