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Conserved domains on  [gi|446466513|ref|WP_000544367|]
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MULTISPECIES: two-component system sensor histidine kinase YpdA [Escherichia]

Protein Classification

sensor histidine kinase( domain architecture ID 11461692)

sensor histidine kinase, part of a two-component regulatory system, functions as a protein kinase that phosphorylates a target protein in response to an external signal

CATH:  3.30.565.10
EC:  2.7.13.3
PubMed:  10637609|10339418
SCOP:  4001957

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LytS COG3275
Sensor histidine kinase, LytS/YehU family [Signal transduction mechanisms];
297-551 3.96e-71

Sensor histidine kinase, LytS/YehU family [Signal transduction mechanisms];


:

Pssm-ID: 442506 [Multi-domain]  Cd Length: 352  Bit Score: 232.07  E-value: 3.96e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 297 IHSMLVIPLWEKGVVTGTLKIYYCHAHQITSSLQEMAVGLSQIISTQLEVSRAEQLREMANKAELRALQSKINPHFLFNA 376
Cdd:COG3275   97 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLILILLALLLSLQEEELELEELEKELLEAELKALKAQINPHFLFNT 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 377 LNAISSSIRLNPDTARQLIFNLSRYLRYNIELKDDEQIDIKKELYQIKDYIAIEQARFGDKLTVIYDIDEEV-NCYIPSL 455
Cdd:COG3275  177 LNSIYSLIREDPEKARELLLKLSDLLRYSLYESDKELVPLEEELEFLENYLELEKLRFGDRLQVEIDIDEELlDLLIPPL 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 456 LIQPLVENAIVHGIQPCKGKGVVTISVAECGNRVRIAVRDTGHGIDPKvierveaNEMPGNKIGLLNVHHRVKLLYGE-- 533
Cdd:COG3275  257 LLQPLVENAIKHGISSKEGGGTISISIEVEGDRLVIEVENNGVGIQPK-------KKKKGSGIGLKNVRERLELLYGDky 329
                        250
                 ....*....|....*....
gi 446466513 534 GLHIRRLEP-GTEIAFYIP 551
Cdd:COG3275  330 SLEIESTDGgGTKVTLKIP 348
5TM-5TMR_LYT pfam07694
5TMR of 5TMR-LYT; This entry represents the transmembrane region of the 5TM-LYT (5TM Receptors ...
28-194 1.01e-42

5TMR of 5TMR-LYT; This entry represents the transmembrane region of the 5TM-LYT (5TM Receptors of the LytS-YhcK type).


:

Pssm-ID: 429599  Cd Length: 170  Bit Score: 150.41  E-value: 1.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513   28 IRLFRELLHKSAHSPKELLAVTAIFSLFALFSTWSGVPVE-GSLVNVRIIAVMSGGILFGPWVGIITGVIAGIHRYLidI 106
Cdd:pfam07694   1 IPLFRRLLSKRRLRLKDKVLLGLIFGLFSILGTYTGIEIEpGAIANTRAVGIVLAGLLGGPIVGLIAGLIAGLHRYF--L 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513  107 GGVTAIPCFITSILAGCISGWINLKIPKAQR---WRVGILGGMLCETLTMILVIVWAPTTALGIDIVSKIGIPMIL-GSV 182
Cdd:pfam07694  79 GGFTALACGISTILAGLIAGLLHRRLKRRRRlisPLLAFLIGLIAEILQMLLILLLALPFDLALALVKTIALPMILvNSL 158
                         170
                  ....*....|..
gi 446466513  183 CIGFIVLLVQSV 194
Cdd:pfam07694 159 GTAIFLSILRDR 170
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
226-347 7.39e-03

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: 37.07  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513  226 ESLRKVCEIIRDDIHADAVAI-TNTDHVLAYVGVGEHNYQNGDDFISPTT-RQAMNYGKIIIKNNDEAH----------R 293
Cdd:pfam01590   4 EILQTILEELRELLGADRCALyLPDADGLEYLPPGARWLKAAGLEIPPGTgVTVLRTGRPLVVPDAAGDprfldpllllR 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446466513  294 TPEIHSMLVIPLWEKGVVTGTLKIYYCHAHqitssLQEMAVGLSQIISTQLEVS 347
Cdd:pfam01590  84 NFGIRSLLAVPIIDDGELLGVLVLHHPRPP-----FTEEELELLEVLADQVAIA 132
 
Name Accession Description Interval E-value
LytS COG3275
Sensor histidine kinase, LytS/YehU family [Signal transduction mechanisms];
297-551 3.96e-71

Sensor histidine kinase, LytS/YehU family [Signal transduction mechanisms];


Pssm-ID: 442506 [Multi-domain]  Cd Length: 352  Bit Score: 232.07  E-value: 3.96e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 297 IHSMLVIPLWEKGVVTGTLKIYYCHAHQITSSLQEMAVGLSQIISTQLEVSRAEQLREMANKAELRALQSKINPHFLFNA 376
Cdd:COG3275   97 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLILILLALLLSLQEEELELEELEKELLEAELKALKAQINPHFLFNT 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 377 LNAISSSIRLNPDTARQLIFNLSRYLRYNIELKDDEQIDIKKELYQIKDYIAIEQARFGDKLTVIYDIDEEV-NCYIPSL 455
Cdd:COG3275  177 LNSIYSLIREDPEKARELLLKLSDLLRYSLYESDKELVPLEEELEFLENYLELEKLRFGDRLQVEIDIDEELlDLLIPPL 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 456 LIQPLVENAIVHGIQPCKGKGVVTISVAECGNRVRIAVRDTGHGIDPKvierveaNEMPGNKIGLLNVHHRVKLLYGE-- 533
Cdd:COG3275  257 LLQPLVENAIKHGISSKEGGGTISISIEVEGDRLVIEVENNGVGIQPK-------KKKKGSGIGLKNVRERLELLYGDky 329
                        250
                 ....*....|....*....
gi 446466513 534 GLHIRRLEP-GTEIAFYIP 551
Cdd:COG3275  330 SLEIESTDGgGTKVTLKIP 348
HATPase_YpdA-like cd16955
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
452-551 4.67e-48

