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Conserved domains on  [gi|446360107|ref|WP_000437962|]
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MULTISPECIES: GAF domain-containing sensor histidine kinase [Staphylococcus]

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];
171-369 8.99e-53

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


:

Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 175.19  E-value: 8.99e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 171 REKEAAKINERNRLARDLHDSVNQMLFSVKLTAHAAYGVSNESI--AKQAFKTIEETSQNAVNEMRALIWQLKPVGLEQ- 247
Cdd:COG4585   44 ARAEEAREEERRRIARELHDGVGQSLSAIKLQLEAARRLLDADPeaAREELEEIRELAREALAELRRLVRGLRPPALDDl 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 248 GLIHALTAY----SKLMHIQLNVNVEG-LIDLSNEIEENIYRALQECINNVKKHADTNKMDLTLKQMNDILYIDVIDYGQ 322
Cdd:COG4585  124 GLAAALEELaerlLRAAGIRVELDVDGdPDRLPPEVELALYRIVQEALTNALKHAGATRVTVTLEVDDGELTLTVRDDGV 203

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446360107 323 GFEIDNVqIASSHGINNIKQRVKLLRGKVTFHSQPTKGTQIQFTIPI 369
Cdd:COG4585  204 GFDPEAA-PGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPL 249
GAF COG2203
GAF domain [Signal transduction mechanisms];
2-288 1.07e-16

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 81.78  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107   2 EQRTRLALLKEIAEFLNEETEMYSMTQGALKYLIEGSNFTTGWIFFINsvGEHELVSHVALPqSLTADHCHYIKDGSCWC 81
Cdd:COG2203  187 LELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVD--EDGGELELVAAP-GLPEEELGRLPLGEGLA 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107  82 VKAFNQGRLMKASNIVNCSRINLASKAFPSQNdNITHHATVPLKSGQEQFGILNVASPNTEIYSDEDLELLESVAFQLGS 161
Cdd:COG2203  264 GRALRTGEPVVVNDASTDPRFAPSLRELLLAL-GIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAI 342

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 162 AIKRIYLTDREKEAAKINERNRLARDLHDSVNQMLFSVKLTAHAAYGVSNESIAKQAFKTIEETSQNAVNEMRALIWQLK 241
Cdd:COG2203  343 AIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLL 422

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 446360107 242 PVGLEQGLIHALTAYSKLMHIQLNVNVEGLIDLSNEIEENIYRALQE 288
Cdd:COG2203  423 LLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILE 469
 
Name Accession Description Interval E-value
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
171-369 8.99e-53

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 175.19  E-value: 8.99e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 171 REKEAAKINERNRLARDLHDSVNQMLFSVKLTAHAAYGVSNESI--AKQAFKTIEETSQNAVNEMRALIWQLKPVGLEQ- 247
Cdd:COG4585   44 ARAEEAREEERRRIARELHDGVGQSLSAIKLQLEAARRLLDADPeaAREELEEIRELAREALAELRRLVRGLRPPALDDl 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 248 GLIHALTAY----SKLMHIQLNVNVEG-LIDLSNEIEENIYRALQECINNVKKHADTNKMDLTLKQMNDILYIDVIDYGQ 322
Cdd:COG4585  124 GLAAALEELaerlLRAAGIRVELDVDGdPDRLPPEVELALYRIVQEALTNALKHAGATRVTVTLEVDDGELTLTVRDDGV 203

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446360107 323 GFEIDNVqIASSHGINNIKQRVKLLRGKVTFHSQPTKGTQIQFTIPI 369
Cdd:COG4585  204 GFDPEAA-PGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPL 249
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 282-368 3.56e-18

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: 78.36  E-value: 3.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 282 IYRALQECINNVKKHADTNKMDLTLKQMNDILYIDVIDYGQGFEIDNVQIASSHGINNIKQRVKLLRGKVTFHSQPTKGT 361
Cdd:cd16917    1 LYRIVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPAPPGGGGFGLLGMRERAELLGGTLTIGSRPGGGT 80


                 ....*..
gi 446360107 362 QIQFTIP 368
Cdd:cd16917   81 RVTARLP 87
HisKA_3 pfam07730
Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of ...
 180-245 7.80e-18

