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Conserved domains on  [gi|26331322|dbj|BAC29391|]
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unnamed protein product [Mus musculus]

Protein Classification

PAS domain-containing protein( domain architecture ID 12091914)

PAS domain-containing protein binds ligand(s) and may act as sensors for light and oxygen in signal transduction; similar to Homo sapiens endothelial PAS domain-containing protein 1

CATH:  3.30.450.20
Gene Ontology:  GO:0005515|GO:0007165
PubMed:  15009198|33647528|16939366|10357859|9382818|21663441
SCOP:  3000471

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 ...
 280-368 3.11e-13

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: 65.44  E-value: 3.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331322   280 FLEVDERAVPLLGYLPQDLIGT--SILTYLHPEDRPLMVAIHQKVLKYAGhpPFEHsPVRFCTQNGEYVILDSSWSSFVN 357
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGE--PYSG-EYRIRRKDGEYRWVEARARPIRD 77

                          90
                  ....*....|.
gi 26331322   358 pWSRKVSFIIG 368
Cdd:pfam08447  78 -ENGKPVRVIG 87
 
Name Accession Description Interval E-value
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 280-368 3.11e-13

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: 65.44  E-value: 3.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331322   280 FLEVDERAVPLLGYLPQDLIGT--SILTYLHPEDRPLMVAIHQKVLKYAGhpPFEHsPVRFCTQNGEYVILDSSWSSFVN 357
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGE--PYSG-EYRIRRKDGEYRWVEARARPIRD 77

                          90
                  ....*....|.
gi 26331322   358 pWSRKVSFIIG 368
Cdd:pfam08447  78 -ENGKPVRVIG 87
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 280-372 3.24e-13

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: 65.73  E-value: 3.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331322 280 FLEVDERAVPLLGYLPQDLIGTSILTYLHPEDRPLMVAIHQKVLKYAGHPPFEhspVRFCTQNGEYVILDSSWSSFVNPW 359
Cdd:cd00130  14 ILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLE---VRLRRKDGSVIWVLVSLTPIRDEG 90

                        90
                ....*....|...
gi 26331322 360 SRKVSFIIGRHKV 372
Cdd:cd00130  91 GEVIGLLGVVRDI 103
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 280-324 1.49e-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: 51.25  E-value: 1.49e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 26331322    280 FLEVDERAVPLLGYLPQDLIGTSILTYLHPEDRPLMVAIHQKVLK 324
Cdd:smart00091  23 ILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS COG2202
PAS domain [Signal transduction mechanisms];
279-406 2.09e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 40.01  E-value: 2.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331322 279 VFLEVDERAVPLLGYLPQDLIGTSILTYLHPEDRPLMVAIHQKVLKYAGHPPFEhspVRFCTQNGEYVILDSSWSSFVNP 358
Cdd:COG2202  32 RILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGE---LRNRRKDGSLFWVELSISPVRDE 108

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 26331322 359 WSRKVSFI-IGRhkvrtsplneDVfaTRIKKAAsndkdiAELQEQIHKL 406
Cdd:COG2202 109 DGEITGFVgIAR----------DI--TERKRAE------EALRESEERL 139
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 279-348 6.39e-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 [Multi-domain]  Cd Length: 124  Bit Score: 36.89  E-value: 6.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331322   279 VFLEVDERAVPLLGYLPQDLIGTSILTYLHPEDRPLMVAIHQKVLKYAGHPPFEhsPVRFCTQNGEYVIL 348
Cdd:TIGR00229  24 NILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSE--ERRVRRKDGSEIWV 91
 
Name Accession Description Interval E-value
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 280-368 3.11e-13

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: 65.44  E-value: 3.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331322   280 FLEVDERAVPLLGYLPQDLIGT--SILTYLHPEDRPLMVAIHQKVLKYAGhpPFEHsPVRFCTQNGEYVILDSSWSSFVN 357
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGE--PYSG-EYRIRRKDGEYRWVEARARPIRD 77