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: 162.24  E-value: 4.67e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 452 IPSLLIQPLVENAIVHGIQPCKGKGVVTISVAEC-GNRVRIAVRDTGHGIDPKVIERVEANEMPGNKIGLLNVHHRVKLL 530
Cdd:cd16955    1 IPKLMIQPLVENAIVHGIQEKKGKGVVKISVKKQlKNRLHIAVEDNGIGISPKVIERVEQDEMPGNKIGLLNVHQRLKLG 80
                         90       100
                 ....*....|....*....|..
gi 446466513 531 YGEGLHIRRL-EPGTEIAFYIP 551
Cdd:cd16955   81 YGEGLHIRSRpDPGTLIAFYIP 102
5TM-5TMR_LYT pfam07694
5TMR of 5TMR-LYT; This entry represents the transmembrane region of the 5TM-LYT (5TM Receptors ...
28-194 1.01e-42

5TMR of 5TMR-LYT; This entry represents the transmembrane region of the 5TM-LYT (5TM Receptors of the LytS-YhcK type).


Pssm-ID: 429599  Cd Length: 170  Bit Score: 150.41  E-value: 1.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513   28 IRLFRELLHKSAHSPKELLAVTAIFSLFALFSTWSGVPVE-GSLVNVRIIAVMSGGILFGPWVGIITGVIAGIHRYLidI 106
Cdd:pfam07694   1 IPLFRRLLSKRRLRLKDKVLLGLIFGLFSILGTYTGIEIEpGAIANTRAVGIVLAGLLGGPIVGLIAGLIAGLHRYF--L 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513  107 GGVTAIPCFITSILAGCISGWINLKIPKAQR---WRVGILGGMLCETLTMILVIVWAPTTALGIDIVSKIGIPMIL-GSV 182
Cdd:pfam07694  79 GGFTALACGISTILAGLIAGLLHRRLKRRRRlisPLLAFLIGLIAEILQMLLILLLALPFDLALALVKTIALPMILvNSL 158
                         170
                  ....*....|..
gi 446466513  183 CIGFIVLLVQSV 194
Cdd:pfam07694 159 GTAIFLSILRDR 170
His_kinase pfam06580
Histidine kinase; This family represents a region within bacterial histidine kinase enzymes. ...
359-438 6.44e-31

Histidine kinase; This family represents a region within bacterial histidine kinase enzymes. Two-component signal transduction systems such as those mediated by histidine kinase are integral parts of bacterial cellular regulatory processes, and are used to regulate the expression of genes involved in virulence. Members of this family often contain pfam02518 and/or pfam00672.


Pssm-ID: 461952 [Multi-domain]  Cd Length: 79  Bit Score: 114.85  E-value: 6.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513  359 AELRALQSKINPHFLFNALNAISSSIRLNPDTARQLIFNLSRYLRYNIElKDDEQIDIKKELYQIKDYIAIEQARFGDKL 438
Cdd:pfam06580   1 AELKALQAQINPHFLFNTLNSISSLAIEDPEEAAEMILKLSDLLRYSLY-EGEELVTLEEELEFLENYLEIQKIRFGDRL 79
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
453-551 5.62e-13

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 65.36  E-value: 5.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513   453 PSLLIQpLVENAIVHGIQPCKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERV---------EANEMPGNKIGLLNV 523
Cdd:smart00387   3 PDRLRQ-VLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIfepffrtdkRSRKIGGTGLGLSIV 81
                           90       100
                   ....*....|....*....|....*...
gi 446466513   524 HHRVKLLYGEGLHIRRLEPGTEIAFYIP 551
Cdd:smart00387  82 KKLVELHGGEISVESEPGGGTTFTITLP 109
ECF-S COG4720
ECF-type riboflavin transporter, membrane (S) component [Coenzyme transport and metabolism];
46-170 1.10e-04

ECF-type riboflavin transporter, membrane (S) component [Coenzyme transport and metabolism];


Pssm-ID: 443755 [Multi-domain]  Cd Length: 170  Bit Score: 42.92  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513  46 LAVTAIFS-LFALFSTWSGVPV--EGSLVNVRIIAVMSGGILFGPWVGIITGVIAGIhryLIDI---GGVTAIPCFITSI 119
Cdd:COG4720    8 LVLIALFAaLVFVLTMFIKIPIpiTNGYIHLGDAFIYLAALLFGPKAGALAGGIGSA---LADLlsgYPIWAPWTFIIKG 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446466513 120 LAGCISGWINLKIPKAQRWR------VGILGGMLCETLTMILVIV--WAPTTALGIDIV 170
Cdd:COG4720   85 LEGLIVGLIAKKLKKKSFKKiilaniLGGLVMVIGYYLAAPILYGgfAAALQSIPGNLL 143
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
453-508 4.03e-04

