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Conserved domains on  [gi|1405594046|gb|PZU51499|]
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histidine kinase [Thauera sp.]

Protein Classification

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];
199-432 3.08e-51

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


:

Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 173.65  E-value: 3.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 199 TMGVIAGIAVVATLLVALAGLALNVSDRRDAELK--MRELARQVVRSQENERARVAGELHDGVSQSLVSVKFLLESVQAR 276
Cdd:COG4585     3 ALALLGALALLVGALLGLLLALVLLRARRAERAAelERELAARAEEAREEERRRIARELHDGVGQSLSAIKLQLEAARRL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 277 LEQpaadALDAARRTLARGVAGVEEVLGDVRRISHGLRPTMLDTLGLVPAMKQVVDEFAQRSGTVVDMQADADIVA-PGD 355
Cdd:COG4585    83 LDA----DPEAAREELEEIRELAREALAELRRLVRGLRPPALDDLGLAAALEELAERLLRAAGIRVELDVDGDPDRlPPE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405594046 356 AGTALFRLLQEALNNIERHARASRVELRLSREPGAIALSIRDDGRGFDVEAVsasPQRGLGLSSMRERVEALGGRFD 432
Cdd:COG4585   159 VELALYRIVQEALTNALKHAGATRVTVTLEVDDGELTLTVRDDGVGFDPEAA---PGGGLGLRGMRERAEALGGTLT 232
sCache_2 pfam17200
Single Cache domain 2; This entry represents the single Cache domain 2 (sCache_2), which ...
 45-188 2.20e-41

Single Cache domain 2; This entry represents the single Cache domain 2 (sCache_2), which contains the long N-terminal helix domain. This domain recognizes pyruvate, acetate, propionate, glycolate, L-lactate, acetoacetate, urea and hydroxyurea, acetamide, formamide, L-malate and citromalate, malonate, methyl and bromosuccinate and citraconic acid (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 435780 [Multi-domain]  Cd Length: 153  Bit Score: 144.42  E-value: 2.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046  45 LMDSRRHELQNYVTLALASIAHLTTR------DEPAAREEALRVLRQLEFGN-DGYFFVYDLSGHVLMHPRQPDLVGQNL 117
Cdd:pfam17200   1 LIDQGKAQLKNLVNGAISLIEAVYAQvesgkiTLEEAQELAKELILGPRYGDgDGYFWVYDEDGNMLVHPFNPQLEGQNR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405594046 118 WELRDPQGRPTIQNLVSRAR-DGGGFVDFIWQRPSTGRIENKLGYVANVPQWGWMIGTGLYTDDIVAARERI 188
Cdd:pfam17200  81 SNLKDANGKYFIRELIATAKkAGGGFVTYLWKNPGEKAVEPKLAYVKYFPPWDWVIGTGSYMDDINAAAEKI 152
 
Name Accession Description Interval E-value
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
199-432 3.08e-51

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 173.65  E-value: 3.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 199 TMGVIAGIAVVATLLVALAGLALNVSDRRDAELK--MRELARQVVRSQENERARVAGELHDGVSQSLVSVKFLLESVQAR 276
Cdd:COG4585     3 ALALLGALALLVGALLGLLLALVLLRARRAERAAelERELAARAEEAREEERRRIARELHDGVGQSLSAIKLQLEAARRL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 277 LEQpaadALDAARRTLARGVAGVEEVLGDVRRISHGLRPTMLDTLGLVPAMKQVVDEFAQRSGTVVDMQADADIVA-PGD 355
Cdd:COG4585    83 LDA----DPEAAREELEEIRELAREALAELRRLVRGLRPPALDDLGLAAALEELAERLLRAAGIRVELDVDGDPDRlPPE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405594046 356 AGTALFRLLQEALNNIERHARASRVELRLSREPGAIALSIRDDGRGFDVEAVsasPQRGLGLSSMRERVEALGGRFD 432
Cdd:COG4585   159 VELALYRIVQEALTNALKHAGATRVTVTLEVDDGELTLTVRDDGVGFDPEAA---PGGGLGLRGMRERAEALGGTLT 232
sCache_2 pfam17200
Single Cache domain 2; This entry represents the single Cache domain 2 (sCache_2), which ...
 45-188 2.20e-41

