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Conserved domains on  [gi|7963664|gb|AAF71306|]
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bHLH-PAS transcription factor MOP9 [Homo sapiens]

Protein Classification

HLH and PAS domain-containing protein (domain architecture ID 13609959)

HLH and PAS domain-containing protein

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), ...
319-421 4.90e-22

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: 317051 [Multi-domain]  Cd Length: 112  Bit Score: 91.20  E-value: 4.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7963664    319 EFITRFAVNGKFVYVDQ---RATAILGYLPQELLGTSCYEYFHQDDHNNLTDKHKAVLQSKEKILTDSYKFRAKDGSFVT 395
Cdd:pfam14598   2 QFTTRHDMDGKIISIDTsslRASFSLGLEKDELVGRSIYDLCHPQDLRTAKSHLREVIDSNGRATSSSYRLRLRDGDFVY 81
                          90       100
                  ....*....|....*....|....*.
gi 7963664    396 LKSQWFSFTNPWTKELEYIVSVNTLV 421
Cdd:pfam14598  82 VHTKSKLFRNQKTNEQDFIMCTHTIL 107
HLH pfam00010
Helix-loop-helix DNA-binding domain;
58-110 3.00e-15

Helix-loop-helix DNA-binding domain;


:

Pssm-ID: 333763  Cd Length: 52  Bit Score: 69.87  E-value: 3.00e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 7963664     58 REAHSQTEKRRRDKMNNLIEELSAMIPQCNpmARKLDKLTVLRMAVQHLRSLK 110
Cdd:pfam00010   2 RRAHNERERRRRDRINDAFDELRELLPTPP--SKKLSKAEILRLAIEYIKHLQ 52
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
141-236 2.09e-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 [Multi-domain]  Cd Length: 103  Bit Score: 54.95  E-value: 2.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7963664  141 GFLFVVgCERGKILFVSKSVSKILNYDQASLTGQSLFDFLHPKDVAKVKEQL----SSFDISPREKLIDTKTGLQVHSNL 216
Cdd:cd00130   3 DGVIVL-DLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLenllSGGEPVTLEVRLRRKDGSVIWVLV 81
                        90       100
                ....*....|....*....|
gi 7963664  217 HAGRTRVYFGSRRSFFCRIK 236
Cdd:cd00130  82 SLTPIRDEGGEVIGLLGVVR 101
 
Name Accession Description Interval E-value
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
319-421 4.90e-22

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 [Multi-domain]  Cd Length: 112  Bit Score: 91.20  E-value: 4.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7963664    319 EFITRFAVNGKFVYVDQ---RATAILGYLPQELLGTSCYEYFHQDDHNNLTDKHKAVLQSKEKILTDSYKFRAKDGSFVT 395
Cdd:pfam14598   2 QFTTRHDMDGKIISIDTsslRASFSLGLEKDELVGRSIYDLCHPQDLRTAKSHLREVIDSNGRATSSSYRLRLRDGDFVY 81
                          90       100
                  ....*....|....*....|....*.
gi 7963664    396 LKSQWFSFTNPWTKELEYIVSVNTLV 421
Cdd:pfam14598  82 VHTKSKLFRNQKTNEQDFIMCTHTIL 107
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
319-417 3.83e-17

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: 76.90  E-value: 3.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7963664  319 EFITRFAVNGKFVYVDQRATAILGYLPQELLGTSCYEYFHQDDHNNLTDKHKAVLQsKEKILTDSYKFRAKDGSFVTLKS 398
Cdd:cd00130   3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLS-GGEPVTLEVRLRRKDGSVIWVLV 81
                        90
                ....*....|....*....
gi 7963664  399 QWFSFTNPWTKELEYIVSV 417
Cdd:cd00130  82 SLTPIRDEGGEVIGLLGVV 100
HLH pfam00010
Helix-loop-helix DNA-binding domain;
58-110 3.00e-15

Helix-loop-helix DNA-binding domain;


Pssm-ID: 333763  Cd Length: 52  Bit Score: 69.87  E-value: 3.00e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 7963664     58 REAHSQTEKRRRDKMNNLIEELSAMIPQCNpmARKLDKLTVLRMAVQHLRSLK 110
Cdd:pfam00010   2 RRAHNERERRRRDRINDAFDELRELLPTPP--SKKLSKAEILRLAIEYIKHLQ 52
HLH cd00083
Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription ...
58-110 7.46e-15