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: 76.89  E-value: 7.80e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446360107  180 ERNRLARDLHDSVNQMLFSVKLTAHAAYGVSNESI--AKQAFKTIEETSQNAVNEMRALIWQLKPVGL 245
Cdd:pfam07730   1 ERNRIARELHDSVGQSLTAIKLQLELARRLLDRDPeeAREQLDAIRELAREALQELRRLLGDLRPPAL 68
GAF COG2203
GAF domain [Signal transduction mechanisms];
2-288 1.07e-16

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 81.78  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107   2 EQRTRLALLKEIAEFLNEETEMYSMTQGALKYLIEGSNFTTGWIFFINsvGEHELVSHVALPqSLTADHCHYIKDGSCWC 81
Cdd:COG2203  187 LELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVD--EDGGELELVAAP-GLPEEELGRLPLGEGLA 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107  82 VKAFNQGRLMKASNIVNCSRINLASKAFPSQNdNITHHATVPLKSGQEQFGILNVASPNTEIYSDEDLELLESVAFQLGS 161
Cdd:COG2203  264 GRALRTGEPVVVNDASTDPRFAPSLRELLLAL-GIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAI 342

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 162 AIKRIYLTDREKEAAKINERNRLARDLHDSVNQMLFSVKLTAHAAYGVSNESIAKQAFKTIEETSQNAVNEMRALIWQLK 241
Cdd:COG2203  343 AIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLL 422

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 446360107 242 PVGLEQGLIHALTAYSKLMHIQLNVNVEGLIDLSNEIEENIYRALQE 288
Cdd:COG2203  423 LLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILE 469
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
 20-163 4.68e-15

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: 71.34  E-value: 4.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107   20 ETEMYSMTQGALKYLIEGSNFTTGWIFFINsvGEHELVSHVALPQSLTADHCHYIKDGSCWcvKAFNQGRLMkasnIVNC 99
Cdd:pfam13185   1 AADLEELLDAVLEAAVELGASAVGFILLVD--DDGRLAAWGGAADELSAALDDPPGEGLVG--EALRTGRPV----IVND 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446360107  100 SRINLASKAFPSQNDNITHHATVPLKSGQEQFGILNVASPNTEIYSDEDLELLESVAFQLGSAI 163
Cdd:pfam13185  73 LAADPAKKGLPAGHAGLRSFLSVPLVSGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAI 136
PRK11644 PRK11644
signal transduction histidine-protein kinase/phosphatase UhpB;
146-368 1.61e-13

signal transduction histidine-protein kinase/phosphatase UhpB;


Pssm-ID: 236945 [Multi-domain]  Cd Length: 495  Bit Score: 71.55  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 146 DEDLELLESVAFQ------LGSAIKRiyltDREKEAAKINE--RNR----------------LARDLHDSVNQMLFSVKL 201
Cdd:PRK11644 247 DHPVDLLLSLLAQsltgllLGAGIQR----QRELNQSLQKElaRNRhlaerlleteesvrrdVARELHDEIGQTITAIRT 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 202 TAHAAYGVSNESI-AKQAFKTIEETSQNAVNEMRALIWQLKP-----VGLEQGlIHALT------AYSKLMHIQLNVNVE 269
Cdd:PRK11644 323 QAGIIKRLAADNAsVKQSAQLIEQLSLGVYDTVRRLLGRLRPrqlddLTLEQA-IRSLMremeleDRGIVSHLDWRIDES 401

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 270 GLidlSNEIEENIYRALQECINNVKKHADTNKMDLTLKQMNDILYIDVIDYGQGFEIDNVQiaSSHGINNIKQRVKLLRG 349
Cdd:PRK11644 402 AL---SETQRVTLFRVCQEGLNNIVKHADASAVTLQGWQQDERLMLVIEDDGSGLPPGSGQ--QGFGLRGMRERVTALGG 476

                        250
                 ....*....|....*....
gi 446360107 350 KVTFHSQPtkGTQIQFTIP 368
Cdd:PRK11644 477 TLTISCTH--GTRLSVSLP 493
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 282-370 8.82e-08