Single Cache domain 2; This entry represents the single Cache domain 2 (sCache_2), which contains the long N-terminal helix domain. This domain recognizes pyruvate, acetate, propionate, glycolate, L-lactate, acetoacetate, urea and hydroxyurea, acetamide, formamide, L-malate and citromalate, malonate, methyl and bromosuccinate and citraconic acid (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 435780 [Multi-domain]  Cd Length: 153  Bit Score: 144.42  E-value: 2.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046  45 LMDSRRHELQNYVTLALASIAHLTTR------DEPAAREEALRVLRQLEFGN-DGYFFVYDLSGHVLMHPRQPDLVGQNL 117
Cdd:pfam17200   1 LIDQGKAQLKNLVNGAISLIEAVYAQvesgkiTLEEAQELAKELILGPRYGDgDGYFWVYDEDGNMLVHPFNPQLEGQNR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405594046 118 WELRDPQGRPTIQNLVSRAR-DGGGFVDFIWQRPSTGRIENKLGYVANVPQWGWMIGTGLYTDDIVAARERI 188
Cdd:pfam17200  81 SNLKDANGKYFIRELIATAKkAGGGFVTYLWKNPGEKAVEPKLAYVKYFPPWDWVIGTGSYMDDINAAAEKI 152
PRK11644 PRK11644
signal transduction histidine-protein kinase/phosphatase UhpB;
234-431 1.28e-31

signal transduction histidine-protein kinase/phosphatase UhpB;


Pssm-ID: 236945 [Multi-domain]  Cd Length: 495  Bit Score: 126.25  E-value: 1.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 234 RELARQVVRSQENERARVAGELHDGVSQSLVSVKfllesVQA----RLE--QPAADALDAARRTLARGVagveevLGDVR 307
Cdd:PRK11644  288 RHLAERLLETEESVRRDVARELHDEIGQTITAIR-----TQAgiikRLAadNASVKQSAQLIEQLSLGV------YDTVR 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 308 RISHGLRPTMLDTLGLVPAMKQVVDEFA-QRSGTVV--DMQADADIVAPGDAGTaLFRLLQEALNNIERHARASRVELRL 384
Cdd:PRK11644  357 RLLGRLRPRQLDDLTLEQAIRSLMREMElEDRGIVShlDWRIDESALSETQRVT-LFRVCQEGLNNIVKHADASAVTLQG 435

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1405594046 385 SREPGAIALSIRDDGRGFDVEavsaSPQRGLGLSSMRERVEALGGRF 431
Cdd:PRK11644  436 WQQDERLMLVIEDDGSGLPPG----SGQQGFGLRGMRERVTALGGTL 478
Cache_2 smart01049
Cache is an extracellular domain that is predicted to have a role in small-molecule ...
 45-129 1.02e-27

Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins; Members include the animal dihydropyridine-sensitive voltage-gated Ca2+ channel; alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. This domain consists of an N-terminal part with three predicted strands and an alpha-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the (unpermuted) Cache domain contains three predicted strands that could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, with Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source. The Cache domain appears to have arisen from the GAF-PAS fold despite their divergent functions.


Pssm-ID: 214995 [Multi-domain]  Cd Length: 91  Bit Score: 105.41  E-value: 1.02e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046   45 LMDSRRHELQNYVTLALASIAHLTTR------DEPAAREEALRVLRQLEFGNDGYFFVYDLSGHVLMHPRQPDLVGQNLW 118
Cdd:smart01049   1 LLEERKAELKNLVEIAVSIVEAYYAQaaagklTEEEAQAQAKAALRALRYGGDGYFFVYDSDGVMLMHPAKPELEGKNLS 80

                           90
                   ....*....|.
gi 1405594046  119 ELRDPQGRPTI 129
Cdd:smart01049  81 DLKDPNGKYLF 91
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 360-431 2.03e-21

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: 87.99  E-value: 2.03e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405594046 360 LFRLLQEALNNIERHARASRVELRLSREPGAIALSIRDDGRGFDVEAvsASPQRGLGLSSMRERVEALGGRF 431
Cdd:cd16917     1 LYRIVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPA--PPGGGGFGLLGMRERAELLGGTL 70
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 359-430 1.46e-12

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 63.82  E-value: 1.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046  359 ALFRLLQEALNNIERHARA-SRVELRLSREPGAIALSIRDDGRGFDVE--------------AVSASPQRGLGLSSMRER 423
Cdd:smart00387   5 RLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHVEITVEDNGPGIPPEdlekifepffrtdkRSRKIGGTGLGLSIVKKL 84


                   ....*..
gi 1405594046  424 VEALGGR 430
Cdd:smart00387  85 VELHGGE 91
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 358-432 6.02e-10

