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Conserved domains on  [gi|2538654094|ref|WP_294955501|]
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PAS domain-containing protein [Sulfurovum sp.]

Protein Classification

PAS domain-containing protein( domain architecture ID 11451328)

PAS domain-containing protein binds ligand(s) and may act as sensors for light and oxygen in signal transduction; similar to Homo sapiens potassium voltage-gated channel subfamily H member 1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PAS COG2202
PAS domain [Signal transduction mechanisms];
18-115 2.19e-27

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 102.03  E-value: 2.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  18 IVSSTDLKGIITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKAAFKELWETIRSGKEWTGIVKNLRKDGLYYWVYSHI 97
Cdd:COG2202    23 AIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSI 102
                          90
                  ....*....|....*...
gi 2538654094  98 TPVMNEEGEITGYTAARR 115
Cdd:COG2202   103 SPVRDEDGEITGFVGIAR 120
 
Name Accession Description Interval E-value
PAS COG2202
PAS domain [Signal transduction mechanisms];
18-115 2.19e-27

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 102.03  E-value: 2.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  18 IVSSTDLKGIITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKAAFKELWETIRSGKEWTGIVKNLRKDGLYYWVYSHI 97
Cdd:COG2202    23 AIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSI 102
                          90
                  ....*....|....*...
gi 2538654094  98 TPVMNEEGEITGYTAARR 115
Cdd:COG2202   103 SPVRDEDGEITGFVGIAR 120
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
17-134 2.44e-22

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 91.12  E-value: 2.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  17 LIVSSTDLKGIITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKAAFKELWETIRSGKEWTGIVKNLRKDGLYYWVYSH 96
Cdd:TIGR02938  15 LAISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELT 94
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2538654094  97 ITPVMNEEGEITGYTAARRPATTA-EIEEVVPVYKALVE 134
Cdd:TIGR02938  95 VAPVLNEAGETTHFLGMHRDITELhRLEQVVANQKLLIE 133
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
28-110 9.84e-19

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: 75.07  E-value: 9.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  28 ITYANRTFCNIAGYTKQELTGK--NHNIVRHPDMPKAAFKELWETIRSGKEWTGIVKNLRKDGLYYWVYSHITPVMNEEG 105
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80

                  ....*
gi 2538654094 106 EITGY 110
Cdd:pfam08447  81 KPVRV 85
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
15-110 1.43e-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: 67.27  E-value: 1.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  15 DGLIVssTDLKGIITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKAAFKELWETIRSGKEWTGIVKNLRKDGLYYWVY 94
Cdd:cd00130     3 DGVIV--LDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                          90
                  ....*....|....*.
gi 2538654094  95 SHITPVMNEEGEITGY 110
Cdd:cd00130    81 VSLTPIRDEGGEVIGL 96
PRK13557 PRK13557
histidine kinase; Provisional
28-107 8.46e-11

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 58.14  E-value: 8.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  28 ITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKAAFKELWETIRSGKEWTGIVKNLRKDGLYYWVYSHITPVMNEEGEI 107
Cdd:PRK13557   55 IVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAGDL 134
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
15-61 4.67e-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: 44.31  E-value: 4.67e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2538654094   15 DGLIVssTDLKGIITYANRTFCNIAGYTKQELTGKN-HNIVRHPDMPK 61
Cdd:smart00091  12 DGIFV--LDLDGRILYANPAAEELLGYSPEELIGKSlLELIHPEDRER 57
 
Name Accession Description Interval E-value
PAS COG2202
PAS domain [Signal transduction mechanisms];
18-115 2.19e-27

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 102.03  E-value: 2.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  18 IVSSTDLKGIITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKAAFKELWETIRSGKEWTGIVKNLRKDGLYYWVYSHI 97
Cdd:COG2202    23 AIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSI 102
                          90
                  ....*....|....*...
gi 2538654094  98 TPVMNEEGEITGYTAARR 115
Cdd:COG2202   103 SPVRDEDGEITGFVGIAR 120
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
17-134 2.44e-22

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 91.12  E-value: 2.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  17 LIVSSTDLKGIITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKAAFKELWETIRSGKEWTGIVKNLRKDGLYYWVYSH 96
Cdd:TIGR02938  15 LAISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELT 94
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2538654094  97 ITPVMNEEGEITGYTAARRPATTA-EIEEVVPVYKALVE 134
Cdd:TIGR02938  95 VAPVLNEAGETTHFLGMHRDITELhRLEQVVANQKLLIE 133
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
28-110 9.84e-19

