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Conserved domains on  [gi|489115238|ref|WP_003025089|]
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MULTISPECIES: aerobic respiration two-component sensor histidine kinase ArcB [Citrobacter]

Protein Classification

sensor histidine kinase( domain architecture ID 11485196)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
1-778 0e+00

aerobic respiration control sensor protein ArcB; Provisional


:

Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 1554.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238   1 MKQIRMLAQYYVDLMMKLGLVRFSLLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
Cdd:PRK11091   1 MKQIRLLAQYYVDLMVKLGLVRFSLLLALALVVLAMVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  81 EESRQRLSRLVQKLEEMRERDLKLNVQLKDNIAQLNQEIVEREKAEAERQETFEQLKVEIKEREEAQIQLEQQSSFLRSF 160
Cdd:PRK11091  81 EESRQRLSRLVAKLEEMRERDLELNVQLKDNIAQLNQEIAEREKAEEARQEAFEQLKNEIKEREETQIELEQQSSLLRSF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 161 LDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKA 240
Cdd:PRK11091 161 LDASPDLVYYRNEDGEFSGCNRAMELLTGKSEKQLIGLTPKDVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 241 CFEIRKVPYYDRVGKRHGLMGFGRDITERKRYQDALERASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLTAEQEKY 320
Cdd:PRK11091 241 CFELRKVPFYDRVGKRHGLMGFGRDITERKRYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKY 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 321 LKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFMADLENLSGLQAQQKGLRFVLEPTLPLPHKVITDGTRLR 400
Cdd:PRK11091 321 LKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLR 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 401 QILWNLISNAVKFTQQGQVTVRARYDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKPATGTGIGLAVSKRLA 480
Cdd:PRK11091 401 QILWNLISNAVKFTQQGGVTVRVRYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKPATGTGIGLAVSKRLA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 481 KNMGGDITVSSQAGKGSIFTLTVHAPAVAEEIEDAFEDDDMPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKA 560
Cdd:PRK11091 481 QAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVEDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKE 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 561 ALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK11091 561 ALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 641 KYWDTRNEEESTVTSEESSKS-QALLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYLSVLESNLTARDKKGVVEEGHKI 719
Cdd:PRK11091 641 KFWDTQDDEESTVTTEESSKAnEALLDIPMLEQYVELVGPKLITDSLAVFEKMMPGYLSVLDSNLTARDQKGIVEEAHKI 720
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489115238 720 KGAAGSVGLRHLQQLGQQIQSPDLPAWEDNVAEWIEEMKQEWQHDVAVLKAWVASVEKK 778
Cdd:PRK11091 721 KGAAGSVGLRHLQQLAQQIQSPDLPAWWDNVQDWVEELKNEWRHDVEVLKAWLAQAEKK 779
 
Name Accession Description Interval E-value
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
1-778 0e+00

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 1554.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238   1 MKQIRMLAQYYVDLMMKLGLVRFSLLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
Cdd:PRK11091   1 MKQIRLLAQYYVDLMVKLGLVRFSLLLALALVVLAMVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  81 EESRQRLSRLVQKLEEMRERDLKLNVQLKDNIAQLNQEIVEREKAEAERQETFEQLKVEIKEREEAQIQLEQQSSFLRSF 160
Cdd:PRK11091  81 EESRQRLSRLVAKLEEMRERDLELNVQLKDNIAQLNQEIAEREKAEEARQEAFEQLKNEIKEREETQIELEQQSSLLRSF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 161 LDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKA 240
Cdd:PRK11091 161 LDASPDLVYYRNEDGEFSGCNRAMELLTGKSEKQLIGLTPKDVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 241 CFEIRKVPYYDRVGKRHGLMGFGRDITERKRYQDALERASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLTAEQEKY 320
Cdd:PRK11091 241 CFELRKVPFYDRVGKRHGLMGFGRDITERKRYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKY 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 321 LKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFMADLENLSGLQAQQKGLRFVLEPTLPLPHKVITDGTRLR 400
Cdd:PRK11091 321 LKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLR 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 401 QILWNLISNAVKFTQQGQVTVRARYDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKPATGTGIGLAVSKRLA 480
Cdd:PRK11091 401 QILWNLISNAVKFTQQGGVTVRVRYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKPATGTGIGLAVSKRLA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 481 KNMGGDITVSSQAGKGSIFTLTVHAPAVAEEIEDAFEDDDMPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKA 560
Cdd:PRK11091 481 QAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVEDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKE 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 561 ALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK11091 561 ALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 641 KYWDTRNEEESTVTSEESSKS-QALLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYLSVLESNLTARDKKGVVEEGHKI 719
Cdd:PRK11091 641 KFWDTQDDEESTVTTEESSKAnEALLDIPMLEQYVELVGPKLITDSLAVFEKMMPGYLSVLDSNLTARDQKGIVEEAHKI 720
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489115238 720 KGAAGSVGLRHLQQLGQQIQSPDLPAWEDNVAEWIEEMKQEWQHDVAVLKAWVASVEKK 778
Cdd:PRK11091 721 KGAAGSVGLRHLQQLAQQIQSPDLPAWWDNVQDWVEELKNEWRHDVEVLKAWLAQAEKK 779
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
277-771 4.01e-105

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 344.84  E-value: 4.01e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  277 ERASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPV 356
Cdd:TIGR02956 458 EEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPF 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  357 DFTSFMADLENLSGLQAQQKGLRFVLEPTLPLPHKVITDGTRLRQILWNLISNAVKFTQQGQVTVRARYDQGDMLHFEVE 436
Cdd:TIGR02956 538 DLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDSSLLFEVE 617
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  437 DSGIGIPQDEQDKIFAMYYQVkdsNGGKPATGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTVHAPaVAEEIEDAF 516
Cdd:TIGR02956 618 DTGCGIAEEEQATLFDAFTQA---DGRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLT-RGKPAEDSA 693
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  517 EDDDMPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYA 596
Cdd:TIGR02956 694 TLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIYG 773
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  597 REDLPPLVALTANVLKDKKE-YLDAGMDDVLSKPLSVPALTAMIKKYWDTRNEEES---------------------TVT 654
Cdd:TIGR02956 774 AKNEVKFIAFSAHVFNEDVAqYLAAGFDGFLAKPVVEEQLTAMIAVILAGGKSNTEapvlsaspsfdsasvienaqaDDI 853
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  655 SEESSKSQALLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYLSVLESNLTARDKKGVVEEGHKIKGAAGSVGLRHLQQL 734
Cdd:TIGR02956 854 PESNQASEFLLDEEQLQQDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQL 933
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 489115238  735 GQQIQSPDLPAWEDNVAewIEEMKQEWQHDVAVLKAW 771
Cdd:TIGR02956 934 CQQLEKQGKTGALELSD--IDEIKQAWQASKTALDQW 968
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
275-502 1.90e-70

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 234.42  E-value: 1.90e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 275 ALERASRDKTTFISTISHELRTPLNGIVGLSRILLDTdLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQ 354
Cdd:COG0642  102 LLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPE 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 355 PVDFTSFMADLENLSGLQAQQKGLRFVLEPTLPLPHkVITDGTRLRQILWNLISNAVKFTQQG-QVTVRARYDqGDMLHF 433
Cdd:COG0642  181 PVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPT-VRGDPDRLRQVLLNLLSNAIKYTPEGgTVTVSVRRE-GDRVRI 258
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489115238 434 EVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKpatGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLT 502
Cdd:COG0642  259 SVEDTGPGIPPEDLERIFEPFFRTDPSRRGG---GTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVT 324
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
399-504 4.60e-47

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 162.66  E-value: 4.60e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFTQQGQVTVRARYD----QGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVkDSNGGKPATGTGIGLA 474
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEeeeeDGVQLRFSVEDTGIGIPEEQQARLFEPFSQA-DSSTTRKYGGTGLGLA 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 489115238 475 VSKRLAKNMGGDITVSSQAGKGSIFTLTVH 504
Cdd:cd16922   80 ISKKLVELMGGDISVESEPGQGSTFTFTLP 109
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
394-504 3.44e-35

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 129.31  E-value: 3.44e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238   394 TDGTRLRQILWNLISNAVKFT-QQGQVTVRARyDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKPatGTGIG 472
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLE-RDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIG--GTGLG 77
                           90       100       110
                   ....*....|....*....|....*....|..
gi 489115238   473 LAVSKRLAKNMGGDITVSSQAGKGSIFTLTVH 504
Cdd:smart00387  78 LSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
394-506 2.14e-32

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: 121.32  E-value: 2.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  394 TDGTRLRQILWNLISNAVKFT-QQGQVTVRARydQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGkpatGTGIG 472
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAaKAGEITVTLS--EGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGG----GTGLG 74
                          90       100       110
                  ....*....|....*....|....*....|....
gi 489115238  473 LAVSKRLAKNMGGDITVSSQAGKGSIFTLTVHAP 506
Cdd:pfam02518  75 LSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
265-502 9.94e-28

cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in Staphylococcus aureus (sp|Q2G2U4.1|WALK_STAA8). A shorter version, as found in Streptococcus pneumoniae, called WalK(Spn) or VicK, is not included. WalK is part of a two-component system and works with partner protein WalR.


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 118.70  E-value: 9.94e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 265 DITErkryQDALERASRDkttFISTISHELRTPLNGIVGLSRILLDTDLTAEQ--EKYLKtihvsaVTLGN------IFN 336
Cdd:NF033092 361 DVTE----QEKIEQERRE---FVANVSHELRTPLTTMRSYLEALADGAWKDPElaPRFLG------VTQNEtermirLVN 427
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 337 DIIDMDKMERRKVQLDNQPVDFTSFMADLENLSGLQAQQKGLRFVLEptlpLPHKVIT---DGTRLRQILWNLISNAVKF 413
Cdd:NF033092 428 DLLQLSRMDSKDYKLNKEWVNFNEFFNYIIDRFEMILKNKNITFKRE----FPKRDLWveiDTDKITQVLDNIISNAIKY 503
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 414 TQQ-GQVTVRARyDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVkDsnggKPAT----GTGIGLAVSKRLAKNMGGDIT 488
Cdd:NF033092 504 SPEgGTITFRLL-ETHNRIIISISDQGLGIPKKDLDKIFDRFYRV-D----KARSrkmgGTGLGLAIAKEVVEAHGGRIW 577
                        250
                 ....*....|....
gi 489115238 489 VSSQAGKGSIFTLT 502
Cdd:NF033092 578 AESEEGKGTTIYFT 591
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
290-501 2.13e-17

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 84.66  E-value: 2.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 290 ISHELRTPLNGIVGLSRILLDTDLTAEqEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFMADLENLS 369
Cdd:NF012226 145 IAHELRTPITILQGRLQGILDGVFEPD-PALFKSLLNQVEGLSHLVEDLRTLSLVENQQLRLNYESVDLKDSIEKVLKMF 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 370 GLQAQQKGLRFVLEPTLPLphkVITDGTRLRQILWNLISNAVKFTQQGQVTVRARYDQGDMLhFEVEDSGIGIPQDEQDK 449
Cdd:NF012226 224 EDRLEQAQLTIVLNLTATP---VFCDRRRIEQVLIALIDNAIRYANAGKLKISSSVIQDDWI-LQIEDEGPGIAEEYQQD 299
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489115238 450 IFAMYYQVKDSNgGKPATGTGIGLAVSKRLAKNMGGDITVSSQAGkGSIFTL 501
Cdd:NF012226 300 LFNPFFRLEQSR-NKEFGGTGLGLAVVHAIVIAHKGSIEYSNSQG-NSVFTI 349
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
276-509 9.08e-17