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 43.24  E-value: 4.03e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446466513 453 PSLLIQPLVeNAIVHGIQPCKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERV 508
Cdd:PRK10364 346 PDRLTQVLL-NLYLNAIQAIGQHGVISVTASESGAGVKISVTDSGKGIAADQLEAI 400
spIIAB TIGR01925
anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates ...
461-501 1.18e-03

anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates spore development in B subtilis. SpoIIAB binds to sigma F, preventing formation of the transcription complex at the promoter. SpoIIAA (anti-anti-sigma F factor) binds to SpoIIAB to inhibit association with sigma F, however SpoIIAB can phosphorylate SpoIIAA, causing disassociation of the SpoIIAA/B complex. The SpoIIE phosphatase dephosphorylates SpoIIAA. [Regulatory functions, Protein interactions, Cellular processes, Sporulation and germination]


Pssm-ID: 130980 [Multi-domain]  Cd Length: 137  Bit Score: 39.52  E-value: 1.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 446466513  461 VENAIVHGIQpCKGKGVVTISVAECGNRVRIAVRDTGHGID 501
Cdd:TIGR01925  48 VTNAIIHGYE-ENCEGVVYISATIEDHEVYITVRDEGIGIE 87
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
226-347 7.39e-03

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: 37.07  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513  226 ESLRKVCEIIRDDIHADAVAI-TNTDHVLAYVGVGEHNYQNGDDFISPTT-RQAMNYGKIIIKNNDEAH----------R 293
Cdd:pfam01590   4 EILQTILEELRELLGADRCALyLPDADGLEYLPPGARWLKAAGLEIPPGTgVTVLRTGRPLVVPDAAGDprfldpllllR 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446466513  294 TPEIHSMLVIPLWEKGVVTGTLKIYYCHAHqitssLQEMAVGLSQIISTQLEVS 347
Cdd:pfam01590  84 NFGIRSLLAVPIIDDGELLGVLVLHHPRPP-----FTEEELELLEVLADQVAIA 132
 
Name Accession Description Interval E-value
LytS COG3275
Sensor histidine kinase, LytS/YehU family [Signal transduction mechanisms];
297-551 3.96e-71

Sensor histidine kinase, LytS/YehU family [Signal transduction mechanisms];


Pssm-ID: 442506 [Multi-domain]  Cd Length: 352  Bit Score: 232.07  E-value: 3.96e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 297 IHSMLVIPLWEKGVVTGTLKIYYCHAHQITSSLQEMAVGLSQIISTQLEVSRAEQLREMANKAELRALQSKINPHFLFNA 376
Cdd:COG3275   97 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLILILLALLLSLQEEELELEELEKELLEAELKALKAQINPHFLFNT 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 377 LNAISSSIRLNPDTARQLIFNLSRYLRYNIELKDDEQIDIKKELYQIKDYIAIEQARFGDKLTVIYDIDEEV-NCYIPSL 455
Cdd:COG3275  177 LNSIYSLIREDPEKARELLLKLSDLLRYSLYESDKELVPLEEELEFLENYLELEKLRFGDRLQVEIDIDEELlDLLIPPL 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 456 LIQPLVENAIVHGIQPCKGKGVVTISVAECGNRVRIAVRDTGHGIDPKvierveaNEMPGNKIGLLNVHHRVKLLYGE-- 533
Cdd:COG3275  257 LLQPLVENAIKHGISSKEGGGTISISIEVEGDRLVIEVENNGVGIQPK-------KKKKGSGIGLKNVRERLELLYGDky 329
                        250
                 ....*....|....*....
gi 446466513 534 GLHIRRLEP-GTEIAFYIP 551
Cdd:COG3275  330 SLEIESTDGgGTKVTLKIP 348
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
324-554 9.59e-60

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 204.87  E-value: 9.59e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 324 QITSSLQEMavgLSQIISTQLEVSRAEQLRemaNKAELRALQSKINPHFLFNALNAISSSIRLN-PDTARQLIFNLSRYL 402
Cdd:COG2972  213 ILARSFNEM---VERIKELIEEVYELELEK---KEAELKALQAQINPHFLFNTLNSIRWLAELEdPEEAEEMLEALSKLL 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 403 RYNIElKDDEQIDIKKELYQIKDYIAIEQARFGDKLTVIYDIDEEV-NCYIPSLLIQPLVENAIVHGIQPCKGKGVVTIS 481
Cdd:COG2972  287 RYSLS-KGDELVTLEEELELIKSYLEIQKLRFGDRLEVEIEIDEELlDLLIPKLILQPLVENAIEHGIEPKEGGGTIRIS 365
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446466513 482 VAECGNRVRIAVRDTGHGIDPKVIERVEANEMP---GNKIGLLNVHHRVKLLYGE--GLHIR-RLEPGTEIAFYIPNQR 554
Cdd:COG2972  366 IRKEGDRLVITVEDNGVGMPEEKLEKLLEELSSkgeGRGIGLRNVRERLKLYYGEeyGLEIEsEPGEGTTVTIRIPLEE 444
HATPase_YpdA-like cd16955
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
452-551 4.67e-48