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: 75.07  E-value: 9.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  28 ITYANRTFCNIAGYTKQELTGK--NHNIVRHPDMPKAAFKELWETIRSGKEWTGIVKNLRKDGLYYWVYSHITPVMNEEG 105
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80

                  ....*
gi 2538654094 106 EITGY 110
Cdd:pfam08447  81 KPVRV 85
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
15-110 7.32e-16

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: 68.21  E-value: 7.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  15 DGLIVssTDLKGIITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKAAFKELWETIRSGKEWTGI-VKNLRKDGLYYWV 93
Cdd:pfam00989  12 DGIFV--VDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFeVSFRVPDGRPRHV 89
                          90
                  ....*....|....*..
gi 2538654094  94 YSHITPVMNEEGEITGY 110
Cdd:pfam00989  90 EVRASPVRDAGGEILGF 106
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
15-110 1.43e-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: 67.27  E-value: 1.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  15 DGLIVssTDLKGIITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKAAFKELWETIRSGKEWTGIVKNLRKDGLYYWVY 94
Cdd:cd00130     3 DGVIV--LDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                          90
                  ....*....|....*.
gi 2538654094  95 SHITPVMNEEGEITGY 110
Cdd:cd00130    81 VSLTPIRDEGGEVIGL 96
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
15-118 5.68e-15

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: 66.16  E-value: 5.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  15 DGLIVssTDLKGIITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKAAFKELWETIRSGKEWTGIVKNL-RKDGLYYWV 93
Cdd:TIGR00229  14 DAIIV--IDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVrRKDGSEIWV 91
                          90       100
                  ....*....|....*....|....*
gi 2538654094  94 YSHITPvMNEEGEITGYTAARRPAT 118
Cdd:TIGR00229  92 EVSVSP-IRTNGGELGVVGIVRDIT 115
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
25-112 1.51e-13

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 61.71  E-value: 1.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  25 KGIITYANRTFCNIAGYTKQELTGKN-HNIVRHPDmPKAAFKELWETIRSgkEWTGIVKNLRKDGLYYWVYSHITPVMNE 103
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSiTDLFAEPE-DSERLREALREGKA--VREFEVVLYRKDGEPFPVLVSLAPIRDD 77

                  ....*....
gi 2538654094 104 EGEITGYTA 112
Cdd:pfam13426  78 GGELVGIIA 86
PRK13557 PRK13557
histidine kinase; Provisional
28-107 8.46e-11

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 58.14  E-value: 8.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  28 ITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKAAFKELWETIRSGKEWTGIVKNLRKDGLYYWVYSHITPVMNEEGEI 107
Cdd:PRK13557   55 IVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAGDL 134
PRK13558 PRK13558
bacterio-opsin activator; Provisional
1-110 2.78e-10

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 56.77  E-value: 2.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094   1 MTRPDPIDQEYRFKD--------GLIVSSTDL--KGIItYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKAAFKELWET 70
Cdd:PRK13558  137 PISDLTVESDRRLKEraldeapvGITIADATLpdEPLI-YINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREA 215
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2538654094  71 IRSGKEWTGIVKNLRKDGLYYWVYSHITPVMNEEGEITGY 110
Cdd:PRK13558  216 IDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHY 255
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
15-114 1.89e-09

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 54.21  E-value: 1.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  15 DGLIVssTDLKGIITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKAAFKELWETIRSGKEWTGIVKNLRKDGLYYWVY 94
Cdd:COG5809   152 DGIIV--TDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLE 229
                          90       100
                  ....*....|....*....|
gi 2538654094  95 SHITPVMNEEGEITGYTAAR 114
Cdd:COG5809   230 ASGAPIKKNGEVDGIVIIFR 249
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
15-107 2.05e-09

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 54.08  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  15 DGLIVssTDLKGIITYANRTFCNIAGYTKQELTGKN-HNIVRHPDmpkAAFKELWETIRSGKE-WTGIVKNLRKDGLYYW 92
Cdd:COG3852    18 DAVIV--LDADGRITYVNPAAERLLGLSAEELLGRPlAELFPEDS---PLRELLERALAEGQPvTEREVTLRRKDGEERP 92
                          90
                  ....*....|....*
gi 2538654094  93 VYSHITPVMNEEGEI 107
Cdd:COG3852    93 VDVSVSPLRDAEGEG 107
PRK13559 PRK13559
hypothetical protein; Provisional
28-120 2.77e-09

