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Conserved domains on  [gi|1622899285|ref|XP_028696093|]
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hypoxia-inducible factor 3-alpha isoform X8 [Macaca mulatta]

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), ...
 172-277 1.77e-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: 78.11  E-value: 1.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899285 172 FLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALD-SDAVSKSIHTLLSKGQAVTGQYRFLARNGGYLWTQTQ 250
Cdd:pfam14598   4 FTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDlRTAKSHLREIIQTRGRATSPSYRLRLRDGDFLSVHTK 83

                          90       100
                  ....*....|....*....|....*..
gi 1622899285 251 ATVVSGGRGPQSESIVCVHFLISRVEE 277
Cdd:pfam14598  84 SKLFLNQNSNQQPFIMCTHTILREENA 110
HIF-1 pfam11413
Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic ...
 409-440 2.92e-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: 61.16  E-value: 2.92e-12
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1622899285 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 4.96e-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: 4.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622899285  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), ...
 172-277 1.77e-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: 78.11  E-value: 1.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899285 172 FLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALD-SDAVSKSIHTLLSKGQAVTGQYRFLARNGGYLWTQTQ 250
Cdd:pfam14598   4 FTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDlRTAKSHLREIIQTRGRATSPSYRLRLRDGDFLSVHTK 83

                          90       100
                  ....*....|....*....|....*..
gi 1622899285 251 ATVVSGGRGPQSESIVCVHFLISRVEE 277
Cdd:pfam14598  84 SKLFLNQNSNQQPFIMCTHTILREENA 110
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 172-269 5.69e-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 [Multi-domain]  Cd Length: 103  Bit Score: 73.82  E-value: 5.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899285 172 FLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARNGGYLWTQTQA 251
Cdd:cd00130     4 GVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSL 83

                          90
                  ....*....|....*...
gi 1622899285 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 2.92e-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: 61.16  E-value: 2.92e-12
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1622899285 409 IAQDADALDLEMLAPYISMDDDFQLNASEQLP 440
Cdd:pfam11413   1 TTQDMEDLDLEMLAPYIPMDDDFQLNPIIPEE 32
PAS COG2202
PAS domain [Signal transduction mechanisms];
178-293 1.42e-07

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 53.10  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899285 178 LDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARNGGYLWTQTQATVVSGG 257
Cdd:COG2202    29 LDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDE 108

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622899285 258 RGpQSESIVCVHFLIS---RVEETgvvlsLEQTEQHSRR 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 6.86e-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: 6.86e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622899285  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 4.96e-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: 4.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622899285  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), ...
 172-277 1.77e-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: 78.11  E-value: 1.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899285 172 FLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALD-SDAVSKSIHTLLSKGQAVTGQYRFLARNGGYLWTQTQ 250
Cdd:pfam14598   4 FTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDlRTAKSHLREIIQTRGRATSPSYRLRLRDGDFLSVHTK 83

                          90       100
                  ....*....|....*....|....*..
gi 1622899285 251 ATVVSGGRGPQSESIVCVHFLISRVEE 277
Cdd:pfam14598  84 SKLFLNQNSNQQPFIMCTHTILREENA 110
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 182-269 1.89e-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: 77.38  E-value: 1.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899285 182 FTYCDDRIAEVAGYSPDDLIG--CSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARNGGYLWTQTQATVVSGGRG 259
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80

                          90
                  ....*....|
gi 1622899285 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 5.69e-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 [Multi-domain]  Cd Length: 103  Bit Score: 73.82  E-value: 5.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899285 172 FLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARNGGYLWTQTQA 251
Cdd:cd00130     4 GVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSL 83

                          90
                  ....*....|....*...
gi 1622899285 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 2.92e-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: 61.16  E-value: 2.92e-12
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1622899285 409 IAQDADALDLEMLAPYISMDDDFQLNASEQLP 440
Cdd:pfam11413   1 TTQDMEDLDLEMLAPYIPMDDDFQLNPIIPEE 32
PAS COG2202
PAS domain [Signal transduction mechanisms];
178-293 1.42e-07

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 53.10  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899285 178 LDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARNGGYLWTQTQATVVSGG 257
Cdd:COG2202    29 LDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDE 108

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622899285 258 RGpQSESIVCVHFLIS---RVEETgvvlsLEQTEQHSRR 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 6.86e-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: 6.86e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622899285  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 2.12e-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: 43.95  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899285 181 KFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLL-SKGQAVTGQYRFLARNGGYLWTQTQATVVSGGRG 259
Cdd:pfam00989  22 RILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALlQGEESRGFEVSFRVPDGRPRHVEVRASPVRDAGG 101

                          90
                  ....*....|
gi 1622899285 260 pQSESIVCVH 269
Cdd:pfam00989 102 -EILGFLGVL 110
PAS COG2202
PAS domain [Signal transduction mechanisms];
176-261 4.99e-05

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 45.40  E-value: 4.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622899285 176 HSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLSKG-QAVTGQYRFLARNGGYLWTQTQATVV 254
Cdd:COG2202   153 LDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGrESYELELRLKDGDGRWVWVEASAVPL 232


                  ....*..
gi 1622899285 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 ...
 232-273 6.02e-04

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: 37.55  E-value: 6.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1622899285  232 TGQYRFLARNGGYLWTQTQATVVSGGRGpQSESIVCVHFLIS 273
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDG-EVEGILGVVRDIT 41
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 51-101 4.96e-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: 4.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622899285  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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