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: 162.24  E-value: 4.67e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 452 IPSLLIQPLVENAIVHGIQPCKGKGVVTISVAEC-GNRVRIAVRDTGHGIDPKVIERVEANEMPGNKIGLLNVHHRVKLL 530
Cdd:cd16955    1 IPKLMIQPLVENAIVHGIQEKKGKGVVKISVKKQlKNRLHIAVEDNGIGISPKVIERVEQDEMPGNKIGLLNVHQRLKLG 80
                         90       100
                 ....*....|....*....|..
gi 446466513 531 YGEGLHIRRL-EPGTEIAFYIP 551
Cdd:cd16955   81 YGEGLHIRSRpDPGTLIAFYIP 102
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
452-551 1.19e-46

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: 158.76  E-value: 1.19e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 452 IPSLLIQPLVENAIVHGIQPCKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERVEANEMPGNKIGLLNVHHRVKLLY 531
Cdd:cd16924    1 IPPFTLQPLVENAIQHGLSPLTDKGVVTISALKEDNHVMIEVEDNGRGIDPKVLNILGKKPKEGNGIGLYNVHQRLILLF 80
                         90       100
                 ....*....|....*....|...
gi 446466513 532 GEGLHIRRL---EPGTEIAFYIP 551
Cdd:cd16924   81 GEDYGIHIAsepDKGTRITFTIP 103
5TM-5TMR_LYT pfam07694
5TMR of 5TMR-LYT; This entry represents the transmembrane region of the 5TM-LYT (5TM Receptors ...
28-194 1.01e-42

5TMR of 5TMR-LYT; This entry represents the transmembrane region of the 5TM-LYT (5TM Receptors of the LytS-YhcK type).


Pssm-ID: 429599  Cd Length: 170  Bit Score: 150.41  E-value: 1.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513   28 IRLFRELLHKSAHSPKELLAVTAIFSLFALFSTWSGVPVE-GSLVNVRIIAVMSGGILFGPWVGIITGVIAGIHRYLidI 106
Cdd:pfam07694   1 IPLFRRLLSKRRLRLKDKVLLGLIFGLFSILGTYTGIEIEpGAIANTRAVGIVLAGLLGGPIVGLIAGLIAGLHRYF--L 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513  107 GGVTAIPCFITSILAGCISGWINLKIPKAQR---WRVGILGGMLCETLTMILVIVWAPTTALGIDIVSKIGIPMIL-GSV 182
Cdd:pfam07694  79 GGFTALACGISTILAGLIAGLLHRRLKRRRRlisPLLAFLIGLIAEILQMLLILLLALPFDLALALVKTIALPMILvNSL 158
                         170
                  ....*....|..
gi 446466513  183 CIGFIVLLVQSV 194
Cdd:pfam07694 159 GTAIFLSILRDR 170
His_kinase pfam06580
Histidine kinase; This family represents a region within bacterial histidine kinase enzymes. ...
359-438 6.44e-31

Histidine kinase; This family represents a region within bacterial histidine kinase enzymes. Two-component signal transduction systems such as those mediated by histidine kinase are integral parts of bacterial cellular regulatory processes, and are used to regulate the expression of genes involved in virulence. Members of this family often contain pfam02518 and/or pfam00672.


Pssm-ID: 461952 [Multi-domain]  Cd Length: 79  Bit Score: 114.85  E-value: 6.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513  359 AELRALQSKINPHFLFNALNAISSSIRLNPDTARQLIFNLSRYLRYNIElKDDEQIDIKKELYQIKDYIAIEQARFGDKL 438
Cdd:pfam06580   1 AELKALQAQINPHFLFNTLNSISSLAIEDPEEAAEMILKLSDLLRYSLY-EGEELVTLEEELEFLENYLEIQKIRFGDRL 79
HATPase_YehU-like cd16956
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
452-551 1.06e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YehU; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) including Escherichia coli YehU, a HK of the two-component system (TCS) YehU-YehT which is involved in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase); some have a GAF sensor domain while some have a cupin domain.


Pssm-ID: 340432 [Multi-domain]  Cd Length: 101  Bit Score: 67.08  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 452 IPSLLIQPLVENAIVHGIQPCKGKGVVTISVAECGNRVRIAVRDTGHGIDPkvIERVEANEMPGNKIGLLNVHHRVKLLY 531
Cdd:cd16956    1 LPFLTLQPIVENAVKHGLSGLLDGGRVEITARLDGQHLLLEVEDNGGGMDP--DTLARILIRSSNGLGLNLVDKRLRQAF 78
                         90       100
                 ....*....|....*....|...
gi 446466513 532 GE--GLHIR-RLEPGTEIAFYIP 551
Cdd:cd16956   79 GNdyGLDIEcAPGEGTRITIRLP 101
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
453-551 5.62e-13

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 65.36  E-value: 5.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513   453 PSLLIQpLVENAIVHGIQPCKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERV---------EANEMPGNKIGLLNV 523
Cdd:smart00387   3 PDRLRQ-VLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIfepffrtdkRSRKIGGTGLGLSIV 81
                           90       100
                   ....*....|....*....|....*...
gi 446466513   524 HHRVKLLYGEGLHIRRLEPGTEIAFYIP 551
Cdd:smart00387  82 KKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
452-551 3.93e-12

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: 62.83  E-value: 3.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 452 IPSLLIQPLVENAIVHGIQPCKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERVEANEMP---GNKIGLLNVHHRVK 528
Cdd:cd16957    1 VPPFALQVLVENAIRHAFPKRKENNEVRVVVKKDQHKVHVSVSDNGQGIPEERLDLLGKTTVTsekGTGTALENLNRRLI 80
                         90       100
                 ....*....|....*....|....*.
gi 446466513 529 LLYGE--GLHIRRLE-PGTEIAFYIP 551
Cdd:cd16957   81 GLFGSeaCLHIESEVhGGTEVWFVIP 106
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
361-508 1.19e-08