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 83.92  E-value: 9.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 276 LERASRDKTTFISTISHELRTPLNGIVGLSRILLDT--DLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDN 353
Cdd:NF040691 264 LEELSRLQQRFVSDVSHELRTPLTTIRMAADVIHDSrdDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAELDV 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 354 QPVDFTSF-MADLENLSGLqAQQKGLRFVLE-PTLPLPHKVitDGTRLRQILWNLISNAVKFTQQGQVTVRARYDqGDML 431
Cdd:NF040691 344 EPVDLRPLvRRVVDALRQL-AERAGVELRVDaPGTPVVAEV--DPRRVERVLRNLVVNAIEHGEGKPVVVTVAQD-DTAV 419
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489115238 432 HFEVEDSGIGIPQDEQDKIFAMYYQVkDSNGGKPATGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTVhaPAVA 509
Cdd:NF040691 420 AVTVRDHGVGLKPGEVALVFDRFWRA-DPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTL--PRVA 494
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
263-487 9.39e-16

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 80.64  E-value: 9.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 263 GRDITERKRYQDALERASRDKTTFISTISHELRTPLngivglsrILLDTDLTAEQE-------KYLKTIHVSAVTLGNIF 335
Cdd:NF012163 220 GKLAQDFNQLASTLEKNEQMRRDFMADISHELRTPL--------AVLRAELEAIQDgirkftpESLDSLQAEVGTLTKLV 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 336 NDIIDMDKMERRKVQLDNQPVDFTSFMADLENLSGLQAQQKGLRfvLEPTLPLPHKVITDGTRLRQILWNLISNAVKFTQ 415
Cdd:NF012163 292 DDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLE--LEVSLPDSSLVFGDRDRLMQLFNNLLENSLRYTD 369
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489115238 416 Q-GQVTVRARyDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKPAtGTGIGLAVSKRLAKNMGGDI 487
Cdd:NF012163 370 SgGSLHISAS-QRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASG-GSGLGLAISLNIVQAHGGTL 440
 
Name Accession Description Interval E-value
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
1-778 0e+00

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 1554.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238   1 MKQIRMLAQYYVDLMMKLGLVRFSLLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
Cdd:PRK11091   1 MKQIRLLAQYYVDLMVKLGLVRFSLLLALALVVLAMVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  81 EESRQRLSRLVQKLEEMRERDLKLNVQLKDNIAQLNQEIVEREKAEAERQETFEQLKVEIKEREEAQIQLEQQSSFLRSF 160
Cdd:PRK11091  81 EESRQRLSRLVAKLEEMRERDLELNVQLKDNIAQLNQEIAEREKAEEARQEAFEQLKNEIKEREETQIELEQQSSLLRSF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 161 LDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKA 240
Cdd:PRK11091 161 LDASPDLVYYRNEDGEFSGCNRAMELLTGKSEKQLIGLTPKDVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 241 CFEIRKVPYYDRVGKRHGLMGFGRDITERKRYQDALERASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLTAEQEKY 320
Cdd:PRK11091 241 CFELRKVPFYDRVGKRHGLMGFGRDITERKRYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKY 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 321 LKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFMADLENLSGLQAQQKGLRFVLEPTLPLPHKVITDGTRLR 400
Cdd:PRK11091 321 LKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLR 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 401 QILWNLISNAVKFTQQGQVTVRARYDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKPATGTGIGLAVSKRLA 480
Cdd:PRK11091 401 QILWNLISNAVKFTQQGGVTVRVRYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKPATGTGIGLAVSKRLA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 481 KNMGGDITVSSQAGKGSIFTLTVHAPAVAEEIEDAFEDDDMPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKA 560
Cdd:PRK11091 481 QAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVEDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKE 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 561 ALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK11091 561 ALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 641 KYWDTRNEEESTVTSEESSKS-QALLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYLSVLESNLTARDKKGVVEEGHKI 719
Cdd:PRK11091 641 KFWDTQDDEESTVTTEESSKAnEALLDIPMLEQYVELVGPKLITDSLAVFEKMMPGYLSVLDSNLTARDQKGIVEEAHKI 720
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489115238 720 KGAAGSVGLRHLQQLGQQIQSPDLPAWEDNVAEWIEEMKQEWQHDVAVLKAWVASVEKK 778
Cdd:PRK11091 721 KGAAGSVGLRHLQQLAQQIQSPDLPAWWDNVQDWVEELKNEWRHDVEVLKAWLAQAEKK 779
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
277-771 4.01e-105

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 344.84  E-value: 4.01e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  277 ERASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPV 356
Cdd:TIGR02956 458 EEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPF 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  357 DFTSFMADLENLSGLQAQQKGLRFVLEPTLPLPHKVITDGTRLRQILWNLISNAVKFTQQGQVTVRARYDQGDMLHFEVE 436
Cdd:TIGR02956 538 DLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDSSLLFEVE 617
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  437 DSGIGIPQDEQDKIFAMYYQVkdsNGGKPATGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTVHAPaVAEEIEDAF 516
Cdd:TIGR02956 618 DTGCGIAEEEQATLFDAFTQA---DGRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLT-RGKPAEDSA 693
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  517 EDDDMPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYA 596
Cdd:TIGR02956 694 TLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIYG 773
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  597 REDLPPLVALTANVLKDKKE-YLDAGMDDVLSKPLSVPALTAMIKKYWDTRNEEES---------------------TVT 654
Cdd:TIGR02956 774 AKNEVKFIAFSAHVFNEDVAqYLAAGFDGFLAKPVVEEQLTAMIAVILAGGKSNTEapvlsaspsfdsasvienaqaDDI 853
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  655 SEESSKSQALLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYLSVLESNLTARDKKGVVEEGHKIKGAAGSVGLRHLQQL 734
Cdd:TIGR02956 854 PESNQASEFLLDEEQLQQDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQL 933
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 489115238  735 GQQIQSPDLPAWEDNVAewIEEMKQEWQHDVAVLKAW 771
Cdd:TIGR02956 934 CQQLEKQGKTGALELSD--IDEIKQAWQASKTALDQW 968
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
275-502 1.90e-70

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 234.42  E-value: 1.90e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 275 ALERASRDKTTFISTISHELRTPLNGIVGLSRILLDTdLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQ 354
Cdd:COG0642  102 LLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPE 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 355 PVDFTSFMADLENLSGLQAQQKGLRFVLEPTLPLPHkVITDGTRLRQILWNLISNAVKFTQQG-QVTVRARYDqGDMLHF 433
Cdd:COG0642  181 PVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPT-VRGDPDRLRQVLLNLLSNAIKYTPEGgTVTVSVRRE-GDRVRI 258
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489115238 434 EVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKpatGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLT 502
Cdd:COG0642  259 SVEDTGPGIPPEDLERIFEPFFRTDPSRRGG---GTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVT 324
PRK15347 PRK15347
two component system sensor kinase;
277-732 2.34e-69

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 245.71  E-value: 2.34e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 277 ERASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPV 356
Cdd:PRK15347 392 EQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEET 471
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 357 DFTSfMADLENLS-GLQAQQKG--LRFVLEPTLPLphKVITDGTRLRQILWNLISNAVKFTQQGQVTVRARYdQGDMLHF 433
Cdd:PRK15347 472 ALLP-LLDQAMLTiQGPAQSKSltLRTFVGAHVPL--YLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVKR-HEQQLCF 547
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 434 EVEDSGIGIPQDEQDKIFAMYYQVKDSNGgkpatGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFT----LTVHAP--- 506
Cdd:PRK15347 548 TVEDTGCGIDIQQQQQIFTPFYQADTHSQ-----GTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSlvlpLNEYAPpep 622
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 507 --------------------------------------------AVAEEI---EDAFEDDDMPLP--ALNVLLVEDIELN 537
Cdd:PRK15347 623 lkgelsaplalhrqlsawgitcqpghqnpalldpelaylpgrlyDLLQQIiqgAPNEPVINLPLQpwQLQILLVDDVETN 702
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 538 V-IVARsVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLdisrELTQKYaREDLP------PLVALTANV 610
Cdd:PRK15347 703 RdIIGM-MLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGL----ETTQLW-RDDPNnldpdcMIVALTANA 776
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 611 LKDKKEYL-DAGMDDVLSKPLSVPALTAMIKKYWDTrneeestvtseessksQALLDIPMLEQyLELVGPKLITDGLAVF 689
Cdd:PRK15347 777 APEEIHRCkKAGMNHYLTKPVTLAQLARALELAAEY----------------QLLRGIELSPQ-DSSCSPLLDTDDMALN 839
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 489115238 690 EKM---MPGYLSVLESNLTARDKkgVVEEGHKIKGAAGSVGLRHLQ 732
Cdd:PRK15347 840 SKLyqsLLLLLAQIEQAVENQEV--LSQLLHTLKGCAGQAGLTELQ 883
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
268-503 3.41e-66

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 219.39  E-value: 3.41e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 268 ERKRYQDALERASRDKTTFISTISHELRTPLNGIVGLSRILLD--TDLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKME 345
Cdd:COG2205    1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDeeDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 346 RRKVQLDNQPVDFTSFMADLENLSGLQAQQKGLRFVLEPTLPLPHkVITDGTRLRQILWNLISNAVKFTQQG-QVTVRAR 424
Cdd:COG2205   81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPL-VYADPELLEQVLANLLDNAIKYSPPGgTITISAR 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489115238 425 yDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKpatGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTV 503
Cdd:COG2205  160 -REGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRGEG---GTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
247-502 3.43e-61

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 211.33  E-value: 3.43e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 247 VPYYDRVGKRHGLMGFGRDITERKRyqdaLERASRDkttFISTISHELRTPLNGIVGLSRILLD--TDLTAEQEKYLKTI 324
Cdd:COG5002  136 LRLSALLLGLLLLAAVERDITELER----LEQMRRE---FVANVSHELRTPLTSIRGYLELLLDgaADDPEERREYLEII 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 325 HVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFMADLENLSGLQAQQKGLRFVLEPTLPLPhKVITDGTRLRQILW 404
Cdd:COG5002  209 LEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPL-LVLGDPDRLEQVLT 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 405 NLISNAVKFTQQG-QVTVRARyDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKpATGTGIGLAVSKRLAKNM 483
Cdd:COG5002  288 NLLDNAIKYTPEGgTITVSLR-EEDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKSRSRE-TGGTGLGLAIVKHIVEAH 365
                        250
                 ....*....|....*....
gi 489115238 484 GGDITVSSQAGKGSIFTLT 502
Cdd:COG5002  366 GGRIWVESEPGKGTTFTIT 384
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
266-775 1.68e-56