                          90
                  ....*....|.
gi 26331322   358 pWSRKVSFIIG 368
Cdd:pfam08447  78 -ENGKPVRVIG 87
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 280-372 3.24e-13

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: 65.73  E-value: 3.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331322 280 FLEVDERAVPLLGYLPQDLIGTSILTYLHPEDRPLMVAIHQKVLKYAGHPPFEhspVRFCTQNGEYVILDSSWSSFVNPW 359
Cdd:cd00130  14 ILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLE---VRLRRKDGSVIWVLVSLTPIRDEG 90

                        90
                ....*....|...
gi 26331322 360 SRKVSFIIGRHKV 372
Cdd:cd00130  91 GEVIGLLGVVRDI 103
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
 270-372 2.33e-09

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: 54.99  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331322   270 FTTTHTPGCVFLEVDERAVPLLGYLPQDLIGTSILTYLHPEDRPLMVAIHQKVLKYAGHppFEHSPVRFCTQNGEYVILD 349
Cdd:pfam14598   4 FTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDLRTAKSHLREIIQTRGR--ATSPSYRLRLRDGDFLSVH 81

                          90       100
                  ....*....|....*....|...
gi 26331322   350 SSWSSFVNPWSRKVSFIIGRHKV 372
Cdd:pfam14598  82 TKSKLFLNQNSNQQPFIMCTHTI 104
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 267-366 7.91e-09

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: 53.58  E-value: 7.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331322   267 KRIFTTTHTPGCV------FLEVDERAVPLLGYLPQDLIGTSILTYLHPEDRPLMVAIHQKVLKyAGHPPFEHSpVRFCT 340
Cdd:pfam00989   4 RAILESLPDGIFVvdedgrILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALL-QGEESRGFE-VSFRV 81

                          90       100
                  ....*....|....*....|....*.
gi 26331322   341 QNGEYVILDSSWSSFVNPWSRKVSFI 366
Cdd:pfam00989  82 PDGRPRHVEVRASPVRDAGGEILGFL 107
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 280-324 1.49e-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: 51.25  E-value: 1.49e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 26331322    280 FLEVDERAVPLLGYLPQDLIGTSILTYLHPEDRPLMVAIHQKVLK 324
Cdd:smart00091  23 ILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS COG2202
PAS domain [Signal transduction mechanisms];
279-406 2.09e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 40.01  E-value: 2.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331322 279 VFLEVDERAVPLLGYLPQDLIGTSILTYLHPEDRPLMVAIHQKVLKYAGHPPFEhspVRFCTQNGEYVILDSSWSSFVNP 358
Cdd:COG2202  32 RILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGE---LRNRRKDGSLFWVELSISPVRDE 108

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 26331322 359 WSRKVSFI-IGRhkvrtsplneDVfaTRIKKAAsndkdiAELQEQIHKL 406
Cdd:COG2202 109 DGEITGFVgIAR----------DI--TERKRAE------EALRESEERL 139
PAS COG2202
PAS domain [Signal transduction mechanisms];
280-369 2.40e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 40.01  E-value: 2.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331322 280 FLEVDERAVPLLGYLPQDLIGTSILTYLHPEDRPLMVAIHQKVLkyAGHPPFEHSPVRFCTQNGEYVILDSSWSSFVNPW 359
Cdd:COG2202 159 ILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLL--EGGRESYELELRLKDGDGRWVWVEASAVPLRDGG 236

                        90
                ....*....|
gi 26331322 360 SRKVSFIIGR 369
Cdd:COG2202 237 EVIGVLGIVR 246
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 279-348 6.39e-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 [Multi-domain]  Cd Length: 124  Bit Score: 36.89  E-value: 6.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331322   279 VFLEVDERAVPLLGYLPQDLIGTSILTYLHPEDRPLMVAIHQKVLKYAGHPPFEhsPVRFCTQNGEYVIL 348
Cdd:TIGR00229  24 NILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSE--ERRVRRKDGSEIWV 91
 
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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