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 57.12  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 361 LRALQSKINPHFLFNALNAISSSIRlnpdTARQLIFNLSRYLRynielKDDEQ---IDIKKelyQIKDYIAIEQARFGDK 437
Cdd:COG4191  168 RRRLEDEPDPEELREALERILEGAE----RAAEIVRSLRAFSR-----RDEEErepVDLNE---LIDEALELLRPRLKAR 235
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446466513 438 -LTVIYDIDEE---VNCYiPSLLIQ---PLVENAIvHGIQPcKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERV 508
Cdd:COG4191  236 gIEVELDLPPDlppVLGD-PGQLEQvllNLLINAI-DAMEE-GEGGRITISTRREGDYVVISVRDNGPGIPPEVLERI 310
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
456-551 1.57e-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: 52.76  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513  456 LIQPLVENAIVHgiQPCKGKGVVTIsvaECGNRVRIAVRDTGHGIDPKVIERV-------EANEMPGNKIGLLNVHHRVK 528
Cdd:pfam02518   9 VLSNLLDNALKH--AAKAGEITVTL---SEGGELTLTVEDNGIGIPPEDLPRIfepfstaDKRGGGGTGLGLSIVRKLVE 83
                          90       100
                  ....*....|....*....|...
gi 446466513  529 LLYGEGLHIRRLEPGTEIAFYIP 551
Cdd:pfam02518  84 LLGGTITVESEPGGGTTVTLTLP 106
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
342-551 2.48e-07

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 52.93  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 342 TQLEvSRAEQLREMANKAE-LRALQskinpHFLFNALNAISSSIRLN-PDTARQLIFNLSrylrynielkDDEQIDIKKE 419
Cdd:COG3290  174 TELE-RLEEELEGVKELAEaLRAQR-----HDFRNHLHTISGLLQLGeYDEALEYIDEIS----------EELQELIDSL 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 420 LYQIKDYI-------AIEQARfGDKLTVIYDIDeevnCYIPSLLIQP---------LVENAIVHGIQPCKGKGVVTISVA 483
Cdd:COG3290  238 LSRIGNPVlaalllgKAARAR-ERGIDLTIDID----SDLPDLPLSDtdlvtilgnLLDNAIEAVEKLPEEERRVELSIR 312
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446466513 484 ECGNRVRIAVRDTGHGIDPKVIERVEANEMPGNK-----IGLLNVHHRVKLLYGEgLHIRRLEP-GTEIAFYIP 551
Cdd:COG3290  313 DDGDELVIEVEDSGPGIPEELLEKIFERGFSTKLgegrgLGLALVKQIVEKYGGT-IEVESEEGeGTVFTVRLP 385
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
395-508 2.67e-07

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 53.02  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 395 IFNLSRYLRYNIELkDDEQIDIKKELYQIKDYIaieQARFGDK-LTVIYDIDEEvNCYI---PSLLIQP---LVENAIVH 467
Cdd:COG5002  222 LLDLSRLESGELKL-EKEPVDLAELLEEVVEEL---RPLAEEKgIELELDLPED-PLLVlgdPDRLEQVltnLLDNAIKY 296
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446466513 468 GiqpcKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERV 508
Cdd:COG5002  297 T----PEGGTITVSLREEDDQVRISVRDTGIGIPEEDLPRI 333
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
376-551 3.47e-07

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 52.22  E-value: 3.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 376 ALNAISSSIrlnpDTARQLI---FNLSRYLRYNIELkDDEQIDIKKELYQIKDYIaieQARFGDK-LTVIYDIDEEVNCY 451
Cdd:COG0642  146 YLETILRSA----DRLLRLIndlLDLSRLEAGKLEL-EPEPVDLAELLEEVVELF---RPLAEEKgIELELDLPDDLPTV 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 452 I--PSLLIQ---PLVENAIVHGiqpcKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERV--------EANEMPGNKI 518
Cdd:COG0642  218 RgdPDRLRQvllNLLSNAIKYT----PEGGTVTVSVRREGDRVRISVEDTGPGIPPEDLERIfepffrtdPSRRGGGTGL 293
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446466513 519 GLLNVHHRVKLLYGEgLHIR-RLEPGTEIAFYIP 551
Cdd:COG0642  294 GLAIVKRIVELHGGT-IEVEsEPGKGTTFTVTLP 326
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
455-515 1.61e-06

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: 46.49  E-value: 1.61e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446466513 455 LLIQPLVENAIVHGiQPCKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERVEANEMPG 515
Cdd:cd16936    3 LAVSEAVTNAVRHA-YRHDGPGPVRLELDLDPDRLRVEVTDSGPGFDPLRPADPDAGLREG 62
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
376-551 2.18e-06