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 208.61  E-value: 1.68e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 266 ITERKRYQDALERASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKME 345
Cdd:PRK11466 427 VIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIE 506
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 346 --RRKVQLDNQPVDFTSFMADLENLSGLQAQQKGLRFVLEPTLPLPHKVITDGTRLRQILWNLISNAVKFTQQGQVTVRA 423
Cdd:PRK11466 507 agGKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRS 586
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 424 RYDQGDMLhFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGgkpatGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTV 503
Cdd:PRK11466 587 RTDGEQWL-VEVEDSGCGIDPAKLAEIFQPFVQVSGKRG-----GTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRL 660
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 504 ----HAPAVAEEIEDAFEDDDmplpaLNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGE-YDLVLLDIQ 578
Cdd:PRK11466 661 plrvATAPVPKTVNQAVRLDG-----LRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEpFAAALVDFD 735
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 579 LPDMTGLDISRELTQKYaredlPPL--VALTANVLKDKKEYLDAGM-DDVLSKPLSVPALTAMIKKYwdtrneeestvtS 655
Cdd:PRK11466 736 LPDYDGITLARQLAQQY-----PSLvlIGFSAHVIDETLRQRTSSLfRGIIPKPVPREVLGQLLAHY------------L 798
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 656 EESSKSQALLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYLSVLESNLTARDKKGVVEEGHKIKGAAGSVGLRHLQQLG 735
Cdd:PRK11466 799 QLQVNNDQPLDVSQLNEDAALMGTEKIHEWLALFKQHALPLLDEIDIARASQDSEKIKRAAHQLKSSCSSLGMRQASQAC 878
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 489115238 736 QQIQSPDLPAwednvaewiEEMKQEWQHDVAVLKAWVASV 775
Cdd:PRK11466 879 AQLEQQPLSA---------PLPHEEITRSVAALEAWLAKK 909
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
270-740 9.11e-56

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 206.62  E-value: 9.11e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 270 KRYQDAleraSRDKTTFISTISHELRTPLNGIVGLSRILLDTDLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKV 349
Cdd:PRK11107 284 KRAQEA----ARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKL 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 350 QLDNQPVDFTSFMADLENLSGLQAQQKGLRFVLEPTLPLPHKVITDGTRLRQILWNLISNAVKFTQQG----QVTVRARY 425
Cdd:PRK11107 360 VLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGnidiLVELRALS 439
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 426 DQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVkDSNGGKPATGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTV-- 503
Cdd:PRK11107 440 NTKVQLEVQIRDTGIGISERQQSQLFQAFRQA-DASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLpl 518
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238     --------------------------------------------------------------------------------
Cdd:PRK11107 519 dlnpnpiidglptdclagkrllyvepnsaaaqatldilsetplevtysptlsqlpeahydilllglpvtfrepltmlher 598
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 504 -----------------HAPAVAEE-----------------------IEDAFEDDDMPLPA-------LNVLLVEDIEL 536
Cdd:PRK11107 599 lakaksmtdflilalpcHEQVLAEQlkqdgadaclskplshtrllpalLEPCHHKQPPLLPPtdesrlpLTVMAVDDNPA 678
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 537 N--VIVArsVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQkyaredLP-----PLVALTAN 609
Cdd:PRK11107 679 NlkLIGA--LLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQ------LPhnqntPIIAVTAH 750
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 610 VLKDKKE-YLDAGMDDVLSKPLSVPALTAMIKKYWDTR---NEEESTVTSEESSKSQALLDIPM-LEQylelVGPK--LI 682
Cdd:PRK11107 751 AMAGERErLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPkftSRVVAPEPPEPVHFPNATLDWQLaLRQ----AAGKpdLA 826
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489115238 683 TDGLAVFEKMMPGYLSVLESNLTARDKKGVVEEGHKIKGAAGSVGLRHLQQLGQQIQS 740
Cdd:PRK11107 827 RDMLQMLLDFLPEVRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQ 884
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
140-760 1.84e-53

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 201.12  E-value: 1.84e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  140 IKEREEAQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMElltgksekqlvNLKPADVYspEAAEKVIETDEKV 219
Cdd:PRK09959  561 VRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFE-----------HYFTADYY--KNAMLPLENSDSP 627
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  220 FRHNVSLTYEQWLDYPDGRK---ACFEI------RKVPYYDRV----GKRHGLMGFG-RDITERKRYQDALE-------R 278
Cdd:PRK09959  628 FKDVFSNAHEVTAETKENRTiytQVFEIdngiekRCINHWHTLcnlpASDHAVYICGwQDITETRDLIHALEvernkaiN 707
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  279 ASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLTAEQE-KYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVD 357
Cdd:PRK09959  708 ATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVD 787
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  358 FTSFMADLENLSGLQAQQKGLRFVLEPTLPLPHKVITDGTRLRQILWNLISNAVKFTQQGQVTVRARY----DQGDMLHF 433
Cdd:PRK09959  788 IPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLghidDNHAVIKM 867
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  434 EVEDSGIGIPQDEQDKIFAMYYQvkdSNGGKPATGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTVHAPAVAE-EI 512
Cdd:PRK09959  868 TIMDSGSGLSQEEQQQLFKRYSQ---TSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQvAT 944
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  513 EDAFEDDDMPLP-ALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISREL 591
Cdd:PRK09959  945 VEAKAEQPITLPeKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKL 1024
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  592 TQKYARedlPPLVALTANVLKDKKEY-LDAGMDDVLSKPLSVPALTAMIKKYWDTRNEE-ESTVTSEESSKSQALLDIPM 669
Cdd:PRK09959 1025 REQNSS---LPIWGLTANAQANEREKgLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIApQYRHLDIEALKNNTANDLQL 1101
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  670 LEQYLELVGPKLITDglavfekmMPGYLSVLEsnltARDKKGVVEEGHKIKGAAGSVGLRHLQQLGQQIQ--------SP 741
Cdd:PRK09959 1102 MQEILMTFQHETHKD--------LPAAFHALE----AGDNRTFHQCIHRIHGAANILNLQKLINISHQLEitpvsddsKP 1169
                         650
                  ....*....|....*....
gi 489115238  742 DLPAWEDNVAEWIEEMKQE 760
Cdd:PRK09959 1170 EILQLLNSVKEHIAELDQE 1188
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
64-502 4.88e-52

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


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 188.64  E-value: 4.88e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  64 LITPWAVYFLSVVVEQLEESRQRlsrlVQKLEEMRERD-LKLNVQLK-DNIAQLNQEIVErekaeaerqetFEQLKVEIK 141
Cdd:COG5809   63 FLHPDDEKELREILKLLKEGESR----DELEFELRHKNgKRLEFSSKlSPIFDQNGDIEG-----------MLAISRDIT 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 142 EREEAQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETDEKVFR 221
Cdd:COG5809  128 ERKRMEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLK 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 222 HNVSLTYEQWLDYPDGRKACFEIRKVPYyDRVGKRHGLMGFGRDITERKRYQDALERAsrDKTTFIS----TISHELRTP 297
Cdd:COG5809  208 DGGIAQGEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVIIFRDITERKKLEELLRKS--EKLSVVGelaaGIAHEIRNP 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 298 LNGIVGLSRILLDTDLTaEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQldnqPVDFTSFMADLENLSGLQAQQKG 377
Cdd:COG5809  285 LTSLKGFIQLLKDTIDE-EQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYE----PKDLNTLIEEVIPLLQPQALLKN 359
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 378 LRFVLEPTLPLPHkVITDGTRLRQILWNLISNAVKFT-QQGQVTVRARYDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQ 456
Cdd:COG5809  360 VQIELELEDDIPD-ILGDENQLKQVFINLLKNAIEAMpEGGNITIETKAEDDDKVVISVTDEGCGIPEERLKKLGEPFYT 438
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 489115238 457 VKDsnggkpaTGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLT 502
Cdd:COG5809  439 TKE-------KGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSIT 477
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
149-501 5.49e-49

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 176.58  E-value: 5.49e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 149 QLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSP-----EAAEKVIETDEKVFRHN 223
Cdd:COG3852    1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEdsplrELLERALAEGQPVTERE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 224 VSLTYeqwldyPDGRKACFEIRKVPYYDRVGKRhGLMGFGRDITERKRYQDALERASRDKT--TFISTISHELRTPLNGI 301
Cdd:COG3852   81 VTLRR------KDGEERPVDVSVSPLRDAEGEG-GVLLVLRDITERKRLERELRRAEKLAAvgELAAGLAHEIRNPLTGI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 302 VGLSRILLDTDLTAEQEKYLKTIHVSAVTLGNIfndiidMDKMER--RKVQLDNQPVDFTSFMADLENLSGLQAQqKGLR 379
Cdd:COG3852  154 RGAAQLLERELPDDELREYTQLIIEEADRLNNL------VDRLLSfsRPRPPEREPVNLHEVLERVLELLRAEAP-KNIR 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 380 FVLE--PTLPLphkVITDGTRLRQILWNLISNAVK-FTQQGQVTVRARYD---------QGDMLHFEVEDSGIGIPQDEQ 447
Cdd:COG3852  227 IVRDydPSLPE---VLGDPDQLIQVLLNLVRNAAEaMPEGGTITIRTRVErqvtlgglrPRLYVRIEVIDNGPGIPEEIL 303
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489115238 448 DKIFamyyqvkdsnggKP-----ATGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTL 501
Cdd:COG3852  304 DRIF------------EPffttkEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRI 350
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
41-502 7.57e-49

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 180.37  E-value: 7.57e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  41 AVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQLEESRQRLSRLVQKLEEMRERDLKLNVQLKDNIAQLNQEIV 120
Cdd:COG4251   33 ALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELALVLLALLLVLLLLLALLLLLAL 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 121 EREKAEAERQETFEQLKVEIKEREEAQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKP 200
Cdd:COG4251  113 LLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLL 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 201 ADVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKACFEIRKVPYYDRVGKRHGLMGFGRDI-------TERKRYQ 273
Cdd:COG4251  193 LLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRleleeleEELEERT 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 274 DALERASRDKTTFISTISHELRTPLNGIVGLSRILLD---TDLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRkvQ 350
Cdd:COG4251  273 AELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEdygDKLDEEGREYLERIRDAAERMQALIDDLLAYSRVGRQ--E 350
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 351 LDNQPVDFTSFMADLENLSGLQAQQKGLRFVLEPtlpLPHkVITDGTRLRQILWNLISNAVKFT---QQGQVTVRARyDQ 427
Cdd:COG4251  351 LEFEPVDLNELLEEVLEDLEPRIEERGAEIEVGP---LPT-VRGDPTLLRQVFQNLISNAIKYSrpgEPPRIEIGAE-RE 425
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489115238 428 GDMLHFEVEDSGIGIPQDEQDKIFAMYYQVkdsNGGKPATGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLT 502
Cdd:COG4251  426 GGEWVFSVRDNGIGIDPEYAEKIFEIFQRL---HSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFT 497
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
399-504 4.60e-47

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 162.66  E-value: 4.60e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFTQQGQVTVRARYD----QGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVkDSNGGKPATGTGIGLA 474
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEeeeeDGVQLRFSVEDTGIGIPEEQQARLFEPFSQA-DSSTTRKYGGTGLGLA 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 489115238 475 VSKRLAKNMGGDITVSSQAGKGSIFTLTVH 504
Cdd:cd16922   80 ISKKLVELMGGDISVESEPGQGSTFTFTLP 109
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
59-502 4.18e-45