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 49.95  E-value: 8.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107   282 IYRALQECINNVKKHADTN-KMDLTLKQMNDILYIDVIDYGQGFEID--------------NVQIASSHGI--NNIKQRV 344
Cdd:smart00387   6 LRQVLSNLLDNAIKYTPEGgRITVTLERDGDHVEITVEDNGPGIPPEdlekifepffrtdkRSRKIGGTGLglSIVKKLV 85

                           90       100
                   ....*....|....*....|....*.
gi 446360107   345 KLLRGKVTFHSQPTKGTQIQFTIPIK 370
Cdd:smart00387  86 ELHGGEISVESEPGGGTTFTITLPLE 111
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
 45-173 5.97e-05

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: 42.75  E-value: 5.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107    45 IFFINSVGEHELVSHVA--LPQSLTADHchyIKDGSCWCVKAFNQGRLMkasNIVNCSRINLASKAFPSQNDNITHHATV 122
Cdd:smart00065  24 IYLVDENDRGELVLVAAdgLTLPTLGIR---FPLDEGLAGRVAETGRPL---NIPDVEADPLFAEDLLGRYQGVRSFLAV 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 446360107   123 PLKSGQEQFGILNVASP-NTEIYSDEDLELLESVAFQLGSAIKRIYLTDREK 173
Cdd:smart00065  98 PLVADGELVGVLALHNKkSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
171-369 8.99e-53

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 175.19  E-value: 8.99e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 171 REKEAAKINERNRLARDLHDSVNQMLFSVKLTAHAAYGVSNESI--AKQAFKTIEETSQNAVNEMRALIWQLKPVGLEQ- 247
Cdd:COG4585   44 ARAEEAREEERRRIARELHDGVGQSLSAIKLQLEAARRLLDADPeaAREELEEIRELAREALAELRRLVRGLRPPALDDl 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 248 GLIHALTAY----SKLMHIQLNVNVEG-LIDLSNEIEENIYRALQECINNVKKHADTNKMDLTLKQMNDILYIDVIDYGQ 322
Cdd:COG4585  124 GLAAALEELaerlLRAAGIRVELDVDGdPDRLPPEVELALYRIVQEALTNALKHAGATRVTVTLEVDDGELTLTVRDDGV 203

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446360107 323 GFEIDNVqIASSHGINNIKQRVKLLRGKVTFHSQPTKGTQIQFTIPI 369
Cdd:COG4585  204 GFDPEAA-PGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPL 249
UhpB COG3851
Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction ...
 133-368 9.17e-19

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


Pssm-ID: 443060 [Multi-domain]  Cd Length: 493  Bit Score: 87.37  E-value: 9.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 133 ILNVASPNTEIYSDEDLELLESVA----FQLGSAIKRIY-----LTDREKEA---------AKINERNRLARDLHDSVNQ 194
Cdd:COG3851  227 ALIAARQISSFHPLADLLLFLAAQsltgLLLGAAIQRQRqlnqqLEQELRENralarqlvsAEESERREIARELHDEIGQ 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 195 MLFSVKLTAHAAYGVSNESIAKQAFKTIEETSQNAVNEMRALIWQLKPVGLEQ-GL---IHALTAYSKL----MHIQLNV 266
Cdd:COG3851  307 NITAIRTQASILKRLAPQPEIEQSAQSIESLALRIYDTTRRLLDRLRPAVLDElGLeeaLRELPRELAFeepgISCQLDL 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 267 NVEGLiDLSNEIEENIYRALQECINNVKKHADTNKMDLTLKQMNDILYIDVIDYGQGFEIDNVqiASSHGINNIKQRVKL 346
Cdd:COG3851  387 RGDPS-LLDDTLQLTLYRLVQEALTNILKHAEASQIRISLSQDKRLLSLEIRDDGIGLPPELR--AKGFGLRGMRERVRA 463

                        250       260
                 ....*....|....*....|..
gi 446360107 347 LRGKVTFHSQPtKGTQIQFTIP 368
Cdd:COG3851  464 LGGDFRLSSAP-KGTRLSVLLP 484
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 282-368 3.56e-18