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: 68.78  E-value: 7.46e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 7963664   58 REAHSQTEKRRRDKMNNLIEELSAMIPQcNPMARKLDKLTVLRMAVQHLRSLK 110
Cdd:cd00083   5 REAHNLRERRRRERINDAFDELRSLLPT-LPPSKKLSKAEILRKAVDYIKSLQ 56
HLH smart00353
helix loop helix domain;
65-110 1.30e-13

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 65.32  E-value: 1.30e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 7963664      65 EKRRRDKMNNLIEELSAMIPQCnPMARKLDKLTVLRMAVQHLRSLK 110
Cdd:smart00353   4 ERRRRRKINEAFDELRSLLPTL-PKNKKLSKAEILRLAIEYIKSLQ 48
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
319-374 7.82e-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: 54.71  E-value: 7.82e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 7963664     319 EFITRFAVNGKFVYVDQRATAILGYLPQELLGTSCYEYFHQDDHNNLTDKHKAVLQ 374
Cdd:smart00091  12 DGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
141-236 2.09e-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 [Multi-domain]  Cd Length: 103  Bit Score: 54.95  E-value: 2.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7963664  141 GFLFVVgCERGKILFVSKSVSKILNYDQASLTGQSLFDFLHPKDVAKVKEQL----SSFDISPREKLIDTKTGLQVHSNL 216
Cdd:cd00130   3 DGVIVL-DLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLenllSGGEPVTLEVRLRRKDGSVIWVLV 81
                        90       100
                ....*....|....*....|
gi 7963664  217 HAGRTRVYFGSRRSFFCRIK 236
Cdd:cd00130  82 SLTPIRDEGGEVIGLLGVVR 101
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
130-192 8.35e-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.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 52.02  E-value: 8.35e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7963664     130 ELRHLILKTAEGFLFVVGcERGKILFVSKSVSKILNYDQASLTGQSLFDFLHPKDVAKVKEQL 192
Cdd:smart00091   1 ERLRAILESLPDGIFVLD-LDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEAL 62
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
130-236 2.17e-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.


Pssm-ID: 334337 [Multi-domain]  Cd Length: 112  Bit Score: 49.33  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7963664    130 ELRHLILKTAEGFLFVVGcERGKILFVSKSVSKILNYDQASLTGQSLFDFLHPKDVAKVKEQLSSF-----DISPREKLI 204
Cdd:pfam00989   1 EDLRAILESLPDGIFVVD-EDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEDDDAEVVELLRQAlrqgeESRGFEVTF 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 7963664    205 DTKTGLQVHSNLHAGRTRVYFGSRRSFFCRIK 236
Cdd:pfam00989  80 KLPDGRPRHVEVRASPVRDAGGEILGFLGFLR 111
PAS COG2202
PAS domain [Signal transduction mechanisms];
318-394 3.04e-05

PAS domain [Signal transduction mechanisms];


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 45.61  E-value: 3.04e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7963664  318 TEFITRFAVNGKFVYVDQRATAILGYLPQELLGTSCYEYFHQDDHNNLTDKHKAVLQSKE-KILTDSYKFRAKDGSFV 394
Cdd:COG2202 122 PDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSDLIHPEDEERRELELARALAEGRgGPLEIEYRVRRKDGERV 199
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
327-392 9.12e-05

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: 42.28  E-value: 9.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7963664    327 NGKFVYVDQRATAILGYLPQELLGTSCYEYFHQDDHNNLTDKHKAVLQSKEKILTDSYKFRAKDGS 392
Cdd:TIGR00229  22 EGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRRKDGS 87
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
130-233 5.80e-04

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: 39.97  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7963664    130 ELRHLILKTAEGFLFVVGcERGKILFVSKSVSKILNYDQASLTGQSLFDFLHPKDVAKVKEQLSSfDISPR------EKL 203
Cdd:TIGR00229   3 ERYRAIFESSPDAIIVID-LEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIER-RLEGEpepvseERR 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 7963664    204 IDTKTGLQVHSNLHAGRTRVYfGSRRSFFC 233
Cdd:TIGR00229  81 VRRKDGSEIWVEVSVSPIRTN-GGELGVVG 109
 
Name Accession Description Interval E-value
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
319-421 4.90e-22

