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Conserved domains on  [gi|446410274|ref|WP_000488129|]
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MULTISPECIES: GAF domain-containing sensor histidine kinase [Bacillus]

Protein Classification

GAF domain-containing sensor histidine kinase( domain architecture ID 11453261)

two-component sensor histidine kinase with GAF sensor domain(s), functions as a protein kinase that phosphorylates a target protein in response to external signals

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
317-523 4.99e-57

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


:

Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 190.60  E-value: 4.99e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 317 ENLRLNEQRRELVRMEERNRLARDLHDSVSQKLFSLTFMTKGAEAVLKGKNEKVDQSLHEMRELAQGALKEMRTLIWQLR 396
Cdd:COG4585   37 ELERELAARAEEAREEERRRIARELHDGVGQSLSAIKLQLEAARRLLDADPEAAREELEEIRELAREALAELRRLVRGLR 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 397 PAGLEK-GLLPALKQYGENL----GLKIREQVTG-VRDLPRVVEEALWRIGQEALNNVSKHAGIKEATIYFTVNEKNVSL 470
Cdd:COG4585  117 PPALDDlGLAAALEELAERLlraaGIRVELDVDGdPDRLPPEVELALYRIVQEALTNALKHAGATRVTVTLEVDDGELTL 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446410274 471 EIVDQGKGFVEKNIKeKKSLGMITMRERVELVGGTIKIVSS-NKRTSVKVNVPL 523
Cdd:COG4585  197 TVRDDGVGFDPEAAP-GGGLGLRGMRERAEALGGTLTIGSApGGGTRVRATLPL 249
GAF COG2203
GAF domain [Signal transduction mechanisms];
6-448 1.27e-14

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 76.77  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274   6 RTNELVILKEIAETLNTSNDTYHVLQAVLEKLLSVTGLTTGWIFLADENGKYtklIDYQLPEALTYENKRPMCEGECWCL 85
Cdd:COG2203  188 ELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGE---LELVAAPGLPEEELGRLPLGEGLAG 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274  86 RGFVDGKLERAVNIIECKRINNAiEYNWGDTEGILHHATVPLKAGGEKFGLLNVASPGKTHFSEEELVLLQSVAFQIGTA 165
Cdd:COG2203  265 RALRTGEPVVVNDASTDPRFAPS-LRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIA 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 166 LKRTKLYENEKRRAHyyvKLERFIQDLKTIHKFNVLPEKVVNHVGEVFQWNQVALFIREEKELSLRASYVQEELKEDIKE 245
Cdd:COG2203  344 IERARLYEALEAALA---ALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEG 420
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 246 AAKRALEQDEPVLIKHQIGHNVHLNRAVIATPIHIQNHIFGVLCVSLNNGEFDANTIDVIQALSNHVSLIIENLRLNEQR 325
Cdd:COG2203  421 LLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLAL 500
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 326 RELVRMEERNRLARDLHDSVSQKLFSLTFMTKGAEAVLKGKNEKVDQSLHEMRELAQGALKEMRTLIWQLRPAGLEKGLL 405
Cdd:COG2203  501 SALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELA 580
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 446410274 406 PALKQYGENLGLKIREQVTGVRDLPRVVEEALWRIGQEALNNV 448
Cdd:COG2203  581 LALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLV 623
 
Name Accession Description Interval E-value
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
317-523 4.99e-57

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 190.60  E-value: 4.99e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 317 ENLRLNEQRRELVRMEERNRLARDLHDSVSQKLFSLTFMTKGAEAVLKGKNEKVDQSLHEMRELAQGALKEMRTLIWQLR 396
Cdd:COG4585   37 ELERELAARAEEAREEERRRIARELHDGVGQSLSAIKLQLEAARRLLDADPEAAREELEEIRELAREALAELRRLVRGLR 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 397 PAGLEK-GLLPALKQYGENL----GLKIREQVTG-VRDLPRVVEEALWRIGQEALNNVSKHAGIKEATIYFTVNEKNVSL 470
Cdd:COG4585  117 PPALDDlGLAAALEELAERLlraaGIRVELDVDGdPDRLPPEVELALYRIVQEALTNALKHAGATRVTVTLEVDDGELTL 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446410274 471 EIVDQGKGFVEKNIKeKKSLGMITMRERVELVGGTIKIVSS-NKRTSVKVNVPL 523
Cdd:COG4585  197 TVRDDGVGFDPEAAP-GGGLGLRGMRERAEALGGTLTIGSApGGGTRVRATLPL 249
HisKA_3 pfam07730
Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of ...
333-400 3.16e-20

Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of histidine kinases. It shares sequence similarity with pfam00512 and pfam07536.