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: 78.36  E-value: 3.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 282 IYRALQECINNVKKHADTNKMDLTLKQMNDILYIDVIDYGQGFEIDNVQIASSHGINNIKQRVKLLRGKVTFHSQPTKGT 361
Cdd:cd16917    1 LYRIVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPAPPGGGGFGLLGMRERAELLGGTLTIGSRPGGGT 80


                 ....*..
gi 446360107 362 QIQFTIP 368
Cdd:cd16917   81 RVTARLP 87
HisKA_3 pfam07730
Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of ...
 180-245 7.80e-18

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: 76.89  E-value: 7.80e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446360107  180 ERNRLARDLHDSVNQMLFSVKLTAHAAYGVSNESI--AKQAFKTIEETSQNAVNEMRALIWQLKPVGL 245
Cdd:pfam07730   1 ERNRIARELHDSVGQSLTAIKLQLELARRLLDRDPeeAREQLDAIRELAREALQELRRLLGDLRPPAL 68
GAF COG2203
GAF domain [Signal transduction mechanisms];
2-288 1.07e-16

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 81.78  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107   2 EQRTRLALLKEIAEFLNEETEMYSMTQGALKYLIEGSNFTTGWIFFINsvGEHELVSHVALPqSLTADHCHYIKDGSCWC 81
Cdd:COG2203  187 LELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVD--EDGGELELVAAP-GLPEEELGRLPLGEGLA 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107  82 VKAFNQGRLMKASNIVNCSRINLASKAFPSQNdNITHHATVPLKSGQEQFGILNVASPNTEIYSDEDLELLESVAFQLGS 161
Cdd:COG2203  264 GRALRTGEPVVVNDASTDPRFAPSLRELLLAL-GIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAI 342

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 162 AIKRIYLTDREKEAAKINERNRLARDLHDSVNQMLFSVKLTAHAAYGVSNESIAKQAFKTIEETSQNAVNEMRALIWQLK 241
Cdd:COG2203  343 AIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLL 422

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 446360107 242 PVGLEQGLIHALTAYSKLMHIQLNVNVEGLIDLSNEIEENIYRALQE 288
Cdd:COG2203  423 LLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILE 469
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
 20-163 4.68e-15

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: 71.34  E-value: 4.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107   20 ETEMYSMTQGALKYLIEGSNFTTGWIFFINsvGEHELVSHVALPQSLTADHCHYIKDGSCWcvKAFNQGRLMkasnIVNC 99
Cdd:pfam13185   1 AADLEELLDAVLEAAVELGASAVGFILLVD--DDGRLAAWGGAADELSAALDDPPGEGLVG--EALRTGRPV----IVND 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446360107  100 SRINLASKAFPSQNDNITHHATVPLKSGQEQFGILNVASPNTEIYSDEDLELLESVAFQLGSAI 163
Cdd:pfam13185  73 LAADPAKKGLPAGHAGLRSFLSVPLVSGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAI 136
PRK11644 PRK11644
signal transduction histidine-protein kinase/phosphatase UhpB;
146-368 1.61e-13

signal transduction histidine-protein kinase/phosphatase UhpB;


Pssm-ID: 236945 [Multi-domain]  Cd Length: 495  Bit Score: 71.55  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 146 DEDLELLESVAFQ------LGSAIKRiyltDREKEAAKINE--RNR----------------LARDLHDSVNQMLFSVKL 201
Cdd:PRK11644 247 DHPVDLLLSLLAQsltgllLGAGIQR----QRELNQSLQKElaRNRhlaerlleteesvrrdVARELHDEIGQTITAIRT 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 202 TAHAAYGVSNESI-AKQAFKTIEETSQNAVNEMRALIWQLKP-----VGLEQGlIHALT------AYSKLMHIQLNVNVE 269
Cdd:PRK11644 323 QAGIIKRLAADNAsVKQSAQLIEQLSLGVYDTVRRLLGRLRPrqlddLTLEQA-IRSLMremeleDRGIVSHLDWRIDES 401

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 270 GLidlSNEIEENIYRALQECINNVKKHADTNKMDLTLKQMNDILYIDVIDYGQGFEIDNVQiaSSHGINNIKQRVKLLRG 349
Cdd:PRK11644 402 AL---SETQRVTLFRVCQEGLNNIVKHADASAVTLQGWQQDERLMLVIEDDGSGLPPGSGQ--QGFGLRGMRERVTALGG 476