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: 167.45  E-value: 4.18e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  59 IFFGLLITPWAVYFLSVVVEQLeesRQRLSRLVQKLEEMRERDL--KLNVQLKDNIAQLNQEiverekaeaerqetFEQL 136
Cdd:COG5000   12 LLIALLLLLLALWLALLLARRL---TRPLRRLAEATRAVAAGDLsvRLPVTGDDEIGELARA--------------FNRM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 137 KVEIKEreeAQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIEtd 216
Cdd:COG5000   75 TDQLKE---QREELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLR-- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 217 eKVFRHNVSLTYEqwldYPDGRKACFEIRKVPYYDRvgkrhGLMGFGRDITErkryqdaLERASRDKT--TFISTISHEL 294
Cdd:COG5000  150 -EALERGWQEEIE----LTRDGRRTLLVRASPLRDD-----GYVIVFDDITE-------LLRAERLAAwgELARRIAHEI 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 295 RTPLNGIVG----LSRILLD--TDLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMErrkvQLDNQPVDFTSFMADLENL 368
Cdd:COG5000  213 KNPLTPIQLsaerLRRKLADklEEDREDLERALDTIIRQVDRLKRIVDEFLDFARLP----EPQLEPVDLNELLREVLAL 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 369 SGLQAQQKGLRFVLEPTLPLPHkVITDGTRLRQILWNLISNAVKFT-QQGQVTVRARYDqGDMLHFEVEDSGIGIPQDEQ 447
Cdd:COG5000  289 YEPALKEKDIRLELDLDPDLPE-VLADRDQLEQVLINLLKNAIEAIeEGGEIEVSTRRE-DGRVRIEVSDNGPGIPEEVL 366
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489115238 448 DKIFAMYYQVKdsnggkpATGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLT 502
Cdd:COG5000  367 ERIFEPFFTTK-------PKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIR 414
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
150-500 1.63e-40

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems]


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 151.98  E-value: 1.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  150 LEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTG-----KSEKQLVNLkpadVYSPEAAEKVietDEKVFRHNV 224
Cdd:TIGR02966   1 LSALLSRFRAAAQALPDAVVVLDEEGQIEWCNPAAERLLGlrwpdDLGQRITNL----IRHPEFVEYL---AAGRFSEPL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  225 SLTYeqwldyPDGRKACFEIRKVPYydrvGKRHGLMGFgRDITERKRyqdaLERASRDkttFISTISHELRTPLNGIVGL 304
Cdd:TIGR02966  74 ELPS------PINSERVLEIRIAPY----GEEQKLLVA-RDVTRLRR----LEQMRRD---FVANVSHELRTPLTVLRGY 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  305 SRILLDTDLT--AEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFMADLENLSGLQAQQKGLRFVL 382
Cdd:TIGR02966 136 LETLADGPDEdpEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEALSQGKNHQITF 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  383 EPTLPLphKVITDGTRLRQILWNLISNAVKFTQ-QGQVTVRARYDQGdMLHFEVEDSGIGIPQDEQDKIFAMYYQVkDSN 461
Cdd:TIGR02966 216 EIDGGV--DVLGDEDELRSAFSNLVSNAIKYTPeGGTITVRWRRDGG-GAEFSVTDTGIGIAPEHLPRLTERFYRV-DKS 291
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 489115238  462 GGKPATGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFT 500
Cdd:TIGR02966 292 RSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFS 330
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
275-642 4.19e-40

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 159.37  E-value: 4.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 275 ALERASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRkvQLDNQ 354
Cdd:PRK10841 439 AAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESE--QLKIE 516
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 355 PVDFtsfmADLENLSGLQA--------QQKGLRFVLEPTLPLphKVITDGTRLRQILWNLISNAVKFTQQGQVTVRARYD 426
Cdd:PRK10841 517 PREF----SPREVINHITAnylplvvkKRLGLYCFIEPDVPV--ALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRVD 590
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 427 qGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVkDSNGGKPATGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLT---- 502
Cdd:PRK10841 591 -GDYLSFRVRDTGVGIPAKEVVRLFDPFFQV-GTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRiply 668
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238     --------------------------------------------------------------------------------
Cdd:PRK10841 669 gaqypqkkgveglqgkrcwlavrnasleqfletllqrsgiqvqryegqeptpedvlitddpvqkkwqgravitfcrrhig 748
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 503 ----------VHAPAVAEE----------IEDAFEDDDMPLPA----------LNVLLVEDIELNVIVARSVLEKLGNSV 552
Cdd:PRK10841 749 ipleiapgewVHSTATPHElpallariyrIELESDDSANALPStdkavsdnddMMILVVDDHPINRRLLADQLGSLGYQC 828
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 553 DVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLdisrELTQkYARED--LPPLVALTANVLKDKKEY-LDAGMDDVLSKP 629
Cdd:PRK10841 829 KTANDGVDALNVLSKNHIDIVLTDVNMPNMDGY----RLTQ-RLRQLglTLPVIGVTANALAEEKQRcLEAGMDSCLSKP 903
                        490
                 ....*....|...
gi 489115238 630 LSVPALTAMIKKY 642
Cdd:PRK10841 904 VTLDVLKQTLTVY 916
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
528-639 1.12e-36

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 133.36  E-value: 1.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLPPLVALT 607
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRRTPIIALT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489115238 608 ANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMI 639
Cdd:cd17546   81 ANALEeDREKCLEAGMDDYLSKPVKLDQLKEVL 113
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
394-504 3.44e-35

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 129.31  E-value: 3.44e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238   394 TDGTRLRQILWNLISNAVKFT-QQGQVTVRARyDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKPatGTGIG 472
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLE-RDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIG--GTGLG 77
                           90       100       110
                   ....*....|....*....|....*....|..
gi 489115238   473 LAVSKRLAKNMGGDITVSSQAGKGSIFTLTVH 504
Cdd:smart00387  78 LSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
264-502 4.26e-34

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 134.16  E-value: 4.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 264 RDITERKRYQDALERASRDKT--TFISTISHELRTPLNGIVG----LSRILLDTDLTAEQEKYLKTIHVSAVTLGNI--- 334
Cdd:COG4191  121 RAEEELRELQEQLVQSEKLAAlgELAAGIAHEINNPLAAILGnaelLRRRLEDEPDPEELREALERILEGAERAAEIvrs 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 335 FNDIIDMDKMERRKVQLdNQPVDftsfmaDLENLSGLQAQQKGLRFVLEPTLPLPhKVITDGTRLRQILWNLISN---AV 411
Cdd:COG4191  201 LRAFSRRDEEEREPVDL-NELID------EALELLRPRLKARGIEVELDLPPDLP-PVLGDPGQLEQVLLNLLINaidAM 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 412 KFTQQGQVTVRARYDqGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDsnGGKpatGTGIGLAVSKRLAKNMGGDITVSS 491
Cdd:COG4191  273 EEGEGGRITISTRRE-GDYVVISVRDNGPGIPPEVLERIFEPFFTTKP--VGK---GTGLGLSISYGIVEKHGGRIEVES 346
                        250
                 ....*....|.
gi 489115238 492 QAGKGSIFTLT 502
Cdd:COG4191  347 EPGGGTTFTIT 357
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
394-506 2.14e-32

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: 121.32  E-value: 2.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  394 TDGTRLRQILWNLISNAVKFT-QQGQVTVRARydQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGkpatGTGIG 472
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAaKAGEITVTLS--EGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGG----GTGLG 74
                          90       100       110
                  ....*....|....*....|....*....|....
gi 489115238  473 LAVSKRLAKNMGGDITVSSQAGKGSIFTLTVHAP 506
Cdd:pfam02518  75 LSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
140-502 3.00e-32

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: 131.39  E-value: 3.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 140 IKEREEAQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETDEKV 219
Cdd:COG5805  142 ITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIESI 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 220 FRHNVSLTYE-QWLDYpDGRKACFEIRKVPYYDRVGKRHGLMGFGRDITERKRyQDALERASrDKTTFI----STISHEL 294
Cdd:COG5805  222 TEVWQEFIIErEIITK-DGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKE-AEELMARS-EKLSIAgqlaAGIAHEI 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 295 RTPLNGIVGLSRILLDTdlTAEQEKYLKtIHVSavTLGNIfNDIIDMDKMERRKVQLDNQPVDFTSFMADLENLSGLQAQ 374
Cdd:COG5805  299 RNPLTSIKGFLQLLQPG--IEDKEEYFD-IMLS--ELDRI-ESIISEFLALAKPQAVNKEKENINELIQDVVTLLETEAI 372
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 375 QKGLRFVLEPTLPLPhKVITDGTRLRQILWNLISNAVK-FTQQGQVTVRARYDQGDmLHFEVEDSGIGIPQDEQDKIFAM 453
Cdd:COG5805  373 LHNIQIRLELLDEDP-FIYCDENQIKQVFINLIKNAIEaMPNGGTITIHTEEEDNS-VIIRVIDEGIGIPEERLKKLGEP 450
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 489115238 454 YYQVKDSnggkpatGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLT 502
Cdd:COG5805  451 FFTTKEK-------GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTIT 492
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
399-502 4.44e-32

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 120.02  E-value: 4.44e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFT-QQGQVTVRARYDqGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKpatGTGIGLAVSK 477
Cdd:cd00075    1 LEQVLSNLLDNALKYSpPGGTIEISLRQE-GDGVVLEVEDNGPGIPEEDLERIFERFYRGDKSREGG---GTGLGLAIVR 76
                         90       100
                 ....*....|....*....|....*
gi 489115238 478 RLAKNMGGDITVSSQAGKGSIFTLT 502
Cdd:cd00075   77 RIVEAHGGRITVESEPGGGTTFTVT 101
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
521-646 8.40e-31

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 117.26  E-value: 8.40e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 521 MPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDL 600
Cdd:COG0784    1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489115238 601 pPLVALTANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIKKYWDTR 646
Cdd:COG0784   81 -PIIALTAYADEeDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
264-501 2.62e-30

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 127.01  E-value: 2.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 264 RDITERKRYQDALERASRDKT--TFISTISHELRTPLNGIVGLSRILLDTDLTAEQEKYLKTIHVSAVTLGNIFNDIIDM 341
Cdd:PRK11360 369 SDLTERKRLQRRVARQERLAAlgELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEF 448
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 342 DKmeRRKVQldNQPVDFTSFMADLENLSGLQAQQKGLRFV--LEPTLPLphkVITDGTRLRQILWNLISNAVK-FTQQGQ 418
Cdd:PRK11360 449 SR--PRESQ--WQPVSLNALVEEVLQLFQTAGVQARVDFEteLDNELPP---IWADPELLKQVLLNILINAVQaISARGK 521
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 419 VTVRARYDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKdsnggkpATGTGIGLAVSKRLAKNMGGDITVSSQAGKGSI 498
Cdd:PRK11360 522 IRIRTWQYSDGQVAVSIEDNGCGIDPELLKKIFDPFFTTK-------AKGTGLGLALSQRIINAHGGDIEVESEPGVGTT 594

                 ...
gi 489115238 499 FTL 501
Cdd:PRK11360 595 FTL 597
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
265-502 9.94e-28

cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in Staphylococcus aureus (sp|Q2G2U4.1|WALK_STAA8). A shorter version, as found in Streptococcus pneumoniae, called WalK(Spn) or VicK, is not included. WalK is part of a two-component system and works with partner protein WalR.