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: 56.22  E-value: 6.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 358 TALFRLLQEALNNIERHA-RASRVELRLSREpGAIALSIRDDGRGFDVE------------AVSASPQRGLGLSSMRERV 424
Cdd:pfam02518   4 LRLRQVLSNLLDNALKHAaKAGEITVTLSEG-GELTLTVEDNGIGIPPEdlprifepfstaDKRGGGGTGLGLSIVRKLV 82


                  ....*...
gi 1405594046 425 EALGGRFD 432
Cdd:pfam02518  83 ELLGGTIT 90
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
 81-178 4.72e-06

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350342 [Multi-domain]  Cd Length: 89  Bit Score: 44.74  E-value: 4.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046  81 RVLRQLEFGNDGYFFVYDLSGHVLMHPRqPDLVGQNLWELRDPQGRPTIQNLVSrardggGFVDFIWqrpSTGriENKLG 160
Cdd:cd18774     4 DLLSSIKLGETGYAFLVDSDGTILAHPP-KELVGKGKSLDDLALLAALLLAGES------GTFEYTS---DDG--VERLV 71

                          90
                  ....*....|....*...
gi 1405594046 161 YVANVPQWGWMIGTGLYT 178
Cdd:cd18774    72 AYRPVPGTPWVVVVGVPE 89
 
Name Accession Description Interval E-value
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
199-432 3.08e-51

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 173.65  E-value: 3.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 199 TMGVIAGIAVVATLLVALAGLALNVSDRRDAELK--MRELARQVVRSQENERARVAGELHDGVSQSLVSVKFLLESVQAR 276
Cdd:COG4585     3 ALALLGALALLVGALLGLLLALVLLRARRAERAAelERELAARAEEAREEERRRIARELHDGVGQSLSAIKLQLEAARRL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 277 LEQpaadALDAARRTLARGVAGVEEVLGDVRRISHGLRPTMLDTLGLVPAMKQVVDEFAQRSGTVVDMQADADIVA-PGD 355
Cdd:COG4585    83 LDA----DPEAAREELEEIRELAREALAELRRLVRGLRPPALDDLGLAAALEELAERLLRAAGIRVELDVDGDPDRlPPE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405594046 356 AGTALFRLLQEALNNIERHARASRVELRLSREPGAIALSIRDDGRGFDVEAVsasPQRGLGLSSMRERVEALGGRFD 432
Cdd:COG4585   159 VELALYRIVQEALTNALKHAGATRVTVTLEVDDGELTLTVRDDGVGFDPEAA---PGGGLGLRGMRERAEALGGTLT 232
COG4564 COG4564
Signal transduction histidine kinase [Signal transduction mechanisms];
32-409 6.66e-48

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 443621 [Multi-domain]  Cd Length: 510  Bit Score: 171.75  E-value: 6.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046  32 ALTDAEHAIVEPALMDSRRHELQNYVTLALASIAHL---TTRDEPAAREEALRVLRQLEFGNDGYFFVYDLSGHVLMHPR 108
Cdd:COG4564    13 ALAALSLETLRQALLEERKAELRALVELAVSIIAALyaaGELSEEEAKEQALAALRALRFGGDGYFFVYDYDGTMLAHPI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 109 QPDLVGQNLWELRDPQGRPTIQNLVSRA-RDGGGFVDFIWQRPSTGRIENKLGYVANVPQWGWMIGTGLYTDDIVAArer 187
Cdd:COG4564    93 NPELVGKNLLDLKDANGKYLIRELIEAAkKKGGGFVEYLWPKPGSGKPEPKLSYVKKFPPWDWVIGTGVYLDDIEAA--- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 188 IDRQARVAIRNTMGVIAGIAVVATLLVALAGLALNVSDRRDAELKMRELARQVVRSQENERARVAGELHDGVSQSLVSVK 267
Cdd:COG4564   170 FAAAALELLLLLALLLALALALLLLVLAALAGLLLASALEGELNLAGALAALLLAAAAELLAALLLIGAAAGALLALAEA 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 268 FLLESVQARLEQPAADALDAARRTLARGVAGVEEVLGDVRRISHGLRPTMLDTLGLVpAMKQVVDEFAQRSGTVVDMQAD 347
Cdd:COG4564   250 VAAVLAEALAAAAAAAAASAAASSAALAAAAAEAEAALAASEASAAAALAAAAAAAA-AAAAAAAAAEAAAAAAAAAAAA 328