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 49.13  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 376 ALNAISSSIRLNPDTARQLIFNL---SRYLRYNIE--LK----DDEQIDIKKELYQIKDYI--AIEQARF---GDKLTVI 441
Cdd:COG2205   37 AAELLLDEEDLSPEERRELLEIIresAERLLRLIEdlLDlsrlESGKLSLELEPVDLAELLeeAVEELRPlaeEKGIRLE 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 442 YDIDEEvNCYI---PSLLIQ---PLVENAIVHGiqpcKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERV------- 508
Cdd:COG2205  117 LDLPPE-LPLVyadPELLEQvlaNLLDNAIKYS----PPGGTITISARREGDGVRISVSDNGPGIPEEELERIferfyrg 191
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446466513 509 -EANEMPGNKIGLLNVHHRVKLLYGEgLHIR-RLEPGTEIAFYIP 551
Cdd:COG2205  192 dNSRGEGGTGLGLAIVKRIVEAHGGT-IWVEsEPGGGTTFTVTLP 235
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
460-546 2.63e-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: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 460 LVENAIVHGiQPCKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERVEANEMPGNkIGLLNVHHRVkllygEGLHIRR 539
Cdd:COG2172   42 AVTNAVRHA-YGGDPDGPVEVELELDPDGLEIEVRDEGPGFDPEDLPDPYSTLAEGG-RGLFLIRRLM-----DEVEYES 114

                 ....*..
gi 446466513 540 LEPGTEI 546
Cdd:COG2172  115 DPGGTTV 121
ECF-ribofla_trS pfam07155
ECF-type riboflavin transporter, S component; This family is the substrate-binding component ...
46-191 8.87e-06

ECF-type riboflavin transporter, S component; This family is the substrate-binding component (S component) of the energy coupling-factor (ECF)-type riboflavin transporter. It is a transmembrane protein which binds riboflavin, and is responsible for riboflavin-uptake by cells.


Pssm-ID: 429320  Cd Length: 167  Bit Score: 46.08  E-value: 8.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513   46 LAVTAIFS-LFALFSTWSGVPVEGSLVNVRI--IAVMSGGILFGPWVGIITGVIAGIHRYLIDIGGVTAIPCFITSILAG 122
Cdd:pfam07155   4 VVAIAIGAaLFVVLTRFISIPTPNTKGYINLgdAFLALAAVLFGPVAGFLVGFIGHALKDLLSGYGIWWPWTLIISGLEG 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446466513  123 CISGWINLKIPKAQRWRVGILGGMLCETLTMIL--VIVWAPTTALGIDIVS----KIGIPMILGSVCIGFIVLLV 191
Cdd:pfam07155  84 LIVGLIAKRLGKNLKNGVFNIKGLLLFNLVMVIgyVIAWGLLAPFGDLIYSepanKVFLQSIPANIIQAVVGAII 158
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
416-551 8.97e-06

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: 45.49  E-value: 8.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 416 IKKELYQIKDYIAIEQARFGDKLTVI---YDIDEEVNCYIpSLLIQPLVENAIVHGIQPcKGKGVVTISVAECGNRVRIA 492
Cdd:cd16951    1 LGEYINRIASAINAIHAVGDIRINITgdtGPVSSEVATAI-GLVVNELLQNALKHAFSD-REGGTITIRSVVDGDYLRIT 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446466513 493 VRDTGHGIDpkvierVEANEMPGNKIGLLNVHHRVKLLYGEGLHIRRLEPGTEIAFYIP 551
Cdd:cd16951   79 VIDDGVGLP------QDEDWPNKGSLGLQIVRSLVEGELKAFLEVQSAENGTRVNIDIP 131
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
453-508 2.03e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; 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 AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 43.56  E-value: 2.03e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446466513 453 PSLLIQPLVeNAIVHGIQPCKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERV 508
Cdd:cd16943    1 PSQLNQVLL-NLLVNAAQAMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRI 55
GAF COG2203
GAF domain [Signal transduction mechanisms];
7-462 4.51e-05

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 46.34  E-value: 4.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513   7 MLLAVFDRAALMLICLFFLIRIRLFRELLHKSAHSPKELLAVTAIFSLFALFSTWSGVPVEGSLVNVRIIAVMSGGILFG 86
Cdd:COG2203    1 LLSVLALALAREVAAAELLEELATLLLALLLLALQALERVLETTELALALELLLERLTELRAAARLAAEAAEAALLLILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513  87 PWVGIITGVIAGIHRYLIDIGGVTAIPCFITSILAGCISGWINLKIPKAQRWRVGILGGMLCETLTMILVIVWAPTTALG 166
Cdd:COG2203   81 IDALVLLSLVATAGLVLELADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 167 IDIVSKIGIPmilgsvcIGFIVLLVQSVEGEKEASAARQAKLA--LDIANKTLPLfrhvnSESLRKVCEIIRDDIHADAV 244
Cdd:COG2203  161 TDLVGQLAAL-------AGLILDIARLLTQRARLELERLALLNeiSQALRSALDL-----EELLQRILELAGELLGADRG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 245 AI------TNTDHVLAYVGVGEHNYQNGDDFISPTtRQAMNYGKIII-----------KNNDEAHRTPEIHSMLVIPLWE 307
Cdd:COG2203  229 AIllvdedGGELELVAAPGLPEEELGRLPLGEGLA-GRALRTGEPVVvndastdprfaPSLRELLLALGIRSLLCVPLLV 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 308 KGVVTGTLKIYYCHAHQITSSLQEMAVGLSQIISTQLEVSRAEQLREMANKAELRALQSKINPHFLFNALNAISSSIRLN 387
Cdd:COG2203  308 DGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLEL 387
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446466513 388 PDTARQLIFNLSRYLRYNIELKDDEQIDIKKELYQIKDYIAIEQARFGDKLTVIYDIDEEVNCYIPSLLIQPLVE 462
Cdd:COG2203  388 LLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAEL 462
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
460-507 5.29e-05

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases; This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain.