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 [Multi-domain]  Cd Length: 112  Bit Score: 91.20  E-value: 4.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7963664    319 EFITRFAVNGKFVYVDQ---RATAILGYLPQELLGTSCYEYFHQDDHNNLTDKHKAVLQSKEKILTDSYKFRAKDGSFVT 395
Cdd:pfam14598   2 QFTTRHDMDGKIISIDTsslRASFSLGLEKDELVGRSIYDLCHPQDLRTAKSHLREVIDSNGRATSSSYRLRLRDGDFVY 81
                          90       100
                  ....*....|....*....|....*.
gi 7963664    396 LKSQWFSFTNPWTKELEYIVSVNTLV 421
Cdd:pfam14598  82 VHTKSKLFRNQKTNEQDFIMCTHTIL 107
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
319-417 3.83e-17

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: 76.90  E-value: 3.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7963664  319 EFITRFAVNGKFVYVDQRATAILGYLPQELLGTSCYEYFHQDDHNNLTDKHKAVLQsKEKILTDSYKFRAKDGSFVTLKS 398
Cdd:cd00130   3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLS-GGEPVTLEVRLRRKDGSVIWVLV 81
                        90
                ....*....|....*....
gi 7963664  399 QWFSFTNPWTKELEYIVSV 417
Cdd:cd00130  82 SLTPIRDEGGEVIGLLGVV 100
HLH pfam00010
Helix-loop-helix DNA-binding domain;
58-110 3.00e-15

Helix-loop-helix DNA-binding domain;


Pssm-ID: 333763  Cd Length: 52  Bit Score: 69.87  E-value: 3.00e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 7963664     58 REAHSQTEKRRRDKMNNLIEELSAMIPQCNpmARKLDKLTVLRMAVQHLRSLK 110
Cdd:pfam00010   2 RRAHNERERRRRDRINDAFDELRELLPTPP--SKKLSKAEILRLAIEYIKHLQ 52
HLH cd00083
Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription ...
58-110 7.46e-15

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: 68.78  E-value: 7.46e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 7963664   58 REAHSQTEKRRRDKMNNLIEELSAMIPQcNPMARKLDKLTVLRMAVQHLRSLK 110
Cdd:cd00083   5 REAHNLRERRRRERINDAFDELRSLLPT-LPPSKKLSKAEILRKAVDYIKSLQ 56
HLH smart00353
helix loop helix domain;
65-110 1.30e-13

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 65.32  E-value: 1.30e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 7963664      65 EKRRRDKMNNLIEELSAMIPQCnPMARKLDKLTVLRMAVQHLRSLK 110
Cdd:smart00353   4 ERRRRRKINEAFDELRSLLPTL-PKNKKLSKAEILRLAIEYIKSLQ 48
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
330-414 1.38e-10

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: 337058 [Multi-domain]  Cd Length: 89  Bit Score: 57.73  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7963664    330 FVYVDQRATAILGYLPQELLGT--SCYEYFHQDDHNNLTDKHKAVLQSKEKILTDsYKFRAKDGSFVTLKSQWFSFTNPW 407
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEPYSGE-YRIRRKDGEYRWVEARARPIRDEN 79

                  ....*..
gi 7963664    408 TKELEYI 414
Cdd:pfam08447  80 GKPVRVI 86
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
319-374 7.82e-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: 54.71  E-value: 7.82e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 7963664     319 EFITRFAVNGKFVYVDQRATAILGYLPQELLGTSCYEYFHQDDHNNLTDKHKAVLQ 374
Cdd:smart00091  12 DGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
141-236 2.09e-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 [Multi-domain]  Cd Length: 103  Bit Score: 54.95  E-value: 2.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7963664  141 GFLFVVgCERGKILFVSKSVSKILNYDQASLTGQSLFDFLHPKDVAKVKEQL----SSFDISPREKLIDTKTGLQVHSNL 216
Cdd:cd00130   3 DGVIVL-DLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLenllSGGEPVTLEVRLRRKDGSVIWVLV 81
                        90       100
                ....*....|....*....|
gi 7963664  217 HAGRTRVYFGSRRSFFCRIK 236
Cdd:cd00130  82 SLTPIRDEGGEVIGLLGVVR 101
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
130-192 8.35e-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.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 52.02  E-value: 8.35e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7963664     130 ELRHLILKTAEGFLFVVGcERGKILFVSKSVSKILNYDQASLTGQSLFDFLHPKDVAKVKEQL 192
Cdd:smart00091   1 ERLRAILESLPDGIFVLD-LDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEAL 62
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
327-415 1.30e-08