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405594046 348 ADIVAPGDAGTALFRLLQEALNNIERHARASRVELRLSREPGAIALSIRDDGRGFDVEAVSA 409
Cdd:COG4564   329 AAAAASVADVAALAAAAAAAAAIAALAAAAAAAAAAAAAAAAIAAAAAAAAAAAAAAAAAAA 390
sCache_2 pfam17200
Single Cache domain 2; This entry represents the single Cache domain 2 (sCache_2), which ...
 45-188 2.20e-41

Single Cache domain 2; This entry represents the single Cache domain 2 (sCache_2), which contains the long N-terminal helix domain. This domain recognizes pyruvate, acetate, propionate, glycolate, L-lactate, acetoacetate, urea and hydroxyurea, acetamide, formamide, L-malate and citromalate, malonate, methyl and bromosuccinate and citraconic acid (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 435780 [Multi-domain]  Cd Length: 153  Bit Score: 144.42  E-value: 2.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046  45 LMDSRRHELQNYVTLALASIAHLTTR------DEPAAREEALRVLRQLEFGN-DGYFFVYDLSGHVLMHPRQPDLVGQNL 117
Cdd:pfam17200   1 LIDQGKAQLKNLVNGAISLIEAVYAQvesgkiTLEEAQELAKELILGPRYGDgDGYFWVYDEDGNMLVHPFNPQLEGQNR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405594046 118 WELRDPQGRPTIQNLVSRAR-DGGGFVDFIWQRPSTGRIENKLGYVANVPQWGWMIGTGLYTDDIVAARERI 188
Cdd:pfam17200  81 SNLKDANGKYFIRELIATAKkAGGGFVTYLWKNPGEKAVEPKLAYVKYFPPWDWVIGTGSYMDDINAAAEKI 152
UhpB COG3851
Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction ...
 226-432 1.06e-36

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


Pssm-ID: 443060 [Multi-domain]  Cd Length: 493  Bit Score: 140.53  E-value: 1.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 226 RRDAELKM-RELARQVVRSQENERARVAGELHDGVSQSLVSVKFLLESVQARLEQPAADALDAARRTLARGVAGVeevlg 304
Cdd:COG3851   270 QLEQELREnRALARQLVSAEESERREIARELHDEIGQNITAIRTQASILKRLAPQPEIEQSAQSIESLALRIYDT----- 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 305 dVRRISHGLRPTMLDTLGLVPAMKQVVDEFAQR-SGTVVDMQADADiVAPGDAGT--ALFRLLQEALNNIERHARASRVE 381
Cdd:COG3851   345 -TRRLLDRLRPAVLDELGLEEALRELPRELAFEePGISCQLDLRGD-PSLLDDTLqlTLYRLVQEALTNILKHAEASQIR 422

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1405594046 382 LRLSREPGAIALSIRDDGRGFDVEavsaSPQRGLGLSSMRERVEALGGRFD 432
Cdd:COG3851   423 ISLSQDKRLLSLEIRDDGIGLPPE----LRAKGFGLRGMRERVRALGGDFR 469
dCache_2 pfam08269
Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 ...
 76-181 4.32e-33

Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 (sCache_2) duplication.


Pssm-ID: 462414 [Multi-domain]  Cd Length: 298  Bit Score: 126.72  E-value: 4.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046  76 REEALRVLRQLEFGNDGYFFVYDLSGHVLMHPRQPDLVGQNLWELRDPQGRPTIQNLVSRA-RDGGGFVDFIWQRPSTGR 154
Cdd:pfam08269 191 KQELLKTLASIRYGNNGYIFIYDTDGNMILHPLKPELNGKDLTENKDDKGQELFQELLEAAkKKGEGFVTYKWPKPGGDK 270

                          90       100
                  ....*....|....*....|....*..
gi 1405594046 155 IENKLGYVANVPQWGWMIGTGLYTDDI 181
Cdd:pfam08269 271 PRPKISYVRYFPPWDWIIGTGVYLDEI 297
PRK11644 PRK11644
signal transduction histidine-protein kinase/phosphatase UhpB;
234-431 1.28e-31

signal transduction histidine-protein kinase/phosphatase UhpB;