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 118.70  E-value: 9.94e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 265 DITErkryQDALERASRDkttFISTISHELRTPLNGIVGLSRILLDTDLTAEQ--EKYLKtihvsaVTLGN------IFN 336
Cdd:NF033092 361 DVTE----QEKIEQERRE---FVANVSHELRTPLTTMRSYLEALADGAWKDPElaPRFLG------VTQNEtermirLVN 427
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 337 DIIDMDKMERRKVQLDNQPVDFTSFMADLENLSGLQAQQKGLRFVLEptlpLPHKVIT---DGTRLRQILWNLISNAVKF 413
Cdd:NF033092 428 DLLQLSRMDSKDYKLNKEWVNFNEFFNYIIDRFEMILKNKNITFKRE----FPKRDLWveiDTDKITQVLDNIISNAIKY 503
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 414 TQQ-GQVTVRARyDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVkDsnggKPAT----GTGIGLAVSKRLAKNMGGDIT 488
Cdd:NF033092 504 SPEgGTITFRLL-ETHNRIIISISDQGLGIPKKDLDKIFDRFYRV-D----KARSrkmgGTGLGLAIAKEVVEAHGGRIW 577
                        250
                 ....*....|....
gi 489115238 489 VSSQAGKGSIFTLT 502
Cdd:NF033092 578 AESEEGKGTTIYFT 591
HKR_ArcB_TM pfam18415
Histidine kinase receptor ArcB trans-membrane domain; Histidine kinase receptors (HKRs) are ...
15-89 1.40e-26

Histidine kinase receptor ArcB trans-membrane domain; Histidine kinase receptors (HKRs) are part of a two-component system, in which an HKR in the bacterial inner membrane transmits a signal to a response regulator located in the cytoplasm. This is a trans-membrane domain (TM) found in ArcB (class 2, aerobic respiratory control sensor). ArcB has two TM helices connected by a short periplasmic loop. TM domain structures suggests a loose helical packing which provides an inherent flexibility in the TM domains and that this is perhaps essential to the mechanism of signal transduction across the membrane.


Pssm-ID: 436484  Cd Length: 75  Bit Score: 103.38  E-value: 1.40e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489115238   15 MMKLGLVRFSLLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQLEESRQRLSR 89
Cdd:pfam18415   1 VIRLGTVRFSLLLAILLILFALLIQILLSLLLTGEVHWEDLLRSIFFGLLSAPWVLYFFSVVVEQLERSRQRLSK 75
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
528-640 5.79e-25

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 99.92  E-value: 5.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQkyaREDLPPLVALT 607
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRR---RDPTTPVIILT 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 489115238  608 ANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:pfam00072  78 AHGdEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
525-639 1.35e-23

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 98.44  E-value: 1.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 525 ALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLpPLV 604
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADI-PII 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 605 ALTANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMI 639
Cdd:COG3706   80 FLTALDDEeDRARALEAGADDYLTKPFDPEELLARV 115
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
528-640 2.83e-23

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 98.49  E-value: 2.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELtqkyaREDLP--PLVA 605
Cdd:COG0745    4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRL-----RARPSdiPIIM 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 606 LTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:COG0745   79 LTArDDEEDRVRGLEAGADDYLTKPFDPEELLARIR 114
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
254-503 7.61e-23

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 101.46  E-value: 7.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 254 GKRHGLMGFGRDITERKRYQDALERAsRDKTTFISTISHELRTPLNGIVGLsrilLDTDLTAEQEKYLKTIhvsavtlgn 333
Cdd:COG3290  161 GRVVGAVATFRDRTELERLEEELEGV-KELAEALRAQRHDFRNHLHTISGL----LQLGEYDEALEYIDEI--------- 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 334 ifndIIDMDKMERRKVQLDNQPVdftsfmadlenLSGL------QAQQKGLRFVLEPTLPLPHKVITDGTrLRQILWNLI 407
Cdd:COG3290  227 ----SEELQELIDSLLSRIGNPV-----------LAALllgkaaRARERGIDLTIDIDSDLPDLPLSDTD-LVTILGNLL 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 408 SNAV-----KFTQQGQVTVRARYDqGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGgkpatgTGIGLAVSKRLAKN 482
Cdd:COG3290  291 DNAIeavekLPEEERRVELSIRDD-GDELVIEVEDSGPGIPEELLEKIFERGFSTKLGEG------RGLGLALVKQIVEK 363
                        250       260
                 ....*....|....*....|.
gi 489115238 483 MGGDITVSSQAGKGSIFTLTV 503
Cdd:COG3290  364 YGGTIEVESEEGEGTVFTVRL 384
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
289-507 9.84e-23

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 102.23  E-value: 9.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 289 TISHELRTPLNGIVGLSRiLLDTDLTAEQ-EKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFMADLEN 367
Cdd:PRK11100 262 TLTHELKSPLAAIRGAAE-LLQEDPPPEDrARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVE 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 368 LSGLQAQQKGLRFVLEPTlplPHKVITDGTRLRQILWNLISNAVKFT-QQGQVTVRARYDQGDmLHFEVEDSGIGIPQDE 446
Cdd:PRK11100 341 AREAQAAAKGITLRLRPD---DARVLGDPFLLRQALGNLLDNAIDFSpEGGTITLSAEVDGEQ-VALSVEDQGPGIPDYA 416
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489115238 447 QDKIFAMYYQVKDSNGGKpaTGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTVHAPA 507
Cdd:PRK11100 417 LPRIFERFYSLPRPANGR--KSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPRHF 475
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
527-641 3.44e-22

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 92.22  E-value: 3.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLpPLVAL 606
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDI-PVIAL 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 607 TANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIKK 641
Cdd:cd17548   80 TAYAMKgDREKILEAGCDGYISKPIDTREFLETVAK 115
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
269-501 3.85e-22

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 100.25  E-value: 3.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 269 RKRYQDA---LERASRDKT------TFISTISHELRTPLNGIVGLSRILLDTDLTAEQEKYLKTIHVSAVT-LGNIFNDI 338
Cdd:PRK10364 214 YRRYLRSrqlLQDEMKRKEklvalgHLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADrLNRVVSEL 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 339 IDMDKMERrkvqLDNQPVDFTSFMADLENLSGLQAQQKG--LRFVLEPTLPLphkVITDGTRLRQILWNLISNAVK-FTQ 415
Cdd:PRK10364 294 LELVKPTH----LALQAVDLNDLINHSLQLVSQDANSREiqLRFTANDTLPE---IQADPDRLTQVLLNLYLNAIQaIGQ 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 416 QGQVTVRARyDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKdsnggkpATGTGIGLAVSKRLAKNMGGDITVSSQAGK 495
Cdd:PRK10364 367 HGVISVTAS-ESGAGVKISVTDSGKGIAADQLEAIFTPYFTTK-------AEGTGLGLAVVHNIVEQHGGTIQVASQEGK 438

                 ....*.
gi 489115238 496 GSIFTL 501
Cdd:PRK10364 439 GATFTL 444
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
524-667 7.39e-22

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 94.85  E-value: 7.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 524 PALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLpPL 603
Cdd:COG3437    5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDI-PV 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489115238 604 VALTANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIKKYWDTRNEEESTVTSEESSKSQALL-DI 667
Cdd:COG3437   84 IFLTALAdPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKLAAPLhDI 149
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
1-774 1.31e-21

HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 100.51  E-value: 1.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238   1 MKQIRMLAQYYVDLMMKLGLVRFSLLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
Cdd:COG2198  104 LLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLLLLALLLALLLLVLLVLLLLLLL 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  81 EESRQRLSRLVQKLEEMRERDLKLNVQLKDNIAQLNQEIVEREKAEAERQETFEQLKVEIKEREEAQIQLEQQSSFLRSF 160
Cdd:COG2198  184 LLLLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAELAALLLLLLLLLLLLILLLLLLL 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 161 LDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKA 240
Cdd:COG2198  264 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 241 CFEIRKVPYYDRVGKRHGLMGFGRDITERKRYQDALERASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLTAEQEKY 320
Cdd:COG2198  344 LLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSLLLLLLLLLLLLLL 423
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 321 LKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFMADLENLSGLQAQQKGLRFVLEPTLPLPHKVITDGTRLR 400
Cdd:COG2198  424 LLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 503
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 401 QILWNLISNAVKFTQQGQVTVRARYDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKPATGTGIGLAVSKRLA 480
Cdd:COG2198  504 LLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALLLGLGLLLGLLLGGLLLLLLLLL 583
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 481 KNMGGDITVSSQAGKGSIFTLTVHAPAVAEEIEDAFEDDDMPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKA 560
Cdd:COG2198  584 LLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAVLLAAAAAAA 663
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 561 ALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAmik 640
Cdd:COG2198  664 ALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLAALLLLLLLLLLLLLLL--- 740
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 641 kyWDTRNEEESTVTSEESSKSQALLDIPMLEQYLElvGPKLITDGLAVFEKMMPGYLSVLESNLTARDKKGVVEEGHKIK 720
Cdd:COG2198  741 --LLLLLAAAAAAAASPAAPALPVLDLEALRRLGG--DPELLRELLELFLEELPELLAELRQALAAGDLEALARLAHKLK 816
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489115238 721 GAAGSVGLRHLQQLGQQIQSPDLPAWEDNVAEWIEEMKQEWQHDVAVLKAWVAS 774
Cdd:COG2198  817 GSAGNLGAPRLAELAAELEQAARAGDLEEAEELLAELEAELERVLAALEALLAE 870
PRK13557 PRK13557
histidine kinase; Provisional
347-629 3.52e-20

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 95.12  E-value: 3.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 347 RKVQLDNQPVDFTSFMADLENLSGlqaQQKG----LRFVLEPTLPlPHKVitDGTRLRQILWNLISNAVK-FTQQGQVTV 421
Cdd:PRK13557 228 RKQRLEGRVLNLNGLVSGMGELAE---RTLGdavtIETDLAPDLW-NCRI--DPTQAEVALLNVLINARDaMPEGGRVTI 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 422 RAR-----------YDQ---GDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSngGKpatGTGIGLAVSKRLAKNMGGDI 487
Cdd:PRK13557 302 RTRnveiededlamYHGlppGRYVSIAVTDTGSGMPPEILARVMDPFFTTKEE--GK---GTGLGLSMVYGFAKQSGGAV 376
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 488 TVSSQAGKGSifTLTVHAPAVAEEIEDAFEDDDMPLP---ALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEM 564
Cdd:PRK13557 377 RIYSEVGEGT--TVRLYFPASDQAENPEQEPKARAIDrggTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEI 454
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 565 FTPG-EYDLVLLDIQLP-DMTGLDISREltqkyAREDLPPL-VALTANVLKDKKEYLDAGMD--DVLSKP 629
Cdd:PRK13557 455 LDSHpEVDLLFTDLIMPgGMNGVMLARE-----ARRRQPKIkVLLTTGYAEASIERTDAGGSefDILNKP 519
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
243-502 9.01e-20

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 92.77  E-value: 9.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 243 EIRKVPYYDRvgkrHGLMgFGRDITERKRyqdaLERASRDkttFISTISHELRTPLNGIVGLSRILLDTDLT-AEQEKYL 321
Cdd:PRK11006 176 EIRVMPYTEG----QLLM-VARDVTQMHQ----LEGARRN---FFANVSHELRTPLTVLQGYLEMMQDQPLEgALREKAL 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 322 KTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFMADLE----NLSglQAQQKgLRFVLEPTLplphKVITDGT 397
Cdd:PRK11006 244 HTMREQTQRMEGLVKQLLTLSKIEAAPTIDLNEKVDVPMMLRVLEreaqTLS--QGKHT-ITFEVDNSL----KVFGNED 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 398 RLRQILWNLISNAVKFTQQG-QVTVR-ARYDQGdmLHFEVEDSGIGIPQDEQDKIFAMYYQVkDSNGGKPATGTGIGLAV 475
Cdd:PRK11006 317 QLRSAISNLVYNAVNHTPEGtHITVRwQRVPQG--AEFSVEDNGPGIAPEHIPRLTERFYRV-DKARSRQTGGSGLGLAI 393
                        250       260
                 ....*....|....*....|....*..
gi 489115238 476 SKRLAKNMGGDITVSSQAGKGSIFTLT 502
Cdd:PRK11006 394 VKHALSHHDSRLEIESEVGKGTRFSFV 420
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-502 1.00e-19