Pssm-ID: 429624 [Multi-domain]  Cd Length: 68  Bit Score: 84.60  E-value: 3.16e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410274  333 ERNRLARDLHDSVSQKLFSLTFMTKGAEAVLKGKNEKVDQSLHEMRELAQGALKEMRTLIWQLRPAGL 400
Cdd:pfam07730   1 ERNRIARELHDSVGQSLTAIKLQLELARRLLDRDPEEAREQLDAIRELAREALQELRRLLGDLRPPAL 68
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
437-522 4.22e-19

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 81.83  E-value: 4.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 437 LWRIGQEALNNVSKHAGIKEATIYFTVNEKNVSLEIVDQGKGFVEKNIKEKKSLGMITMRERVELVGGTIKIVSSNKR-T 515
Cdd:cd16917    1 LYRIVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPAPPGGGGFGLLGMRERAELLGGTLTIGSRPGGgT 80

                 ....*..
gi 446410274 516 SVKVNVP 522
Cdd:cd16917   81 RVTARLP 87
PRK11644 PRK11644
signal transduction histidine-protein kinase/phosphatase UhpB;
320-523 2.69e-16

signal transduction histidine-protein kinase/phosphatase UhpB;


Pssm-ID: 236945 [Multi-domain]  Cd Length: 495  Bit Score: 81.56  E-value: 2.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 320 RLNEQR---RELVRMEE--RNRLARDLHDSVSQklfSLTFMTKGAEAV--LKGKNEKVDQSLHEMRELAQGALKEMRTLI 392
Cdd:PRK11644 283 ELARNRhlaERLLETEEsvRRDVARELHDEIGQ---TITAIRTQAGIIkrLAADNASVKQSAQLIEQLSLGVYDTVRRLL 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 393 WQLRPAGLEKglLPaLKQYGENLglkIRE------QVTGVRD-------LPRVVEEALWRIGQEALNNVSKHAGIKEATI 459
Cdd:PRK11644 360 GRLRPRQLDD--LT-LEQAIRSL---MREmeledrGIVSHLDwridesaLSETQRVTLFRVCQEGLNNIVKHADASAVTL 433
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446410274 460 YFTVNEKNVSLEIVDQGKGFVEKNIkeKKSLGMITMRERVELVGGTIKIvSSNKRTSVKVNVPL 523
Cdd:PRK11644 434 QGWQQDERLMLVIEDDGSGLPPGSG--QQGFGLRGMRERVTALGGTLTI-SCTHGTRLSVSLPQ 494
GAF COG2203
GAF domain [Signal transduction mechanisms];
6-448 1.27e-14

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 76.77  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274   6 RTNELVILKEIAETLNTSNDTYHVLQAVLEKLLSVTGLTTGWIFLADENGKYtklIDYQLPEALTYENKRPMCEGECWCL 85
Cdd:COG2203  188 ELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGE---LELVAAPGLPEEELGRLPLGEGLAG 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274  86 RGFVDGKLERAVNIIECKRINNAiEYNWGDTEGILHHATVPLKAGGEKFGLLNVASPGKTHFSEEELVLLQSVAFQIGTA 165
Cdd:COG2203  265 RALRTGEPVVVNDASTDPRFAPS-LRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIA 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 166 LKRTKLYENEKRRAHyyvKLERFIQDLKTIHKFNVLPEKVVNHVGEVFQWNQVALFIREEKELSLRASYVQEELKEDIKE 245
Cdd:COG2203  344 IERARLYEALEAALA---ALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEG 420
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 246 AAKRALEQDEPVLIKHQIGHNVHLNRAVIATPIHIQNHIFGVLCVSLNNGEFDANTIDVIQALSNHVSLIIENLRLNEQR 325
Cdd:COG2203  421 LLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLAL 500
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 326 RELVRMEERNRLARDLHDSVSQKLFSLTFMTKGAEAVLKGKNEKVDQSLHEMRELAQGALKEMRTLIWQLRPAGLEKGLL 405
Cdd:COG2203  501 SALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELA 580
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 446410274 406 PALKQYGENLGLKIREQVTGVRDLPRVVEEALWRIGQEALNNV 448
Cdd:COG2203  581 LALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLV 623
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
29-166 1.91e-13