Pssm-ID: 236945 [Multi-domain]  Cd Length: 495  Bit Score: 126.25  E-value: 1.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 234 RELARQVVRSQENERARVAGELHDGVSQSLVSVKfllesVQA----RLE--QPAADALDAARRTLARGVagveevLGDVR 307
Cdd:PRK11644  288 RHLAERLLETEESVRRDVARELHDEIGQTITAIR-----TQAgiikRLAadNASVKQSAQLIEQLSLGV------YDTVR 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 308 RISHGLRPTMLDTLGLVPAMKQVVDEFA-QRSGTVV--DMQADADIVAPGDAGTaLFRLLQEALNNIERHARASRVELRL 384
Cdd:PRK11644  357 RLLGRLRPRQLDDLTLEQAIRSLMREMElEDRGIVShlDWRIDESALSETQRVT-LFRVCQEGLNNIVKHADASAVTLQG 435

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1405594046 385 SREPGAIALSIRDDGRGFDVEavsaSPQRGLGLSSMRERVEALGGRF 431
Cdd:PRK11644  436 WQQDERLMLVIEDDGSGLPPG----SGQQGFGLRGMRERVTALGGTL 478
dCache_2 pfam08269
Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 ...
 48-199 2.15e-28

Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 (sCache_2) duplication.


Pssm-ID: 462414 [Multi-domain]  Cd Length: 298  Bit Score: 113.62  E-value: 2.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046  48 SRRHELQNYVTLALASIAHL-----TTRDEPAAREEALRVLRQLEF-GNDGYFFVYDLSGHVLMHPRQPDLVGQNLWELR 121
Cdd:pfam08269  45 SLKESLKSRVNEAYSIAESIyekykNKLSEEEIKKLIKEALRSIRFnDGTGYYFIIDKKGTVILHPDNPSLEGKNLLDLK 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 122 DPQGRPTIQNLVSRAR-DGGGFVDFIWQRPST-GRIENKLGYVANVPQWGWMIGTGLYTDDIvaaRERIDRQARVAIRNT 199
Cdd:pfam08269 125 DKDGRYIIREMIKLAKkKGEGFVDYLWPKPNGsDKPYKKISYVKYFEPLDWIIGTGEYLDDI---EEEIKQELLKTLASI 201
Cache_2 smart01049
Cache is an extracellular domain that is predicted to have a role in small-molecule ...
 45-129 1.02e-27

Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins; Members include the animal dihydropyridine-sensitive voltage-gated Ca2+ channel; alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. This domain consists of an N-terminal part with three predicted strands and an alpha-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the (unpermuted) Cache domain contains three predicted strands that could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, with Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source. The Cache domain appears to have arisen from the GAF-PAS fold despite their divergent functions.


Pssm-ID: 214995 [Multi-domain]  Cd Length: 91  Bit Score: 105.41  E-value: 1.02e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046   45 LMDSRRHELQNYVTLALASIAHLTTR------DEPAAREEALRVLRQLEFGNDGYFFVYDLSGHVLMHPRQPDLVGQNLW 118
Cdd:smart01049   1 LLEERKAELKNLVEIAVSIVEAYYAQaaagklTEEEAQAQAKAALRALRYGGDGYFFVYDSDGVMLMHPAKPELEGKNLS 80

                           90
                   ....*....|.
gi 1405594046  119 ELRDPQGRPTI 129
Cdd:smart01049  81 DLKDPNGKYLF 91
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 360-431 2.03e-21

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: 87.99  E-value: 2.03e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405594046 360 LFRLLQEALNNIERHARASRVELRLSREPGAIALSIRDDGRGFDVEAvsASPQRGLGLSSMRERVEALGGRF 431
Cdd:cd16917     1 LYRIVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPA--PPGGGGFGLLGMRERAELLGGTL 70
Cache_3-Cache_2 pfam17201
Cache 3/Cache 2 fusion domain; The Cache_3-Cache_2 domain likely originated as a fusion of ...
 71-191 6.65e-14

Cache 3/Cache 2 fusion domain; The Cache_3-Cache_2 domain likely originated as a fusion of sCache_3 and sCache_2 domains.