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 53.67  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  28 ITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKAAFKELWETIRSGKEWTGIVKNLRKDGLYYWVYSHITPVMNEEG-- 105
Cdd:PRK13559   68 IVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPVYGEDGrl 147
                          90       100
                  ....*....|....*....|...
gi 2538654094 106 --------EITGYTAARRPATTA 120
Cdd:PRK13559  148 lyffgsqwDVTDIRAVRALEAHE 170
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
15-138 3.09e-09

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 53.62  E-value: 3.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  15 DGLIVssTDLKGIITYANRTFCNIAGYTKQELTGKN-HNIVRHPDMPKAafkelwetIRSGKEWTGIVKNLRKDGLYywV 93
Cdd:COG3829    22 DGIIV--VDADGRITYVNRAAERILGLPREEVIGKNvTELIPNSPLLEV--------LKTGKPVTGVIQKTGGKGKT--V 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2538654094  94 YSHITPVMnEEGEITGYTaarrpATTAEIEEVVPVYKALVEEENK 138
Cdd:COG3829    90 IVTAIPIF-EDGEVIGAV-----ETFRDITELKRLERKLREEELE 128
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
18-107 4.56e-09

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 53.20  E-value: 4.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  18 IVSSTDLKGIITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKaAFKELWETIRSGKEWTGIVKNLRKDGLYYWVYSHI 97
Cdd:COG5805    46 AIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLEKEYHY-RVKTRIERLQKGYDVVMIEQIYCKDGELIYVEVKL 124
                          90
                  ....*....|
gi 2538654094  98 TPVMNEEGEI 107
Cdd:COG5805   125 FPIYNQNGQA 134
PAS COG2202
PAS domain [Signal transduction mechanisms];
18-107 9.92e-09

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 51.95  E-value: 9.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  18 IVSSTDLKGIITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKAAFKELWETIRSGKEWTGIVKNLR-KDGLYYWVYSH 96
Cdd:COG2202   149 GIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKdGDGRWVWVEAS 228
                          90
                  ....*....|.
gi 2538654094  97 ITPVMNEEGEI 107
Cdd:COG2202   229 AVPLRDGGEVI 239
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
15-61 4.67e-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: 44.31  E-value: 4.67e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2538654094   15 DGLIVssTDLKGIITYANRTFCNIAGYTKQELTGKN-HNIVRHPDMPK 61
Cdd:smart00091  12 DGIFV--LDLDGRILYANPAAEELLGYSPEELIGKSlLELIHPEDRER 57
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
23-138 7.86e-07

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 46.89  E-value: 7.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  23 DLKGIITYANRTFCNIAGYTKQELTGKNHNIVRHPDMPKaAFKELWETIRSGKEWTGIVKNLR-KDGLYYWVYSHITPVM 101
Cdd:COG5809    32 DLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEK-ELREILKLLKEGESRDELEFELRhKNGKRLEFSSKLSPIF 110
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2538654094 102 NEEGEITGYTAARRPATTAEIEEvvpvyKALVEEENK 138
Cdd:COG5809   111 DQNGDIEGMLAISRDITERKRME-----EALRESEEK 142
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
18-110 2.26e-06

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 45.49  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  18 IVSSTDLKGIITYANRTFCNIAGYTKQELTGKN-HNIVRHPDmpKAAFKELWETIRSGKEWTGIVKNLR-KDGLYYWVYS 95
Cdd:COG5805   169 LICVIDTDGRILFINESIERLFGAPREELIGKNlLELLHPCD--KEEFKERIESITEVWQEFIIEREIItKDGRIRYFEA 246
                          90
                  ....*....|....*
gi 2538654094  96 HITPVMNEEGEITGY 110
Cdd:COG5805   247 VIVPLIDTDGSVKGI 261
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
78-110 2.54e-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: 36.39  E-value: 2.54e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2538654094   78 TGIVKNLRKDGLYYWVYSHITPVMNEEGEITGY 110
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGI 33
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
15-118 8.05e-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. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 36.62  E-value: 8.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538654094  15 DGLIVSSTDlkGIITYANRTFCNIAGYTKQELTGKnhnivRHPDMP----KAAFKELWETIRSGKEWTGIVKNLRKDGLY 90
Cdd:pfam08448   6 DALAVLDPD--GRVRYANAAAAELFGLPPEELLGK-----TLAELLppedAARLERALRRALEGEEPIDFLEELLLNGEE 78
                          90       100
                  ....*....|....*....|....*...
gi 2538654094  91 YWVYSHITPVMNEEGEITGYTAARRPAT 118
Cdd:pfam08448  79 RHYELRLTPLRDPDGEVIGVLVISRDIT 106
 
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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