                        250
                 ....*....|....*....
gi 446360107 350 KVTFHSQPtkGTQIQFTIP 368
Cdd:PRK11644 477 TLTISCTH--GTRLSVSLP 493
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 286-368 1.88e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA, YehU, Bacillus subtilis LytS, and some hybrid sensor histidine kinases; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. It also includes the HATPase domains of Escherichia coli YpdA and YehU, HKs of YpdA-YpdB and YehU-YehTCSs, which are involved together in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), some having accessory sensor domain(s) such as Cache, HAMP or GAF; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340401 [Multi-domain]  Cd Length: 103  Bit Score: 51.68  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 286 LQECINNVKKHA-----DTNKMDLTLKQMNDILYIDVIDYGQGFEID-------NVQIASSHGINNIKQRVKLLRGK--- 350
Cdd:cd16924    6 LQPLVENAIQHGlspltDKGVVTISALKEDNHVMIEVEDNGRGIDPKvlnilgkKPKEGNGIGLYNVHQRLILLFGEdyg 85

                         90
                 ....*....|....*...
gi 446360107 351 VTFHSQPTKGTQIQFTIP 368
Cdd:cd16924   86 IHIASEPDKGTRITFTIP 103
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 285-368 3.36e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis LytS and Staphylococcus aureus LytS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and a GAF sensor domain; most contain a DUF3816 domain.


Pssm-ID: 340433 [Multi-domain]  Cd Length: 106  Bit Score: 50.89  E-value: 3.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 285 ALQECINNVKKHADTNKmdltlKQMNDI----------LYIDVIDYGQGFEIDNVQ------IASSHG----INNIKQRV 344
Cdd:cd16957    5 ALQVLVENAIRHAFPKR-----KENNEVrvvvkkdqhkVHVSVSDNGQGIPEERLDllgkttVTSEKGtgtaLENLNRRL 79

                         90       100
                 ....*....|....*....|....*..
gi 446360107 345 KLLRGKVT---FHSQPTKGTQIQFTIP 368
Cdd:cd16957   80 IGLFGSEAclhIESEVHGGTEVWFVIP 106
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 282-370 8.32e-08

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: 50.06  E-value: 8.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107  282 IYRALQECINNVKKHA-DTNKMDLTLKQMNDIlYIDVIDYGQGFEIDNVQIASSH--------------GINNIKQRVKL 346
Cdd:pfam02518   6 LRQVLSNLLDNALKHAaKAGEITVTLSEGGEL-TLTVEDNGIGIPPEDLPRIFEPfstadkrggggtglGLSIVRKLVEL 84

                          90       100
                  ....*....|....*....|....
gi 446360107  347 LRGKVTFHSQPTKGTQIQFTIPIK 370
Cdd:pfam02518  85 LGGTITVESEPGGGTTVTLTLPLA 108
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 282-370 8.82e-08

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 49.95  E-value: 8.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107   282 IYRALQECINNVKKHADTN-KMDLTLKQMNDILYIDVIDYGQGFEID--------------NVQIASSHGI--NNIKQRV 344
Cdd:smart00387   6 LRQVLSNLLDNAIKYTPEGgRITVTLERDGDHVEITVEDNGPGIPPEdlekifepffrtdkRSRKIGGTGLglSIVKKLV 85

                           90       100
                   ....*....|....*....|....*.
gi 446360107   345 KLLRGKVTFHSQPTKGTQIQFTIPIK 370
Cdd:smart00387  86 ELHGGEISVESEPGGGTTFTITLPLE 111
GAF_3 pfam13492
GAF domain;
122-165 1.86e-07

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 49.68  E-value: 1.86e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 446360107  122 VPLKSGQEQFGILNVASPNTEIYSDEDLELLESVAFQLGSAIKR 165
Cdd:pfam13492  86 VPLVAGRRVIGVLALASSKPRAFDAEDLRLLESLAAQIATAIEN 129
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 169-370 6.31e-07