Pssm-ID: 465378 [Multi-domain]  Cd Length: 298  Bit Score: 72.00  E-value: 6.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046  71 DEPAAREEALRVLRQLEFGNDGYFFVYD----LSGHVLMHPrqpDLVGQNLWELRDPQGRPTIQNLVSrARDGggFVDFI 146
Cdd:pfam17201 182 PQDEALASLRKAIKKVKIGKTGYLYVLDgkgdQKGKFIVHP---TLEGKNILDAKDADGEPFVKKLLQ-KKVG--SLEYP 255

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1405594046 147 WQRPSTGRieNKLGYVANVPQWGWMIGTGLYTDDIVAARERIDRQ 191
Cdd:pfam17201 256 WKADAAGR--DKLAAFTYFEPWDWVIVASVYEDEFLAATNRLLNQ 298
PRK10600 PRK10600
nitrate/nitrite two-component system sensor histidine kinase NarX;
236-430 8.30e-14

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


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 73.55  E-value: 8.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 236 LARQVVRSQE----NERARVAGELHDGVSQSLVSVKFLLESVQ---ARLEQPAADALDAARRTLARGVAGVEEVLGDVRr 308
Cdd:PRK10600  346 LERQQERQQQlivmEERATIARELHDSIAQSLSCMKMQVSCLQmqgDALPESSRELLSQIRNELNASWRQLRELLTTFR- 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 309 ishgLRptmLDTLGLVPAMKQVVDEFAQRSG--TVVDMQADADIVaPGDAGTALFRLLQEALNNIERHARASRVELRLSR 386
Cdd:PRK10600  425 ----LQ---LTEPGLRPALEASCEEFSARFGfpVKLDYQLPPRLV-PSHQAIHLLQIAREALSNALKHAQASEVVVTVAQ 496

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1405594046 387 EPGAIALSIRDDGRGfdveaVSASPQRG--LGLSSMRERVEALGGR 430
Cdd:PRK10600  497 NQNQVKLSVQDNGCG-----VPENAERSnhYGLIIMRDRAQSLRGD 537
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 359-430 1.46e-12

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 63.82  E-value: 1.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046  359 ALFRLLQEALNNIERHARA-SRVELRLSREPGAIALSIRDDGRGFDVE--------------AVSASPQRGLGLSSMRER 423
Cdd:smart00387   5 RLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHVEITVEDNGPGIPPEdlekifepffrtdkRSRKIGGTGLGLSIVKKL 84


                   ....*..
gi 1405594046  424 VEALGGR 430
Cdd:smart00387  85 VELHGGE 91
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 358-432 6.02e-10

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: 56.22  E-value: 6.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 358 TALFRLLQEALNNIERHA-RASRVELRLSREpGAIALSIRDDGRGFDVE------------AVSASPQRGLGLSSMRERV 424
Cdd:pfam02518   4 LRLRQVLSNLLDNALKHAaKAGEITVTLSEG-GELTLTVEDNGIGIPPEdlprifepfstaDKRGGGGTGLGLSIVRKLV 82


                  ....*...
gi 1405594046 425 EALGGRFD 432
Cdd:pfam02518  83 ELLGGTIT 90
HisKA_3 pfam07730
Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of ...
 247-316 4.42e-08

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: 49.93  E-value: 4.42e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 247 ERARVAGELHDGVSQSLVSVKFLLESVQARLEQPaadaLDAARRTLARGVAGVEEVLGDVRRISHGLRPT 316
Cdd:pfam07730   1 ERNRIARELHDSVGQSLTAIKLQLELARRLLDRD----PEEAREQLDAIRELAREALQELRRLLGDLRPP 66
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
299-430 7.08e-07

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 50.29  E-value: 7.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 299 VEEVLgDVRRISHGLRPTMLDTLGLVPAMKQVVDEF---AQRSGTVVDMQADAD-IVAPGDAgTALFRLLQEALNNIERH 374
Cdd:COG2205    70 IEDLL-DLSRLESGKLSLELEPVDLAELLEEAVEELrplAEEKGIRLELDLPPElPLVYADP-ELLEQVLANLLDNAIKY 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 375 ARA-SRVELRLSREPGAIALSIRDDGRG---------FD----VEAVSASPQRGLGLSSMRERVEALGGR 430
Cdd:COG2205   148 SPPgGTITISARREGDGVRISVSDNGPGipeeeleriFErfyrGDNSRGEGGTGLGLAIVKRIVEAHGGT 217
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 331-432 8.16e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Erythrobacter litoralis blue light-activated histidine kinase 2; This domain family includes the histidine kinase-like ATPase (HATPase) domain of blue light-activated histidine kinase 2 of Erythrobacter litoralis (EL346). Signaling commonly occurs within HK dimers, however EL346 functions as a monomer. Also included in this family are the HATPase domains of ethanolamine utilization sensory transduction histidine kinase (EutW), whereby regulation of ethanolamine, a carbon and nitrogen source for gut bacteria, results in autophosphorylation and subsequent phosphoryl transfer to a response regulator (EutV) containing an RNA-binding domain. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory PAS sensor domain, while some have an N-terminal histidine kinase domain.