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 84.69  E-value: 1.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFTQQG---QVTVRARyDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVK-DSNGGkpatGTGIGLA 474
Cdd:cd16921    1 LGQVLTNLLGNAIKFRRPRrppRIEVGAE-DVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHsREEYE----GTGVGLA 75
                         90       100
                 ....*....|....*....|....*...
gi 489115238 475 VSKRLAKNMGGDITVSSQAGKGSIFTLT 502
Cdd:cd16921   76 IVRKIIERHGGRIWLESEPGEGTTFYFT 103
PAS COG2202
PAS domain [Signal transduction mechanisms];
145-281 1.02e-19

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 89.70  E-value: 1.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 145 EAQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETDEKVFRHNV 224
Cdd:COG2202    1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489115238 225 SLTYEQWLDYPDGRKACFEIRKVPYYDRVGKRHGLMGFGRDITERKRYQDALERASR 281
Cdd:COG2202   81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEE 137
PRK09303 PRK09303
histidine kinase;
287-503 5.12e-19

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 89.63  E-value: 5.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 287 ISTISHELRTPLNGIV------GLSRILLDTDLTAE-QEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFT 359
Cdd:PRK09303 155 LAMLAHDLRTPLTAASlaletlELGQIDEDTELKPAlIEQLQDQARRQLEEIERLITDLLEVGRTRWEALRFNPQKLDLG 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 360 SFMAD-LENLSgLQAQQKGLRFVLEPTLPLPhKVITDGTRLRQILWNLISNAVKFTQ-QGQVTVrarydqgDMLH----- 432
Cdd:PRK09303 235 SLCQEvILELE-KRWLAKSLEIQTDIPSDLP-SVYADQERIRQVLLNLLDNAIKYTPeGGTITL-------SMLHrttqk 305
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489115238 433 --FEVEDSGIGIPQDEQDKIFAMYYQVKDSNGgkpATGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTV 503
Cdd:PRK09303 306 vqVSICDTGPGIPEEEQERIFEDRVRLPRDEG---TEGYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTL 375
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-501 6.07e-19

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: 82.47  E-value: 6.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVK-FTQQGQVTVRArYDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKdsnggKPATGTGIGLAVSK 477
Cdd:cd16943    4 LNQVLLNLLVNAAQaMEGRGRITIRT-WAHVDQVLIEVEDTGSGIDPEILGRIFDPFFTTK-----PVGEGTGLGLSLSY 77
                         90       100
                 ....*....|....*....|....
gi 489115238 478 RLAKNMGGDITVSSQAGKGSIFTL 501
Cdd:cd16943   78 RIIQKHGGTIRVASVPGGGTRFTI 101
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
270-503 6.64e-19

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 90.52  E-value: 6.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  270 KRYQDALERASRdkttFISTISHELRTPLNGIVGLSRILLDTDLTaeQEKYLKTIHVSAVT---LGNIFNDIIDMDKMER 346
Cdd:TIGR01386 232 GRLEDAFQRLSQ----FSADLAHELRTPLTNLLGQTQVALSQPRT--GEEYREVLESNLEElerLSRMVSDMLFLARADN 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  347 RKVQLDNQPVDFTSFMADLENLSGLQAQQKGLRFVLEPTLPLPhkviTDGTRLRQILWNLISNAVKFTQQGQ-VTVRARy 425
Cdd:TIGR01386 306 GQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEGLVR----GDPQMFRRAISNLLSNALRHTPDGGtITVRIE- 380
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489115238  426 DQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKPAtGTGIGLAVSKRLAKNMGGDITVSSQAGKgSIFTLTV 503
Cdd:TIGR01386 381 RRSDEVRVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGE-GTGLGLAIVRSIMEAHGGRASAESPDGK-TRFILRF 456
PRK10490 PRK10490
sensor protein KdpD; Provisional
267-514 9.42e-19

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 91.25  E-value: 9.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 267 TERKRYQDALerasrdkttfISTISHELRTPLNGIVGLSRILLdTDLTAEQEKYlkTIHVSAV---TLGNI--FNDIIDM 341
Cdd:PRK10490 658 SEREQLRNAL----------LAALSHDLRTPLTVLFGQAEILT-LDLASEGSPH--ARQASEIrqqVLNTTrlVNNLLDM 724
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 342 DKMERRKVQLDNQpvdftsFMAdLENLSG--LQAQQKGL-RFVLEPTLPLPHKVI-TDGTRLRQILWNLISNAVKFT-QQ 416
Cdd:PRK10490 725 ARIQSGGFNLRKE------WLT-LEEVVGsaLQMLEPGLsGHPINLSLPEPLTLIhVDGPLFERVLINLLENAVKYAgAQ 797
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 417 GQVTVRARYdQGDMLHFEVEDSGIGIPQDEQDKIFAmyyqvKDSNGGKPAT--GTGIGLAVSKRLAKNMGGDITVSSQAG 494
Cdd:PRK10490 798 AEIGIDAHV-EGERLQLDVWDNGPGIPPGQEQLIFD-----KFARGNKESAipGVGLGLAICRAIVEVHGGTIWAENRPE 871
                        250       260
                 ....*....|....*....|...
gi 489115238 495 KGSIFTLTV---HAPAVAEEIED 514
Cdd:PRK10490 872 GGACFRVTLpleTPPELEEFHED 894
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
526-635 1.16e-18

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 82.45  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 526 LNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGE--YDLVLLDIQLPDMTGLDISRELTQKYAREDLPPL 603
Cdd:cd19933    1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEhsFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPLI 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489115238 604 VALTANVLKDKKEY-LDAGMDDVLSKPLSVPAL 635
Cdd:cd19933   81 VALTANTDDSTREKcLSLGMNGVITKPVSLHAL 113
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
529-640 2.59e-18

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 81.11  E-value: 2.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 529 LLVED-IELNVIVARSvLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKyaREDLPPLVaLT 607
Cdd:cd17625    1 LVVEDeKDLSEAITKH-LKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREE--GIETPVLL-LT 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489115238 608 A-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17625   77 AlDAVEDRVKGLDLGADDYLPKPFSLAELLARIR 110
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-503 2.71e-18

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA).


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 81.41  E-value: 2.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFTQQGQVTVRARYDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGgKPATGTGIGLAVSKR 478
Cdd:cd16947   21 LQRILKNLISNAIKYGSDGKFLGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRN-SAKQGNGLGLTITKR 99
                         90       100
                 ....*....|....*....|....*
gi 489115238 479 LAKNMGGDITVSSQAGKGSIFTLTV 503
Cdd:cd16947  100 LAESMGGSIYVNSKPYEKTVFTVTL 124
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
528-640 2.79e-18

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 80.99  E-value: 2.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDielNVIVARSV---LEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREdlpPLV 604
Cdd:cd17624    1 ILLVED---DALLGDGLktgLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSL---PVL 74
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489115238 605 ALTAN-VLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17624   75 ILTARdGVDDRVAGLDAGADDYLVKPFALEELLARLR 111
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
156-266 9.82e-18

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 79.38  E-value: 9.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  156 FLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETDEKVFRH-NVSLTYEQWLDY 234
Cdd:pfam00989   2 DLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQgEESRGFEVSFRV 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 489115238  235 PDGRKACFEIRKVPYYDRVGKRHGLMGFGRDI 266
Cdd:pfam00989  82 PDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
526-642 1.48e-17

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 79.63  E-value: 1.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 526 LNVLLVEDIELNVIVARSVLEKLGN--SVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYARedlPPL 603
Cdd:COG4565    4 IRVLIVEDDPMVAELLRRYLERLPGfeVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPD---VDV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489115238 604 VALTANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIKKY 642
Cdd:COG4565   81 IVITAARdPETVREALRAGVVDYLIKPFTFERLREALERY 120
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
290-501 2.13e-17

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 84.66  E-value: 2.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 290 ISHELRTPLNGIVGLSRILLDTDLTAEqEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFMADLENLS 369
Cdd:NF012226 145 IAHELRTPITILQGRLQGILDGVFEPD-PALFKSLLNQVEGLSHLVEDLRTLSLVENQQLRLNYESVDLKDSIEKVLKMF 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 370 GLQAQQKGLRFVLEPTLPLphkVITDGTRLRQILWNLISNAVKFTQQGQVTVRARYDQGDMLhFEVEDSGIGIPQDEQDK 449
Cdd:NF012226 224 EDRLEQAQLTIVLNLTATP---VFCDRRRIEQVLIALIDNAIRYANAGKLKISSSVIQDDWI-LQIEDEGPGIAEEYQQD 299
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489115238 450 IFAMYYQVKDSNgGKPATGTGIGLAVSKRLAKNMGGDITVSSQAGkGSIFTL 501
Cdd:NF012226 300 LFNPFFRLEQSR-NKEFGGTGLGLAVVHAIVIAHKGSIEYSNSQG-NSVFTI 349
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
529-629 3.21e-17

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 77.45  E-value: 3.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 529 LLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELtqkyaREDLP--PLVAL 606
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRL-----REKGSdiPIIML 75
                         90       100
                 ....*....|....*....|....
gi 489115238 607 TA-NVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd17574   76 TAkDEEEDKVLGLELGADDYITKP 99
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
264-639 4.15e-17

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 85.88  E-value: 4.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 264 RDITERKRYQDALERASRDKT--TFISTISHELRTPLNGIVGLSRILLDT-DLTAEQEKYLKTIhVSAvtlGNIFNDIID 340
Cdd:PRK13837 429 RLETERDALERRLEHARRLEAvgTLASGIAHNFNNILGAILGYAEMALNKlARHSRAARYIDEI-ISA---GARARLIID 504
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 341 MDKMERRKVQLDNQPVDFTSFMADLENLsglqaqqkgLRFVLEPTLPL-------PHKVITDGTRLRQILWNLISNAVK- 412
Cdd:PRK13837 505 QILAFGRKGERNTKPFDLSELVTEIAPL---------LRVSLPPGVELdfdqdqePAVVEGNPAELQQVLMNLCSNAAQa 575
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 413 FTQQGQVTVRARYDQ--------------GDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKdsnggkpATGTGIGLAVSKR 478
Cdd:PRK13837 576 MDGAGRVDISLSRAKlrapkvlshgvlppGRYVLLRVSDTGAGIDEAVLPHIFEPFFTTR-------AGGTGLGLATVHG 648
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 479 LAKNMGGDITVSSQAGKGSIFTL---TVHAPAVAEeiEDAFEDDDMPLPA-LNVLLVEDIELNVIVARSVLEKLGNSvDV 554
Cdd:PRK13837 649 IVSAHAGYIDVQSTVGRGTRFDVylpPSSKVPVAP--QAFFGPGPLPRGRgETVLLVEPDDATLERYEEKLAALGYE-PV 725
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 555 AMTG-KAALEMFT--PGEYDLVLLDIQLPDMTGLDISRELtqkyAREDLPPLVAltANVLKDK-KEYLDAGMDDVLSKPL 630
Cdd:PRK13837 726 GFSTlAAAIAWISkgPERFDLVLVDDRLLDEEQAAAALHA----AAPTLPIILG--GNSKTMAlSPDLLASVAEILAKPI 799

                 ....*....
gi 489115238 631 SVPALTAMI 639
Cdd:PRK13837 800 SSRTLAYAL 808
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-496 7.09e-17

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain.