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 51.00  E-value: 6.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 169 TDREKEAAKINERNRLARDL----HDSVNQMlfsvkltaHAAYG-VSNESI--AKQAFKTIEETSQNAVNEMRALIwqlK 241
Cdd:COG3290  174 TELERLEEELEGVKELAEALraqrHDFRNHL--------HTISGlLQLGEYdeALEYIDEISEELQELIDSLLSRI---G 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 242 PVGLeQGLIHALTAYSKLMHIQLNVNVEGLIDLSNEIEENIYRALQECINN----VKKHADTNK-MDLTLKQMNDILYID 316
Cdd:COG3290  243 NPVL-AALLLGKAARARERGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNaieaVEKLPEEERrVELSIRDDGDELVIE 321

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446360107 317 VIDYGQG---FEIDNV-------QIASSHGI--NNIKQRVKLLRGKVTFHSQPTKGTQIQFTIPIK 370
Cdd:COG3290  322 VEDSGPGipeELLEKIfergfstKLGEGRGLglALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKE 387
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
122-189 1.14e-06

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 48.35  E-value: 1.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446360107 122 VPLKSGQEQFGILNVASPNTEIYSDEDLELLESVAFQLGSAIKRIYLTDREKEAakiNERNRLARDLH 189
Cdd:COG3605  114 VPIIRRGRVLGVLVVQSREPREFTEEEVEFLVTLAAQLAEAIANAELLGELRAA---LAELSLAREEE 178
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
 66-163 1.15e-06

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: 47.47  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107   66 LTADHCHYIKDGSCW------------CVKAFNQGRLMKASNIVNCSRinLASKAFPSQNDNITHHATVPLKSGQEQFGI 133
Cdd:pfam01590  27 PDADGLEYLPPGARWlkaagleippgtGVTVLRTGRPLVVPDAAGDPR--FLDPLLLLRNFGIRSLLAVPIIDDGELLGV 104

                          90       100       110
                  ....*....|....*....|....*....|
gi 446360107  134 LNVASPnTEIYSDEDLELLESVAFQLGSAI 163
Cdd:pfam01590 105 LVLHHP-RPPFTEEELELLEVLADQVAIAL 133
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
 122-163 5.89e-05

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: 44.45  E-value: 5.89e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446360107 122 VPLKSGQEQFGILNVASPNTEIYSDEDLELLESVAFQLGSAI 163
Cdd:COG3604   79 VPLRVGGEVLGVLTLDSRRPGAFSEEDLRLLETLASLAAVAI 120
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
 45-173 5.97e-05

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: 42.75  E-value: 5.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107    45 IFFINSVGEHELVSHVA--LPQSLTADHchyIKDGSCWCVKAFNQGRLMkasNIVNCSRINLASKAFPSQNDNITHHATV 122
Cdd:smart00065  24 IYLVDENDRGELVLVAAdgLTLPTLGIR---FPLDEGLAGRVAETGRPL---NIPDVEADPLFAEDLLGRYQGVRSFLAV 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 446360107   123 PLKSGQEQFGILNVASP-NTEIYSDEDLELLESVAFQLGSAIKRIYLTDREK 173
Cdd:smart00065  98 PLVADGELVGVLALHNKkSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
232-369 2.15e-04

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 42.20  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 232 EMRALIWQLKPVGLEQgLIHALTAYSKLMHIQLNVNVEGLIDLSNEI----EENIYRALQECINNVKKHADTN-KMDLTL 306
Cdd:COG2205   80 ESGKLSLELEPVDLAE-LLEEAVEELRPLAEEKGIRLELDLPPELPLvyadPELLEQVLANLLDNAIKYSPPGgTITISA 158

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446360107 307 KQMNDILYIDVIDYGQGF---EIDNV-----QIASSHGINN-------IKQRVKLLRGKVTFHSQPTKGTQIQFTIPI 369
Cdd:COG2205  159 RREGDGVRISVSDNGPGIpeeELERIferfyRGDNSRGEGGtglglaiVKRIVEAHGGTIWVESEPGGGTTFTVTLPL 236
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
293-370 2.69e-04