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 48.18  E-value: 8.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 331 VDEFAQRSGTVVDMQADaDIVAPGDAGTALFRLLQEALNNIERHARASR----VELRLSREPGAIALSIRDDGRGFDVEA 406
Cdd:cd16951    12 INAIHAVGDIRINITGD-TGPVSSEVATAIGLVVNELLQNALKHAFSDReggtITIRSVVDGDYLRITVIDDGVGLPQDE 90

                          90       100
                  ....*....|....*....|....*.
gi 1405594046 407 VSASPQRgLGLSSMRERVEALGGRFD 432
Cdd:cd16951    91 DWPNKGS-LGLQIVRSLVEGELKAFL 115
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
324-421 1.98e-06

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 46.83  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 324 VPAMKQVVDEFAQRSGTVVDMQADADIVapgdagtalfrlLQEALNNIERHARAS----RVELRLSREPGAIALSIRDDG 399
Cdd:COG2172    11 LGLARRAVRALLRELGLDEDDADDLVLA------------VSEAVTNAVRHAYGGdpdgPVEVELELDPDGLEIEVRDEG 78

                          90       100
                  ....*....|....*....|....*.
gi 1405594046 400 RGFDVEAV----SASPQRGLGLSSMR 421
Cdd:COG2172    79 PGFDPEDLpdpySTLAEGGRGLFLIR 104
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
 81-178 4.72e-06

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350342 [Multi-domain]  Cd Length: 89  Bit Score: 44.74  E-value: 4.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046  81 RVLRQLEFGNDGYFFVYDLSGHVLMHPRqPDLVGQNLWELRDPQGRPTIQNLVSrardggGFVDFIWqrpSTGriENKLG 160
Cdd:cd18774     4 DLLSSIKLGETGYAFLVDSDGTILAHPP-KELVGKGKSLDDLALLAALLLAGES------GTFEYTS---DDG--VERLV 71

                          90
                  ....*....|....*...
gi 1405594046 161 YVANVPQWGWMIGTGLYT 178
Cdd:cd18774    72 AYRPVPGTPWVVVVGVPE 89
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
299-430 2.40e-05

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 46.05  E-value: 2.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 299 VEEVLgDVRRISHGLRPTMLDTLGLVPAMKQVVDEF---AQRSGTVVDMQADADIV-APGDAGtalfrLLQEALNN---- 370
Cdd:COG0642   161 INDLL-DLSRLEAGKLELEPEPVDLAELLEEVVELFrplAEEKGIELELDLPDDLPtVRGDPD-----RLRQVLLNllsn 234

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1405594046 371 -IERHARASRVELRLSREPGAIALSIRDDGRGFDVEA--------VSASPQR-----GLGLSSMRERVEALGGR 430
Cdd:COG0642   235 aIKYTPEGGTVTVSVRREGDRVRISVEDTGPGIPPEDlerifepfFRTDPSRrgggtGLGLAIVKRIVELHGGT 308
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 83-180 2.63e-05

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350337 [Multi-domain]  Cd Length: 92  Bit Score: 42.75  E-value: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046  83 LRQLEFGNDGYFFVYDLSGHVLMHPRQpDLVGQNLweLRDPQGRPTIQNLVSRARdgGGFVDFIWQrpstGriENKLGYV 162
Cdd:cd12912     6 ISSIKIGETGYAFLVDKDGTIIAHPDK-ELVGKKI--SDDEAAEEELAKKMLAGK--SGSVEYTFN----G--EKKYVAY 74

                          90
                  ....*....|....*...
gi 1405594046 163 ANVPQWGWMIGTGLYTDD 180
Cdd:cd12912    75 APIPGTGWSLVVVVPESE 92
PRK10935 PRK10935
nitrate/nitrite two-component system sensor histidine kinase NarQ;
363-429 6.11e-05

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


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 45.23  E-value: 6.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1405594046 363 LLQ---EA-LNNIeRHARASRVELRLSREP-GAIALSIRDDGRGFDVeavSASPQRGLGLSSMRERVEALGG 429
Cdd:PRK10935  472 LLQiirEAtLNAI-KHANASEIAVSCVTNPdGEHTVSIRDDGIGIGE---LKEPEGHYGLNIMQERAERLGG 539
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 363-417 7.23e-05