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 67.49  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274   29 VLQAVLEKLLSVTGLTTGWIFLADENGKYtkLIDYQLPEALTYENKRPMCEGECW-CLRgfvDGKLERAVNIIECKRINN 107
Cdd:pfam13185   7 LLDAVLEAAVELGASAVGFILLVDDDGRL--AAWGGAADELSAALDDPPGEGLVGeALR---TGRPVIVNDLAADPAKKG 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446410274  108 AIEynwgDTEGILHHATVPLKAGGEKFGLLNVASPGKTHFSEEELVLLQSVAFQIGTAL 166
Cdd:pfam13185  82 LPA----GHAGLRSFLSVPLVSGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAI 136
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
201-326 6.73e-10

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 57.78  E-value: 6.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274   201 LPEKVVNHVGEVFQWNQVALFIREEKELSLRASYVQEELKEDIKE--------AAKRALEQDEPVLIKHQIGHNVHLN-- 270
Cdd:smart00065   5 LLQTILEELRQLLGADRVLIYLVDENDRGELVLVAADGLTLPTLGirfpldegLAGRVAETGRPLNIPDVEADPLFAEdl 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410274   271 -------RAVIATPIHIQNHIFGVLCV--SLNNGEFDANTIDVIQALSNHVSLIIENLRLNEQRR 326
Cdd:smart00065  85 lgryqgvRSFLAVPLVADGELVGVLALhnKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
434-523 2.98e-04

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 40.32  E-value: 2.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274   434 EEALWRIGQEALNNVSKHAGiKEATIYFTVN--EKNVSLEIVDQGKGFVEKNI----------KEKKS------LGMITM 495
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTP-EGGRITVTLErdGDHVEITVEDNGPGIPPEDLekifepffrtDKRSRkiggtgLGLSIV 81
                           90       100
                   ....*....|....*....|....*....
gi 446410274   496 RERVELVGGTIKIVSSNKR-TSVKVNVPL 523
Cdd:smart00387  82 KKLVELHGGEISVESEPGGgTTFTITLPL 110
 
Name Accession Description Interval E-value
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
317-523 4.99e-57

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 190.60  E-value: 4.99e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 317 ENLRLNEQRRELVRMEERNRLARDLHDSVSQKLFSLTFMTKGAEAVLKGKNEKVDQSLHEMRELAQGALKEMRTLIWQLR 396
Cdd:COG4585   37 ELERELAARAEEAREEERRRIARELHDGVGQSLSAIKLQLEAARRLLDADPEAAREELEEIRELAREALAELRRLVRGLR 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 397 PAGLEK-GLLPALKQYGENL----GLKIREQVTG-VRDLPRVVEEALWRIGQEALNNVSKHAGIKEATIYFTVNEKNVSL 470
Cdd:COG4585  117 PPALDDlGLAAALEELAERLlraaGIRVELDVDGdPDRLPPEVELALYRIVQEALTNALKHAGATRVTVTLEVDDGELTL 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446410274 471 EIVDQGKGFVEKNIKeKKSLGMITMRERVELVGGTIKIVSS-NKRTSVKVNVPL 523
Cdd:COG4585  197 TVRDDGVGFDPEAAP-GGGLGLRGMRERAEALGGTLTIGSApGGGTRVRATLPL 249
UhpB COG3851
Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction ...
317-523 6.32e-26

Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction mechanisms];