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 44.11  E-value: 5.29e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446466513 460 LVENAIVHGIQP-----CKGK---GVVTISVAECGNRVRIAVRDTGHGIDPKVIER 507
Cdd:cd16916   46 LLRNAVDHGIEApeerlAAGKppeGTITLRAEHQGNQVVIEVSDDGRGIDREKIRE 101
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
423-508 7.13e-05

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 45.22  E-value: 7.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 423 IKDYIAIEQARFGDKLTVIYDIDE---EVNCYiPSLLIQpLVENAIVHGIQPCKGKGVVTISVA----------ECGNRV 489
Cdd:COG3852  210 LERVLELLRAEAPKNIRIVRDYDPslpEVLGD-PDQLIQ-VLLNLVRNAAEAMPEGGTITIRTRverqvtlgglRPRLYV 287
                         90
                 ....*....|....*....
gi 446466513 490 RIAVRDTGHGIDPKVIERV 508
Cdd:COG3852  288 RIEVIDNGPGIPEEILDRI 306
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
460-508 1.03e-04

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 44.95  E-value: 1.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446466513 460 LVENAIvhgiQPCKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERV 508
Cdd:COG5000  325 LLKNAI----EAIEEGGEIEVSTRREDGRVRIEVSDNGPGIPEEVLERI 369
ECF-S COG4720
ECF-type riboflavin transporter, membrane (S) component [Coenzyme transport and metabolism];
46-170 1.10e-04

ECF-type riboflavin transporter, membrane (S) component [Coenzyme transport and metabolism];


Pssm-ID: 443755 [Multi-domain]  Cd Length: 170  Bit Score: 42.92  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513  46 LAVTAIFS-LFALFSTWSGVPV--EGSLVNVRIIAVMSGGILFGPWVGIITGVIAGIhryLIDI---GGVTAIPCFITSI 119
Cdd:COG4720    8 LVLIALFAaLVFVLTMFIKIPIpiTNGYIHLGDAFIYLAALLFGPKAGALAGGIGSA---LADLlsgYPIWAPWTFIIKG 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446466513 120 LAGCISGWINLKIPKAQRWR------VGILGGMLCETLTMILVIV--WAPTTALGIDIV 170
Cdd:COG4720   85 LEGLIVGLIAKKLKKKSFKKiilaniLGGLVMVIGYYLAAPILYGgfAAALQSIPGNLL 143
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
478-551 1.14e-04

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 43.84  E-value: 1.14e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446466513 478 VTISVAECGNRVRIAVRDTGHGIDPkvierveaNEMPGNKIGLLNVHHRVKLLYGEgLHIRRLEP-GTEIAFYIP 551
Cdd:COG4585  183 VTVTLEVDDGELTLTVRDDGVGFDP--------EAAPGGGLGLRGMRERAEALGGT-LTIGSAPGgGTRVRATLP 248
ECF_trnsprt pfam12822
ECF transporter, substrate-specific component; Energy-coupling factor (ECF) transporters ...
46-159 1.48e-04

ECF transporter, substrate-specific component; Energy-coupling factor (ECF) transporters consist of a substrate-specific component (known as the S component), and an energy-coupling module. The substrate-binding component is a small integral membrane protein which captures specific substrates and forms an active transporter in the presence of the energy-coupling AT module.


Pssm-ID: 432808  Cd Length: 157  Bit Score: 42.29  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513   46 LAVTAIFS----LFALFSTWSGVPVEGSLVNvriIAVMSGGILFGPWVGIITGVIAGIHRYLIDIG-GVTAIPCFI-TSI 119
Cdd:pfam12822   3 LVIIALLSalsiVLMFTPPFPPIPLKIDLSH---IPALLGALLLGPLAGILIGLLTSLLSALTTGGgGPTGEPANFlPGI 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 446466513  120 LAGCISGWINLKIPKAQRWR--VGILGGMLCETLTMILVIVW 159
Cdd:pfam12822  80 LIGLVAGYLYKYGRNKKKKRilLALILGTILGTLVATLLNLL 121
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
379-520 1.77e-04

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 44.39  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 379 AISSSIRLnpdtaRQLIFNLSRYLRYNIELKDDEQIDIKKELYQIKD--YIAIEQARFgdklTVIYDIDEEVNCYiPSLL 456
Cdd:COG4251  326 IRDAAERM-----QALIDDLLAYSRVGRQELEFEPVDLNELLEEVLEdlEPRIEERGA----EIEVGPLPTVRGD-PTLL 395
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446466513 457 ---IQPLVENAIVHGIQpcKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERV--------EANEMPGNKIGL 520
Cdd:COG4251  396 rqvFQNLISNAIKYSRP--GEPPRIEIGAEREGGEWVFSVRDNGIGIDPEYAEKIfeifqrlhSRDEYEGTGIGL 468
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
460-507 2.09e-04

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 44.02  E-value: 2.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446466513 460 LVENAIVHGIQP-----CKGK---GVVTISVAECGNRVRIAVRDTGHGIDP-----KVIER 507
Cdd:COG0643  285 LVRNAVDHGIETpeerlAAGKpetGTITLSAYHEGGRVVIEVSDDGRGLDLekiraKAIEK 345
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
461-500 2.88e-04

Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of SpoIIAB, an anti sigma-F factor and a serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli where, early in sporulation, the cell divides into two unequal compartments: a larger mother cell and a smaller forespore. Sigma-F transcription factor is activated in the forespore directly after the asymmetric septum forms, and its spatial and temporal activation is required for sporulation. Free sigma-F can associate with the RNA polymerase core and activate transcription of the sigma-F regulon, its regulation may comprise a partner-switching mechanism involving SpoIIAB, SpoIIAA, and sigma-F as follows: SpoIIAB can form alternative complexes with either: i) sigma-F, holding it in an inactive form and preventing its association with RNA polymerase, or ii) unphosphorylated SpoIIAA and a nucleotide, either ATP or ADP. In the presence of ATP, SpoIIAB acts as a kinase to specifically phosphorylate a serine residue of SpoIIAA; this phosphorylated form has low affinity for SpoIIAB and dissociates, making SpoIIAB available to capture sigma-F. SpoIIAA may then be dephosphorylated by a SpoIIE serine phosphatase and be free to attack the SpoIIAB sigma-F complex to induce the release of sigma-F.