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 41.48  E-value: 7.23e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405594046 363 LLQEALNNIERHARAS----RVELRLSREPGAIALSIRDDGRGFDVEAVS----ASPQRGLGL 417
Cdd:cd16936     4 AVSEAVTNAVRHAYRHdgpgPVRLELDLDPDRLRVEVTDSGPGFDPLRPAdpdaGLREGGRGL 66
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
320-417 7.98e-05

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 42.28  E-value: 7.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 320 TLGLVPAMKQVVDEFAQRSGtvVDMQADADIvapgdagtalfRL-LQEALNNIERHAR----ASRVELRLSREPGAIALS 394
Cdd:pfam13581   4 DPEQLRAARRVLEAVLRRAG--LPEELLDEV-----------ELaVGEACTNAVEHAYregpEGPVEVRLTSDGGGLVVT 70

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1405594046 395 IRDDGRGFDVEAVSASPQ---------RGLGL 417
Cdd:pfam13581  71 VADSGPPFDPLTLPPPDLeepdedrkeGGRGL 102
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 323-430 2.48e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG. PhoQ is the histidine kinase (HK) of the PhoP-PhoQ two-component regulatory system (TCS), which responds to the levels of Mg2+ and Ca2+, controls virulence, mediates the adaptation to Mg2+-limiting environments, and regulates numerous cellular activities. Providencia stuartii AarG is a putative sensor kinase which controls the expression of the 2'-N-acetyltransferase and an intrinsic multiple antibiotic resistance (Mar) response in Providencia stuartii. The AarG product is similar to PhoQ in that it is able to restore wild-type levels of resistance to a Salmonella typhimurium phoQ mutant. However, the expression of the 2'-N-acetyltransferase gene and of aarP (a gene encoding a transcriptional activator of 2'-N-acetyltransferase) are not significantly affected by the levels of Mg2+ or Ca2+. Most proteins in this group contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory HAMP sensor domain, and some have an intracellular membrane -interaction PhoQ sensor domain.


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 41.08  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 323 LVPAMKQVVDEFAQRSGTVVDMQADADIVAPGDAGtALFRLLQEALNNIERHArASRVELRLSREPGAIALSIRDDGRGF 402
Cdd:cd16954     2 LLDSLCSALNKVYQRKGVSISLDISPELRFPGERN-DLMELLGNLLDNACKWC-LEFVEVTARQTDGGLHLIVDDDGPGV 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1405594046 403 DVEAVSASPQR-----------GLGLSSMRERVEALGGR 430
Cdd:cd16954    80 PESQRSKIFQRgqrldeqrpgqGLGLAIAKEIVEQYGGE 118
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 366-432 2.55e-04

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 43.30  E-value: 2.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405594046 366 EALNNIERHARasRVELRLSREPGAIALSIRDDGRGFDVEAVS----------ASPQRGLGLSSMRERVEALGGRFD 432
Cdd:COG3290   295 EAVEKLPEEER--RVELSIRDDGDELVIEVEDSGPGIPEELLEkifergfstkLGEGRGLGLALVKQIVEKYGGTIE 369
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
299-430 4.39e-04

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 42.23  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 299 VEEVLgDVRRISHGLRPTMLDTLGLVPAMKQVVDEF---AQRSGTVVDMQA-DADIVAPGDAgtalfRLLQEALNN-IE- 372
Cdd:COG5002   219 VNDLL-DLSRLESGELKLEKEPVDLAELLEEVVEELrplAEEKGIELELDLpEDPLLVLGDP-----DRLEQVLTNlLDn 292

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1405594046 373 --RHARA-SRVELRLSREPGAIALSIRDDGRGFDVEA----------VSASPQR-----GLGLSSMRERVEALGGR 430
Cdd:COG5002   293 aiKYTPEgGTITVSLREEDDQVRISVRDTGIGIPEEDlpriferfyrVDKSRSRetggtGLGLAIVKHIVEAHGGR 368
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
 349-432 1.67e-03

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 40.66  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405594046 349 DIVAPGDAGTALFRLLQEALNNIERHARAS----RVELRLSREPGAIALSIRDDGRGFDvEAVSASPQRGLGLSSMRERV 424
Cdd:COG3920   389 DVELPADAAVPLGLILNELVTNALKHAFLSgeggRIRVSWRREDGRLRLTVSDNGVGLP-EDVDPPARKGLGLRLIRALV 467


                  ....*...
gi 1405594046 425 EALGGRFD 432
Cdd:COG3920   468 RQLGGTLE 475
 
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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