Pssm-ID: 443060 [Multi-domain]  Cd Length: 493  Bit Score: 110.87  E-value: 6.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 317 ENLRLNEQrreLVRMEERNR--LARDLHDSVSQKLFSLTFMTKGAEAVlkGKNEKVDQSLHEMRELAQGALKEMRTLIWQ 394
Cdd:COG3851  277 ENRALARQ---LVSAEESERreIARELHDEIGQNITAIRTQASILKRL--APQPEIEQSAQSIESLALRIYDTTRRLLDR 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 395 LRPAGLEK-GLLPALKQYGENLGLkireQVTGV----------RDLPRVVEEALWRIGQEALNNVSKHAGIKEATIYFTV 463
Cdd:COG3851  352 LRPAVLDElGLEEALRELPRELAF----EEPGIscqldlrgdpSLLDDTLQLTLYRLVQEALTNILKHAEASQIRISLSQ 427
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 464 NEKNVSLEIVDQGKGFVEKNIkeKKSLGMITMRERVELVGGTIKIVSSNKRTSVKVNVPL 523
Cdd:COG3851  428 DKRLLSLEIRDDGIGLPPELR--AKGFGLRGMRERVRALGGDFRLSSAPKGTRLSVLLPT 485
HisKA_3 pfam07730
Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of ...
333-400 3.16e-20

Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of histidine kinases. It shares sequence similarity with pfam00512 and pfam07536.


Pssm-ID: 429624 [Multi-domain]  Cd Length: 68  Bit Score: 84.60  E-value: 3.16e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410274  333 ERNRLARDLHDSVSQKLFSLTFMTKGAEAVLKGKNEKVDQSLHEMRELAQGALKEMRTLIWQLRPAGL 400
Cdd:pfam07730   1 ERNRIARELHDSVGQSLTAIKLQLELARRLLDRDPEEAREQLDAIRELAREALQELRRLLGDLRPPAL 68
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
437-522 4.22e-19

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 81.83  E-value: 4.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 437 LWRIGQEALNNVSKHAGIKEATIYFTVNEKNVSLEIVDQGKGFVEKNIKEKKSLGMITMRERVELVGGTIKIVSSNKR-T 515
Cdd:cd16917    1 LYRIVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPAPPGGGGFGLLGMRERAELLGGTLTIGSRPGGgT 80

                 ....*..
gi 446410274 516 SVKVNVP 522
Cdd:cd16917   81 RVTARLP 87
PRK11644 PRK11644
signal transduction histidine-protein kinase/phosphatase UhpB;
320-523 2.69e-16

signal transduction histidine-protein kinase/phosphatase UhpB;


Pssm-ID: 236945 [Multi-domain]  Cd Length: 495  Bit Score: 81.56  E-value: 2.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 320 RLNEQR---RELVRMEE--RNRLARDLHDSVSQklfSLTFMTKGAEAV--LKGKNEKVDQSLHEMRELAQGALKEMRTLI 392
Cdd:PRK11644 283 ELARNRhlaERLLETEEsvRRDVARELHDEIGQ---TITAIRTQAGIIkrLAADNASVKQSAQLIEQLSLGVYDTVRRLL 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 393 WQLRPAGLEKglLPaLKQYGENLglkIRE------QVTGVRD-------LPRVVEEALWRIGQEALNNVSKHAGIKEATI 459
Cdd:PRK11644 360 GRLRPRQLDD--LT-LEQAIRSL---MREmeledrGIVSHLDwridesaLSETQRVTLFRVCQEGLNNIVKHADASAVTL 433
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446410274 460 YFTVNEKNVSLEIVDQGKGFVEKNIkeKKSLGMITMRERVELVGGTIKIvSSNKRTSVKVNVPL 523
Cdd:PRK11644 434 QGWQQDERLMLVIEDDGSGLPPGSG--QQGFGLRGMRERVTALGGTLTI-SCTHGTRLSVSLPQ 494
PRK10600 PRK10600
nitrate/nitrite two-component system sensor histidine kinase NarX;
320-498 1.02e-15

nitrate/nitrite two-component system sensor histidine kinase NarX;


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 79.71  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 320 RLNEQRRELVRMEERNRLARDLHDSVSQKLFSLTFMTKGAEAVLKGKNEKVDQSLHEMRELAQGALKEMRTLIWQLRPAG 399
Cdd:PRK10600 348 RQQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESSRELLSQIRNELNASWRQLRELLTTFRLQL 427
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 400 LEKGLLPALK----QYGENLGLKIR--EQVTgvrdlPRVV--EEA--LWRIGQEALNNVSKHAGIKEATIYFTVNEKNVS 469
Cdd:PRK10600 428 TEPGLRPALEasceEFSARFGFPVKldYQLP-----PRLVpsHQAihLLQIAREALSNALKHAQASEVVVTVAQNQNQVK 502
                        170       180
                 ....*....|....*....|....*....
gi 446410274 470 LEIVDQGKGfVEKNIKEKKSLGMITMRER 498
Cdd:PRK10600 503 LSVQDNGCG-VPENAERSNHYGLIIMRDR 530
GAF COG2203
GAF domain [Signal transduction mechanisms];
6-448 1.27e-14