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 76.72  E-value: 7.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFTQqGQVTVRARYDqGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKpatGTGIGLAVSKR 478
Cdd:cd16950    1 LKRVLSNLVDNALRYGG-GWVEVSSDGE-GNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNARGTS---GTGLGLAIVQR 75
                         90
                 ....*....|....*...
gi 489115238 479 LAKNMGGDITVSSQAGKG 496
Cdd:cd16950   76 ISDAHGGSLTLANRAGGG 93
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
529-629 7.67e-17

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 76.50  E-value: 7.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 529 LLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYARedlPPLVALTA 608
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPD---IPVIVLTA 77
                         90       100
                 ....*....|....*....|..
gi 489115238 609 NV-LKDKKEYLDAGMDDVLSKP 629
Cdd:cd00156   78 KAdEEDAVRALELGADDYLVKP 99
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
276-509 9.08e-17

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 83.92  E-value: 9.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 276 LERASRDKTTFISTISHELRTPLNGIVGLSRILLDT--DLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDN 353
Cdd:NF040691 264 LEELSRLQQRFVSDVSHELRTPLTTIRMAADVIHDSrdDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAELDV 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 354 QPVDFTSF-MADLENLSGLqAQQKGLRFVLE-PTLPLPHKVitDGTRLRQILWNLISNAVKFTQQGQVTVRARYDqGDML 431
Cdd:NF040691 344 EPVDLRPLvRRVVDALRQL-AERAGVELRVDaPGTPVVAEV--DPRRVERVLRNLVVNAIEHGEGKPVVVTVAQD-DTAV 419
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489115238 432 HFEVEDSGIGIPQDEQDKIFAMYYQVkDSNGGKPATGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTVhaPAVA 509
Cdd:NF040691 420 AVTVRDHGVGLKPGEVALVFDRFWRA-DPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTL--PRVA 494
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
395-501 1.58e-16

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain.


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 75.99  E-value: 1.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 395 DGTRLRQILWNLISNAVKFTQQGQVtVRARYDQGDMLHFE--VEDSGIGIPQDEQDKIFAMYYQVKDSNGGKPAtGTGIG 472
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTPDGGR-IRCILEKFRLNRFLltVSDSGPGIPPNLREEIFERFRQGDGSSTRAHG-GTGLG 78
                         90       100
                 ....*....|....*....|....*....
gi 489115238 473 LAVSKRLAKNMGGDITVSSQAGKGSIFTL 501
Cdd:cd16925   79 LSIVKEFVELHGGTVTVSDAPGGGALFQV 107
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
290-502 1.97e-16

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


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 82.22  E-value: 1.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 290 ISHELRTPLNGIVGLSRILLDTDLTAEQEKYLktIHVSAVTLGNIfNDIID---------MDKMERRKVQLDNQPVdfTS 360
Cdd:COG5806  208 IAHEVRNPLTVVRGFIQLLQEPELSDEKRKQY--IRIALEELDRA-EAIITdyltfakpqPEKLEKIDVSEELEHV--ID 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 361 FMADLENLSGLQAQQKglrfvLEPTLplphKVITDGTRLRQILWNLISNAVKFTQQG---QVTVRArydQGDMLHFEVED 437
Cdd:COG5806  283 VLSPYANMNNVEIQTE-----LEPGL----YIEGDRQKLQQCLINIIKNGIEAMPNGgtlTIDVSI---DKNKVIISIKD 350
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489115238 438 SGIGIPQDEQDKIFAMYYQVKDsnggkpaTGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLT 502
Cdd:COG5806  351 TGVGMTKEQLERLGEPYFSTKE-------KGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTIT 408
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
283-345 2.35e-16

His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 73.78  E-value: 2.35e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489115238  283 KTTFISTISHELRTPLNGIVGLSRILLDTDLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKME 345
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIE 64
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
283-345 3.58e-16

His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 73.37  E-value: 3.58e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489115238   283 KTTFISTISHELRTPLNGIVGLSRILLDTDLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKME 345
Cdd:smart00388   2 KREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIE 64
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-503 4.47e-16

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 74.36  E-value: 4.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFTQQG-----QVTVRARYDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKdsnggkpATGTGIGL 473
Cdd:cd16920    1 IQQVLINLVRNGIEAMSEGgcerrELTIRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFYTTK-------SEGLGMGL 73
                         90       100       110
                 ....*....|....*....|....*....|
gi 489115238 474 AVSKRLAKNMGGDITVSSQAGKGSIFTLTV 503
Cdd:cd16920   74 SICRSIIEAHGGRLSVESPAGGGATFQFTL 103
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
402-503 8.07e-16

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 73.86  E-value: 8.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 402 ILWNLISNAV-----KFTQQGQVTVRARYDqGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKdsnggkPATGTGIGLAVS 476
Cdd:cd16915    4 IVGNLIDNALdalaaTGAPNKQVEVFLRDE-GDDLVIEVRDTGPGIAPELRDKVFERGVSTK------GQGERGIGLALV 76
                         90       100
                 ....*....|....*....|....*..
gi 489115238 477 KRLAKNMGGDITVSSQAGKGSIFTLTV 503
Cdd:cd16915   77 RQSVERLGGSITVESEPGGGTTFSIRI 103
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
263-487 9.39e-16

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 80.64  E-value: 9.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 263 GRDITERKRYQDALERASRDKTTFISTISHELRTPLngivglsrILLDTDLTAEQE-------KYLKTIHVSAVTLGNIF 335
Cdd:NF012163 220 GKLAQDFNQLASTLEKNEQMRRDFMADISHELRTPL--------AVLRAELEAIQDgirkftpESLDSLQAEVGTLTKLV 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 336 NDIIDMDKMERRKVQLDNQPVDFTSFMADLENLSGLQAQQKGLRfvLEPTLPLPHKVITDGTRLRQILWNLISNAVKFTQ 415
Cdd:NF012163 292 DDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLE--LEVSLPDSSLVFGDRDRLMQLFNNLLENSLRYTD 369
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489115238 416 Q-GQVTVRARyDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKPAtGTGIGLAVSKRLAKNMGGDI 487
Cdd:NF012163 370 SgGSLHISAS-QRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASG-GSGLGLAISLNIVQAHGGTL 440
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
394-502 1.23e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 73.47  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 394 TDGTRLRQILWNLISNAVKFTQQ-GQVTVRArYDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQvkDSNGGKPATGTGIG 472
Cdd:cd16948    1 TDAKWLSFIIGQIVSNALKYSKQgGKIEIYS-ETNEQGVVLSIKDFGIGIPEEDLPRVFDKGFT--GENGRNFQESTGMG 77
                         90       100       110
                 ....*....|....*....|....*....|
gi 489115238 473 LAVSKRLAKNMGGDITVSSQAGKGSIFTLT 502
Cdd:cd16948   78 LYLVKKLCDKLGHKIDVESEVGEGTTFTIT 107
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
527-646 1.27e-15

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 80.01  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYARedlPPLVAL 606
Cdd:COG2204    4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPD---LPVILL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489115238 607 TANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIKKYWDTR 646
Cdd:COG2204   81 TGYGdVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERR 121
PAS COG2202
PAS domain [Signal transduction mechanisms];
140-276 1.33e-15

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 77.37  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 140 IKEREEAQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETDEKV 219
Cdd:COG2202  122 ITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRL 201
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489115238 220 FRHNVSlTYEQWLDYPDGRKACFEIR-KVPYYDRVGKRHGLMGFGRDITERKRYQDAL 276
Cdd:COG2202  202 LEGGRE-SYELELRLKDGDGRWVWVEaSAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
528-639 1.84e-15

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 72.88  E-value: 1.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLpPLVALT 607
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANT-PAIALT 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489115238 608 A-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMI 639
Cdd:cd17580   80 GyGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-500 1.88e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoR; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli or Vibrio cholera PhoR, the histidine kinase (HK) of PhoB-PhoR a two-component signal transduction system (TCS) involved in phosphate regulation. PhoR monitors extracellular inorganic phosphate (Pi) availability and PhoB, the response regulator, regulates transcription of genes of the phosphate regulon. PhoR is a bifunctional histidine autokinase/phospho-PhoB phosphatase; in phosphate deficiency, it autophosphorylates and Pi is transferred to PhoB, and when environmental Pi is abundant, it removes the phosphoryl group from phosphorylated PhoB. Other roles of PhoB-PhoR TCS have been described, including motility, biofilm formation, intestinal colonization, and virulence in V. cholera. E.coli PhoR and Bacillus subtilis PhoR (whose HATPase domain belongs to a different family) sense very different signals in each bacterium. In E. coli the PhoR signal comes from phosphate transport mediated by the PstSCAB2 phosphate transporter and the PhoU chaperone-like protein while in B. subtilis, the PhoR activation signal comes from wall teichoic acid (WTA) metabolism.


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 73.01  E-value: 1.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFT-QQGQVTVR-ARYDQGdmLHFEVEDSGIGIPQDEQDKIFAMYYQVkDSNGGKPATGTGIGLAVS 476
Cdd:cd16952    1 LRSAFSNLVSNAVKYTpPSDTITVRwSQEESG--ARLSVEDTGPGIPPEHIPRLTERFYRV-DIERCRNTGGTGLGLAIV 77
                         90       100
                 ....*....|....*....|....
gi 489115238 477 KRLAKNMGGDITVSSQAGKGSIFT 500
Cdd:cd16952   78 KHVMSRHDARLLIASELGKGSRFT 101
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
389-496 1.99e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 72.82  E-value: 1.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 389 PHKVITDGTRLRQILWNLISNAVKFTQQG-QVTVRARYDQGDMlhFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGkpat 467
Cdd:cd16940    4 DIQVQGDALLLFLLLRNLVDNAVRYSPQGsRVEIKLSADDGAV--IRVEDNGPGIDEEELEALFERFYRSDGQNYG---- 77
                         90       100
                 ....*....|....*....|....*....
gi 489115238 468 GTGIGLAVSKRLAKNMGGDITVSSQAGKG 496
Cdd:cd16940   78 GSGLGLSIVKRIVELHGGQIFLGNAQGGG 106
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
678-769 2.66e-15

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 71.90  E-value: 2.66e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238   678 GPKLITDGLAVFEKMMPGYLSVLESNLTARDKKGVVEEGHKIKGAAGSVGLRHLQQLGQQIQSPDLPAWEDNVaEWIEEM 757
Cdd:smart00073   2 GLELFREELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEV-ELTPDL 80
                           90
                   ....*....|..
gi 489115238   758 KQEWQHDVAVLK 769
Cdd:smart00073  81 LDLLLELVDVLK 92
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
528-629 6.06e-15

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 70.93  E-value: 6.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQkyAREDLPPLVaLT 607
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRA--AGKQTPVLM-LT 77
                         90       100
                 ....*....|....*....|...
gi 489115238 608 A-NVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd19935   78 ArDSVEDRVKGLDLGADDYLVKP 100
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
528-640 6.97e-15

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 71.54  E-value: 6.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDielNVIVARSV---LEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAreDLPPLV 604
Cdd:cd19934    1 LLLVED---DALLAAQLkeqLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGR--ATPVLI 75
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489115238 605 aLTANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd19934   76 -LTARDsWQDKVEGLDAGADDYLTKPFHIEELLARLR 111
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
528-629 1.91e-14

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 69.83  E-value: 1.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLpPLVALT 607
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHI-PVIMIT 80
                         90       100
                 ....*....|....*....|...
gi 489115238 608 A-NVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd17538   81 AlDDREDRIRGLEAGADDFLSKP 103
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
395-487 2.69e-14

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain.