Pssm-ID: 340418 [Multi-domain]  Cd Length: 135  Bit Score: 40.98  E-value: 2.88e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446466513 461 VENAIVHGIQpCKGKGVVTISVAECGNRVRIAVRDTGHGI 500
Cdd:cd16942   47 VTNAIIHGYN-NDPNGIVSISVIIEDGVVHLTVRDEGVGI 85
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
453-508 4.03e-04

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 43.24  E-value: 4.03e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446466513 453 PSLLIQPLVeNAIVHGIQPCKGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERV 508
Cdd:PRK10364 346 PDRLTQVLL-NLYLNAIQAIGQHGVISVTASESGAGVKISVTDSGKGIAADQLEAI 400
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
457-551 5.27e-04

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: 39.07  E-value: 5.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 457 IQPLVENAIVHGiqpckGKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERveaneMPGNkiGLLNVHHRVKLLYGEgLH 536
Cdd:cd16917    5 VQEALTNALKHA-----GASRVRVTLSYTADELTLTVVDDGVGFDGPAPPG-----GGGF--GLLGMRERAELLGGT-LT 71
                         90
                 ....*....|....*.
gi 446466513 537 IRRLEP-GTEIAFYIP 551
Cdd:cd16917   72 IGSRPGgGTRVTARLP 87
spIIAB TIGR01925
anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates ...
461-501 1.18e-03

anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates spore development in B subtilis. SpoIIAB binds to sigma F, preventing formation of the transcription complex at the promoter. SpoIIAA (anti-anti-sigma F factor) binds to SpoIIAB to inhibit association with sigma F, however SpoIIAB can phosphorylate SpoIIAA, causing disassociation of the SpoIIAA/B complex. The SpoIIE phosphatase dephosphorylates SpoIIAA. [Regulatory functions, Protein interactions, Cellular processes, Sporulation and germination]


Pssm-ID: 130980 [Multi-domain]  Cd Length: 137  Bit Score: 39.52  E-value: 1.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 446466513  461 VENAIVHGIQpCKGKGVVTISVAECGNRVRIAVRDTGHGID 501
Cdd:TIGR01925  48 VTNAIIHGYE-ENCEGVVYISATIEDHEVYITVRDEGIGIE 87
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
476-507 2.33e-03

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


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 40.49  E-value: 2.33e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446466513 476 GVVTISVAECGNRVRIAVRDTGHGIDPKVIER 507
Cdd:COG5805  415 GTITIHTEEEDNSVIIRVIDEGIGIPEERLKK 446
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
454-561 2.45e-03

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 40.82  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 454 SLLIQPLVENAIVHGIQPCKGKGVVTISV---------------AECGNRVRIAVRDTGHGIDPKVIERV-EanemP--- 514
Cdd:PRK13837 558 PAELQQVLMNLCSNAAQAMDGAGRVDISLsraklrapkvlshgvLPPGRYVLLRVSDTGAGIDEAVLPHIfE----Pfft 633
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446466513 515 ----GNKIGLLNVHHRVKLLYGEGLHIRRLEPGTEIAFYIPNQ-RTPVASQA 561
Cdd:PRK13837 634 tragGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSsKVPVAPQA 685
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
226-347 7.39e-03

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: 37.07  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513  226 ESLRKVCEIIRDDIHADAVAI-TNTDHVLAYVGVGEHNYQNGDDFISPTT-RQAMNYGKIIIKNNDEAH----------R 293
Cdd:pfam01590   4 EILQTILEELRELLGADRCALyLPDADGLEYLPPGARWLKAAGLEIPPGTgVTVLRTGRPLVVPDAAGDprfldpllllR 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446466513  294 TPEIHSMLVIPLWEKGVVTGTLKIYYCHAHqitssLQEMAVGLSQIISTQLEVS 347
Cdd:pfam01590  84 NFGIRSLLAVPIIDDGELLGVLVLHHPRPP-----FTEEELELLEVLADQVAIA 132
envZ PRK09467
osmolarity sensor protein; Provisional
401-508 7.96e-03

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 38.74  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466513 401 YLRYNIELkDDEQIDIKKelyQIKDYIAIEQARFGDkltviydIDEEVNCYIPSLLIQP---------LVENAIVHGiqp 471
Cdd:PRK09467 282 YLRTGQEM-PMEMADLNA---LLGEVIAAESGYERE-------IETALQPGPIEVPMNPiaikralanLVVNAARYG--- 347
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446466513 472 ckgKGVVTISVAECGNRVRIAVRDTGHGIDPKVIERV 508
Cdd:PRK09467 348 ---NGWIKVSSGTEGKRAWFQVEDDGPGIPPEQLKHL 381
 
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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