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 76.77  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274   6 RTNELVILKEIAETLNTSNDTYHVLQAVLEKLLSVTGLTTGWIFLADENGKYtklIDYQLPEALTYENKRPMCEGECWCL 85
Cdd:COG2203  188 ELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGE---LELVAAPGLPEEELGRLPLGEGLAG 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274  86 RGFVDGKLERAVNIIECKRINNAiEYNWGDTEGILHHATVPLKAGGEKFGLLNVASPGKTHFSEEELVLLQSVAFQIGTA 165
Cdd:COG2203  265 RALRTGEPVVVNDASTDPRFAPS-LRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIA 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 166 LKRTKLYENEKRRAHyyvKLERFIQDLKTIHKFNVLPEKVVNHVGEVFQWNQVALFIREEKELSLRASYVQEELKEDIKE 245
Cdd:COG2203  344 IERARLYEALEAALA---ALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEG 420
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 246 AAKRALEQDEPVLIKHQIGHNVHLNRAVIATPIHIQNHIFGVLCVSLNNGEFDANTIDVIQALSNHVSLIIENLRLNEQR 325
Cdd:COG2203  421 LLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLAL 500
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 326 RELVRMEERNRLARDLHDSVSQKLFSLTFMTKGAEAVLKGKNEKVDQSLHEMRELAQGALKEMRTLIWQLRPAGLEKGLL 405
Cdd:COG2203  501 SALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELA 580
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 446410274 406 PALKQYGENLGLKIREQVTGVRDLPRVVEEALWRIGQEALNNV 448
Cdd:COG2203  581 LALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLV 623
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
29-166 1.91e-13

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 67.49  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274   29 VLQAVLEKLLSVTGLTTGWIFLADENGKYtkLIDYQLPEALTYENKRPMCEGECW-CLRgfvDGKLERAVNIIECKRINN 107
Cdd:pfam13185   7 LLDAVLEAAVELGASAVGFILLVDDDGRL--AAWGGAADELSAALDDPPGEGLVGeALR---TGRPVIVNDLAADPAKKG 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446410274  108 AIEynwgDTEGILHHATVPLKAGGEKFGLLNVASPGKTHFSEEELVLLQSVAFQIGTAL 166
Cdd:pfam13185  82 LPA----GHAGLRSFLSVPLVSGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAI 136
PRK10935 PRK10935
nitrate/nitrite two-component system sensor histidine kinase NarQ;
276-521 6.60e-10

nitrate/nitrite two-component system sensor histidine kinase NarQ;


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 61.41  E-value: 6.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 276 TPIHIQNHIFGVLCVSLNNGEFDANTID-VIQALSNhvSLIIENLRlnEQRRELVRMEERNRLARDLHDSVSQklfSLTF 354
Cdd:PRK10935 309 LPLTMEDTVLGYLHWQASLPCPDEPLMNnVAQMLGR--GLYFNQAQ--KQQQQLLLMEERATIARELHDSLAQ---VLSY 381
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 355 MtKGAEAVLK-GKNEKVDQSLHEMRELAQGaLKEMRTliwQLRpaglekGLLP----ALKQygENLGLKIREQVTGVRD- 428
Cdd:PRK10935 382 L-KIQLTLLKrSLDEDNAKAQSIIAEFDQA-LSDAYR---QLR------ELLTtfrlTIQE--ANLGSALEEMLDQLRNq 448
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274 429 ----------LPRVVEEA-----LWRIGQEALNNVSKHAGIKEATI-YFTVNEKNVSLEIVDQGKGFVEKNIKEKKsLGM 492
Cdd:PRK10935 449 tdakitldcrLPSQALDAqqqvhLLQIIREATLNAIKHANASEIAVsCVTNPDGEHTVSIRDDGIGIGELKEPEGH-YGL 527
                        250       260
                 ....*....|....*....|....*....
gi 446410274 493 ITMRERVELVGGTIKIvSSNKRTSVKVNV 521
Cdd:PRK10935 528 NIMQERAERLGGTLTI-SQPPGGGTTVSL 555
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
201-326 6.73e-10