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 42.70  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 293 VKKHADTNKMDLTLKQMNDILYIDVIDYGQGF---EIDNVQIA-------SSHGINNIKQRVKLLRGK---VTFHSQPTK 359
Cdd:COG2972  353 IEPKEGGGTIRISIRKEGDRLVITVEDNGVGMpeeKLEKLLEElsskgegRGIGLRNVRERLKLYYGEeygLEIESEPGE 432

                         90
                 ....*....|.
gi 446360107 360 GTQIQFTIPIK 370
Cdd:COG2972  433 GTTVTIRIPLE 443
PRK10935 PRK10935
nitrate/nitrite two-component system sensor histidine kinase NarQ;
123-368 1.08e-03

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


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 40.99  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 123 PLKSGQEQFGILNVASPNTEIysdeDLELLESVAFQLGSAIkRIYLTDREKEA-AKINERNRLARDLHDSVNQML--FSV 199
Cdd:PRK10935 310 PLTMEDTVLGYLHWQASLPCP----DEPLMNNVAQMLGRGL-YFNQAQKQQQQlLLMEERATIARELHDSLAQVLsyLKI 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 200 KLTahaaygvsnesIAKQAFKTIEETSQNAVNEmraliwqlkpvgLEQGLIhalTAYSKL--------MHIQ---LNVNV 268
Cdd:PRK10935 385 QLT-----------LLKRSLDEDNAKAQSIIAE------------FDQALS---DAYRQLrellttfrLTIQeanLGSAL 438

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 269 EGLID-LSNEIEENI---YR-------------ALQ---ECINNVKKHADTNKMDLTLKQMNDILY-IDVIDYGQGFEID 327
Cdd:PRK10935 439 EEMLDqLRNQTDAKItldCRlpsqaldaqqqvhLLQiirEATLNAIKHANASEIAVSCVTNPDGEHtVSIRDDGIGIGEL 518

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446360107 328 NVQIasSH-GINNIKQRVKLLRGKVTFHSQPTKGTQIQFTIP 368
Cdd:PRK10935 519 KEPE--GHyGLNIMQERAERLGGTLTISQPPGGGTTVSLTFP 558
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
101-369 3.37e-03

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 39.12  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 101 RINLASKAFPSQNDNITHHATVPLKSGQEQFGILNVASPNTEIYSDEDLELLESVAFQLGSAIKRIYLTDREKEAAKINE 180
Cdd:COG0642   29 LLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 181 -RNRLARDL-HDsVNQMLFSVKLTAHAAYGVSNESIaKQAFKTIEEtsqnAVNEMRALI---------------WQLKPV 243
Cdd:COG0642  109 aKSRFLANVsHE-LRTPLTAIRGYLELLLEELDEEQ-REYLETILR----SADRLLRLIndlldlsrleagkleLEPEPV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 244 GLEQGLIHALTAYSKLM---HIQLNVNVEGLIDLSNEIEENIYRALQECINNVKKHADTNKM-DLTLKQMNDILYIDVID 319
Cdd:COG0642  183 DLAELLEEVVELFRPLAeekGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGTvTVSVRREGDRVRISVED 262

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446360107 320 YGQG---------FE----IDNVQIASSHGI-----NNIkqrVKLLRGKVTFHSQPTKGTQIQFTIPI 369
Cdd:COG0642  263 TGPGippedleriFEpffrTDPSRRGGGTGLglaivKRI---VELHGGTIEVESEPGKGTTFTVTLPL 327
HATPase_YpdA-like cd16955
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 307-368 9.20e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli YpdA, a HK of the two-component system (TCS) YpdA-YpdB which is involved in a nutrient sensing regulatory network with YehU-YehT. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and some have a GAF sensor domain; some contain a DUF3816 domain; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340431 [Multi-domain]  Cd Length: 102  Bit Score: 35.51  E-value: 9.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360107 307 KQMNDILYIDVIDYGQGFE---IDNVQIA----SSHGINNIKQRVKLLRG-KVTFHSQPTKGTQIQFTIP 368
Cdd:cd16955   33 KQLKNRLHIAVEDNGIGISpkvIERVEQDempgNKIGLLNVHQRLKLGYGeGLHIRSRPDPGTLIAFYIP 102
 
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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