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: 334337 [Multi-domain]  Cd Length: 112  Bit Score: 52.79  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7963664    327 NGKFVYVDQRATAILGYLPQELLGTSCYEYFHQDDHNNLTDKHKAVLQSKEKILTDSYKFRAKDGSFVTLKSQWFSFTNP 406
Cdd:pfam00989  20 DGRILYVNAAAEELLGLSREEVIGKSLLDLIPEDDDAEVVELLRQALRQGEESRGFEVTFKLPDGRPRHVEVRASPVRDA 99

                  ....*....
gi 7963664    407 WTKELEYIV 415
Cdd:pfam00989 100 GGEILGFLG 108
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
130-236 2.17e-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.


Pssm-ID: 334337 [Multi-domain]  Cd Length: 112  Bit Score: 49.33  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7963664    130 ELRHLILKTAEGFLFVVGcERGKILFVSKSVSKILNYDQASLTGQSLFDFLHPKDVAKVKEQLSSF-----DISPREKLI 204
Cdd:pfam00989   1 EDLRAILESLPDGIFVVD-EDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEDDDAEVVELLRQAlrqgeESRGFEVTF 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 7963664    205 DTKTGLQVHSNLHAGRTRVYFGSRRSFFCRIK 236
Cdd:pfam00989  80 KLPDGRPRHVEVRASPVRDAGGEILGFLGFLR 111
PAS COG2202
PAS domain [Signal transduction mechanisms];
318-394 3.04e-05

PAS domain [Signal transduction mechanisms];


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 45.61  E-value: 3.04e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7963664  318 TEFITRFAVNGKFVYVDQRATAILGYLPQELLGTSCYEYFHQDDHNNLTDKHKAVLQSKE-KILTDSYKFRAKDGSFV 394
Cdd:COG2202 122 PDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSDLIHPEDEERRELELARALAEGRgGPLEIEYRVRRKDGERV 199
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
327-392 9.12e-05

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: 42.28  E-value: 9.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7963664    327 NGKFVYVDQRATAILGYLPQELLGTSCYEYFHQDDHNNLTDKHKAVLQSKEKILTDSYKFRAKDGS 392
Cdd:TIGR00229  22 EGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRRKDGS 87
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
130-233 5.80e-04

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: 39.97  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7963664    130 ELRHLILKTAEGFLFVVGcERGKILFVSKSVSKILNYDQASLTGQSLFDFLHPKDVAKVKEQLSSfDISPR------EKL 203
Cdd:TIGR00229   3 ERYRAIFESSPDAIIVID-LEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIER-RLEGEpepvseERR 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 7963664    204 IDTKTGLQVHSNLHAGRTRVYfGSRRSFFC 233
Cdd:TIGR00229  81 VRRKDGSEIWVEVSVSPIRTN-GGELGVVG 109
PAS_9 pfam13426
PAS domain;
144-233 1.55e-03

PAS domain;


Pssm-ID: 338733 [Multi-domain]  Cd Length: 102  Bit Score: 38.21  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7963664    144 FVVGCERGKILFVSKSVSKILNYDQASLTGQSLFDFL-HPKDVAKVKEQLSSFDIS-PREKLIDTKTGLQVHSNLHAGRT 221
Cdd:pfam13426   4 ILITDEDGRIIYVNPAALRLLGYTREELLGKSLTDLFgEPEASEALEEALREGREVrEVEVVLYRKDGEPFWVLVSASPI 83
                          90
                  ....*....|..
gi 7963664    222 RVYFGSRRSFFC 233
Cdd:pfam13426  84 RDDGGELVGIIA 95
PAS_9 pfam13426
PAS domain;
327-392 3.19e-03

PAS domain;


Pssm-ID: 338733 [Multi-domain]  Cd Length: 102  Bit Score: 37.06  E-value: 3.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7963664    327 NGKFVYVDQRATAILGYLPQELLGTSCYEYFHQDDHNNLTdkhKAVLQSKEKILTDSYKFRAKDGS 392
Cdd:pfam13426  10 DGRIIYVNPAALRLLGYTREELLGKSLTDLFGEPEASEAL---EEALREGREVREVEVVLYRKDGE 72
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
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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