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 57.78  E-value: 6.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274   201 LPEKVVNHVGEVFQWNQVALFIREEKELSLRASYVQEELKEDIKE--------AAKRALEQDEPVLIKHQIGHNVHLN-- 270
Cdd:smart00065   5 LLQTILEELRQLLGADRVLIYLVDENDRGELVLVAADGLTLPTLGirfpldegLAGRVAETGRPLNIPDVEADPLFAEdl 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410274   271 -------RAVIATPIHIQNHIFGVLCV--SLNNGEFDANTIDVIQALSNHVSLIIENLRLNEQRR 326
Cdd:smart00065  85 lgryqgvRSFLAVPLVADGELVGVLALhnKKSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
29-166 2.43e-09

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 55.56  E-value: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274   29 VLQAVLEKLLSVTGLTTGWIFLADENGKYTklidyqlpealtyenkrpMCEGECWCLRGFVDGKLERAVNIIECKR---I 105
Cdd:pfam01590   5 ILQTILEELRELLGADRCALYLPDADGLEY------------------LPPGARWLKAAGLEIPPGTGVTVLRTGRplvV 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410274  106 NNAIE-------YNWGDTEGILHHATVPLKAGGEKFGLLNVASPGKtHFSEEELVLLQSVAFQIGTAL 166
Cdd:pfam01590  67 PDAAGdprfldpLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHPRP-PFTEEELELLEVLADQVAIAL 133
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
8-178 1.01e-08

Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 54.90  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274   8 NELVILKEIAETLNTSNDtyhvLQAVLEKLLSVTGLTTGW----IFLADENGKYTKLIDYQ-LPEALTYENKRPMCEGec 82
Cdd:COG3605    1 EMLKALRRISEAVASALD----LDEALDRIVRRIAEALGVdvcsIYLLDPDGGRLELRATEgLNPEAVGKVRLPLGEG-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274  83 wcLRGFVdGKLERAVNIIE------CKRINNAIEYNwgdTEGILhhaTVPLKAGGEKFGLLNVASPGKTHFSEEELVLLQ 156
Cdd:COG3605   75 --LVGLV-AERGEPLNLADaashprFKYFPETGEEG---FRSFL---GVPIIRRGRVLGVLVVQSREPREFTEEEVEFLV 145
                        170       180
                 ....*....|....*....|..
gi 446410274 157 SVAFQIGTALKRTKLYENEKRR 178
Cdd:COG3605  146 TLAAQLAEAIANAELLGELRAA 167
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
203-316 2.31e-08

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 52.87  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274  203 EKVVNHVGEVFQWNQVALFIREEKELSLR---ASYVQEELKEDIKEAAKRALEQDEPVLIKHQIGHNVHLN--------- 270
Cdd:pfam01590   7 QTILEELRELLGADRCALYLPDADGLEYLppgARWLKAAGLEIPPGTGVTVLRTGRPLVVPDAAGDPRFLDpllllrnfg 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 446410274  271 -RAVIATPIHIQNHIFGVLCVSLNNGEFDANTIDVIQALSNHVSLII 316
Cdd:pfam01590  87 iRSLLAVPIIDDGELLGVLVLHHPRPPFTEEELELLEVLADQVAIAL 133
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
30-176 1.24e-06

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 48.15  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274    30 LQAVLEKLLSVTGLTTGWIFLADENGKY---TKLIDYQLPEalTYENKRPMCEGECwclrGFVDgKLERAVNIIECkrin 106
Cdd:smart00065   6 LQTILEELRQLLGADRVLIYLVDENDRGelvLVAADGLTLP--TLGIRFPLDEGLA----GRVA-ETGRPLNIPDV---- 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410274   107 NAIEYNWGD----TEGILHHATVPLKAGGEKFGLLNVASPGK-THFSEEELVLLQSVAFQIGTALKRTKLYENEK 176
Cdd:smart00065  75 EADPLFAEDllgrYQGVRSFLAVPLVADGELVGVLALHNKKSpRPFTEEDEELLQALANQLAIALANAQLYEELR 149
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
433-523 5.58e-06

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 45.44  E-value: 5.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274  433 VEEALWRIGQEALNNVSKHAGiKEATIYFTVNEKN-VSLEIVDQGKGFVEKNIK---EKKS-----------LGMITMRE 497
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAA-KAGEITVTLSEGGeLTLTVEDNGIGIPPEDLPrifEPFStadkrggggtgLGLSIVRK 80
                          90       100
                  ....*....|....*....|....*..
gi 446410274  498 RVELVGGTIKIVSS-NKRTSVKVNVPL 523
Cdd:pfam02518  81 LVELLGGTITVESEpGGGTTVTLTLPL 107
GAF_3 pfam13492
GAF domain;
203-318 6.60e-06

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 45.44  E-value: 6.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274  203 EKVVNHVGEVFQWNQVALFIREE--KELSLRASYVQEE-LKEDIKEA---AKRALEQDEPVLIKHQIGHNVHLNRAVIAT 276
Cdd:pfam13492   7 EALLKLLVRLLGAERAAVYLLDEdgNKLQVAAGYDGEPdPSESLDADsplARRALSSGEPISGLGSAGEDGLPDGPALVV 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 446410274  277 PIHIQNHIFGVLCV-SLNNGEFDANTIDVIQALSNHVSLIIEN 318
Cdd:pfam13492  87 PLVAGRRVIGVLALaSSKPRAFDAEDLRLLESLAAQIATAIEN 129
GAF_3 pfam13492
GAF domain;
125-168 1.91e-05

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 44.28  E-value: 1.91e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 446410274  125 VPLKAGGEKFGLLNVASPGKTHFSEEELVLLQSVAFQIGTALKR 168
Cdd:pfam13492  86 VPLVAGRRVIGVLALASSKPRAFDAEDLRLLESLAAQIATAIEN 129
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
271-336 3.92e-05

Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 44.50  E-value: 3.92e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446410274 271 RAVIATPIHIQNHIFGVLCV-SLNNGEFDANTIDVIQALSNHVSLIIENLRLNEQRRELVRMEERNR 336
Cdd:COG3605  109 RSFLGVPIIRRGRVLGVLVVqSREPREFTEEEVEFLVTLAAQLAEAIANAELLGELRAALAELSLAR 175
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
219-317 6.08e-05

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 42.84  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274  219 ALFIREEKELSLRASYVQEELKEDIKEA-----AKRALEQDEPVLIKHQIGHNVHLN--------RAVIATPIHIQNHIF 285
Cdd:pfam13185  25 FILLVDDDGRLAAWGGAADELSAALDDPpgeglVGEALRTGRPVIVNDLAADPAKKGlpaghaglRSFLSVPLVSGGRVV 104
                          90       100       110
                  ....*....|....*....|....*....|...
gi 446410274  286 GVLCV-SLNNGEFDANTIDVIQALSNHVSLIIE 317
Cdd:pfam13185 105 GVLALgSNRPGAFDEEDLELLELLAEQAAIAIE 137
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
434-523 2.98e-04

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 40.32  E-value: 2.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410274   434 EEALWRIGQEALNNVSKHAGiKEATIYFTVN--EKNVSLEIVDQGKGFVEKNI----------KEKKS------LGMITM 495
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTP-EGGRITVTLErdGDHVEITVEDNGPGIPPEDLekifepffrtDKRSRkiggtgLGLSIV 81
                           90       100
                   ....*....|....*....|....*....
gi 446410274   496 RERVELVGGTIKIVSSNKR-TSVKVNVPL 523
Cdd:smart00387  82 KKLVELHGGEISVESEPGGgTTFTITLPL 110
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
125-166 5.11e-04

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


Pssm-ID: 442823 [Multi-domain]  Cd Length: 338  Bit Score: 42.14  E-value: 5.11e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446410274 125 VPLKAGGEKFGLLNVASPGKTHFSEEELVLLQSVAFQIGTAL 166
Cdd:COG3604   79 VPLRVGGEVLGVLTLDSRRPGAFSEEDLRLLETLASLAAVAI 120
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
125-168 5.86e-03

GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, Signal transduction mechanisms];


Pssm-ID: 441559 [Multi-domain]  Cd Length: 156  Bit Score: 37.50  E-value: 5.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446410274 125 VPLKAGGEKFGLLNVASPGKTHFSEEELVLLQSVAFQIGTALKR 168
Cdd:COG1956  113 VPIFKDGEVIGVLDIDSPTPGRFDEEDQAGLEALAALLAEALDA 156
 
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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