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 69.41  E-value: 2.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 395 DGTRLRQILWNLISNAVKFTQQ-GQVTVRA-RYDQGdmLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNgGKPATGTGIG 472
Cdd:cd16946    1 DRDRLQQLFVNLLENSLRYTDTgGKLRIRAaQTPQE--VRLDVEDSAPGVSDDQLARLFERFYRVESSR-NRASGGSGLG 77
                         90
                 ....*....|....*
gi 489115238 473 LAVSKRLAKNMGGDI 487
Cdd:cd16946   78 LAICHNIALAHGGTI 92
PRK10604 PRK10604
sensor protein RstB; Provisional
283-501 2.75e-14

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 75.80  E-value: 2.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 283 KTTFISTISHELRTPLngiVGLS-RILLDTDLTAEQEKYLKTihvsavTLGNIfNDIID----MDKMERRKVQLDNQPVD 357
Cdd:PRK10604 212 KKQLIDGIAHELRTPL---VRLRyRLEMSDNLSAAESQALNR------DIGQL-EALIEelltYARLDRPQNELHLSEPD 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 358 FTSFMADleNLSGLQAQQKGLRFVLEPtLPLPHKVITDGTRLRQILWNLISNAVKFTQQgQVTVRARYDqGDMLHFEVED 437
Cdd:PRK10604 282 LPAWLST--HLADIQAVTPEKTVRLDT-PHQGDYGALDMRLMERVLDNLLNNALRYAHS-RVRVSLLLD-GNQACLIVED 356
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489115238 438 SGIGIPQDEQDKIFAMYYQVKDSNGGKPAtGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTL 501
Cdd:PRK10604 357 DGPGIPPEERERVFEPFVRLDPSRDRATG-GCGLGLAIVHSIALAMGGSVNCDESELGGARFSF 419
envZ PRK09467
osmolarity sensor protein; Provisional
282-490 3.40e-14

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 75.33  E-value: 3.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 282 DKTTFISTISHELRTPLngivglSRILLDTDLTAEQEKYLKTihvsavtlgNIFNDIIDMDK-----ME--RRKVQLDNQ 354
Cdd:PRK09467 228 DRTLLMAGVSHDLRTPL------TRIRLATEMMSEEDGYLAE---------SINKDIEECNAiieqfIDylRTGQEMPME 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 355 PVDFTSFMADLenlsgLQAQQKGLRfVLEPTL-PLPHKVITDGTRLRQILWNLISNAVKFTQqGQVTVRARYDqGDMLHF 433
Cdd:PRK09467 293 MADLNALLGEV-----IAAESGYER-EIETALqPGPIEVPMNPIAIKRALANLVVNAARYGN-GWIKVSSGTE-GKRAWF 364
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489115238 434 EVEDSGIGIPQDEQDKIFAMYYQVKDSNGGkpaTGTGIGLAVSKRLAKNMGGDITVS 490
Cdd:PRK09467 365 QVEDDGPGIPPEQLKHLFQPFTRGDSARGS---SGTGLGLAIVKRIVDQHNGKVELG 418
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
285-576 3.53e-14

phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 76.51  E-value: 3.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 285 TFISTISHELRTPLNGIVGLSRILLDTDLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFMAD 364
Cdd:PRK10618 452 AFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDLIDE 531
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 365 --LENLSGLQaqQKGLRFVLEPTLPLPHKVITDGTRLRQILWNLISNAVKFTQQGQVTVRARYDQG--DMLHFEVEDSGI 440
Cdd:PRK10618 532 vlPEVLPAIK--RKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEVDQDESspDRLTIRILDTGA 609
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 441 GIPQDEQDKIfaMYYQVKDSNGGKPATGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTVHAPAVAEEIEdafEDDD 520
Cdd:PRK10618 610 GVSIKELDNL--HFPFLNQTQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKMLAADPEVE---EEEE 684
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489115238 521 MPLPALNVLLveDI---ELNVIVARsVLEKLGNSVDVAMtgkaalEMFTPGEYDLVLLD 576
Cdd:PRK10618 685 KLLDGVTVLL--DItseEVRKIVTR-QLENWGATCITPD------ERLISQEYDIFLTD 734
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
527-640 6.12e-14

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 68.62  E-value: 6.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMT-GKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLpPLVA 605
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSAGYLEVVSFTdPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDV-PIVM 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 606 LTANVLKD-KKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17551   81 ITADTDREvRLRALEAGATDFLTKPFDPVELLARVR 116
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
161-271 9.54e-14

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 67.82  E-value: 9.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  161 LDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDyPDGRKA 240
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELL-LNGEER 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 489115238  241 CFEIRKVPYYDRVGKRHGLMGFGRDITERKR 271
Cdd:pfam08448  80 HYELRLTPLRDPDGEVIGVLVISRDITERRR 110
PRK13560 PRK13560
hypothetical protein; Provisional
122-276 1.06e-13

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 75.09  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 122 REKAEAERQETFEQLKVEIKEREEAQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPA 201
Cdd:PRK13560 171 RFERHAHADDQVDGFAEDITERKRAEERIDEALHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIH 250
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489115238 202 DVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKACFEIR--KVPYYDRVGKRHGLMGFGRDITERKRYQDAL 276
Cdd:PRK13560 251 DFAPAQPADDYQEADAAKFDADGSQIIEAEFQNKDGRTRPVDVIfnHAEFDDKENHCAGLVGAITDISGRRAAEREL 327
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
271-503 6.09e-13

Cu(+)/Ag(+) sensor histidine kinase;


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 71.73  E-value: 6.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 271 RYQDALERASrdktTFISTISHELRTPLNGIVGLSRILLDTDLTaeqEKYLKTIHVSAVT----LGNIFNDIIDMDKMER 346
Cdd:PRK09835 254 RIEDVFTRQS----NFSADIAHEIRTPITNLITQTEIALSQSRS---QKELEDVLYSNLEeltrMAKMVSDMLFLAQADN 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 347 RKVQLDNQPVDFTSFMADLENLSGLQAQQKGLRFVLEPTlplPHKVITDGTRLRQILWNLISNAVKFTQQGQ-VTVRARy 425
Cdd:PRK09835 327 NQLIPEKKMLDLADEVGKVFDFFEAWAEERGVELRFVGD---PCQVAGDPLMLRRAISNLLSNALRYTPAGEaITVRCQ- 402
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489115238 426 DQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKpATGTGIGLAVSKRLAKNMGGDITVSSQAgKGSIFTLTV 503
Cdd:PRK09835 403 EVDHQVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQRK-GEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVISL 478
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
395-503 6.78e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Azorhizobium caulinodans NtrY; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Azorhizobium caulinodans ORS571 NtrY of the NtrY-NtrX TCS, which is involved in nitrogen fixation and metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also have PAS sensor domains.


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 65.64  E-value: 6.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 395 DGTRLRQILWNLISNAVKFTQ-----QGQVTVRARYDQGDMLHFEVEDSGIGIPQDEQDKIFAMYyqVKDSnggkpATGT 469
Cdd:cd16944    1 DTTQISQVLTNILKNAAEAIEgrpsdVGEVRIRVEADQDGRIVLIVCDNGKGFPREMRHRATEPY--VTTR-----PKGT 73
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489115238 470 GIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTV 503
Cdd:cd16944   74 GLGLAIVKKIMEEHGGRISLSNREAGGACIRIIL 107
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
390-503 9.06e-13

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 71.48  E-value: 9.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 390 HKVITdgtrlrqILWNLISN---AVKFTQQGQVTVRARYDQGdMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNggkpa 466
Cdd:PRK11086 432 HELIT-------ILGNLIENaleAVGGEEGGEISVSLHYRNG-WLHCEVSDDGPGIAPDEIDAIFDKGYSTKGSN----- 498
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489115238 467 tgTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTV 503
Cdd:PRK11086 499 --RGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQI 533
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
529-640 1.89e-12

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 64.60  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 529 LLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLpPLVALTA 608
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSI-PIIMLTA 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489115238 609 NVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd19937   80 KGEEfDKVLGLELGADDYITKPFSPRELLARVK 112
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
266-501 2.84e-12

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 70.10  E-value: 2.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 266 ITERKRYQDALERA-SRDKTTF--------ISTISHELRTPLNGIvglSRILLDTDLTAEQEKYLKTIHvsavTLGNIFN 336
Cdd:COG4192  407 IEERKRIEKNLRQTqDELIQAAkmavvgqtMTSLAHELNQPLNAM---SMYLFSAKKALEQENYAQLPT----SLDKIEG 479
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 337 DIIDMDKMER------RKVQLDNQPVDFTSFMADLENLsgLQAQQKGLRFVLepTLPLPHKVITDGTRLRQILWNLISNA 410
Cdd:COG4192  480 LIERMDKIIKslrqfsRKSDTPLQPVDLRQVIEQAWEL--VESRAKPQQITL--HIPDDLMVQGDQVLLEQVLVNLLVNA 555
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 411 VK-FTQQGQVTVrARYDQGDMLHFEVEDSGIGIPqdEQDKIFAMYYQVKDsnggkpaTGTGIGLAVSKRLAKNMGGDITV 489
Cdd:COG4192  556 LDaVATQPQISV-DLLSNAENLRVAISDNGNGWP--LVDKLFTPFTTTKE-------VGLGLGLSICRSIMQQFGGDLYL 625
                        250
                 ....*....|..
gi 489115238 490 SSQAGKGSIFTL 501
Cdd:COG4192  626 ASTLERGAMVIL 637
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
280-341 8.90e-12

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 60.69  E-value: 8.90e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489115238 280 SRDKTTFISTISHELRTPLNGIVGLSRILLDTDL-TAEQEKYLKTIHVSAVTLGNIFNDIIDM 341
Cdd:cd00082    1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLdDEEQREYLERIREEAERLLRLINDLLDL 63
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
275-475 9.37e-12

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 68.04  E-value: 9.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 275 ALERASRDKTTFISTISHELRTPLngivglSRILLDTDLTAEQE---KYLKTIHVSAVTLGNIFNDIIDMDKMERrKVQL 351
Cdd:PRK09470 235 ALERMMTSQQRLLSDISHELRTPL------TRLQLATALLRRRQgesKELERIETEAQRLDSMINDLLVLSRNQQ-KNHL 307
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 352 DNQPVDFTSFMADLENLSGLQAQQKGLRFVLePTLPLPHKVITDGTRLRQILWNLISNAVKFTQQgQVTVrARYDQGDML 431
Cdd:PRK09470 308 ERETFKANSLWSEVLEDAKFEAEQMGKSLTV-SAPPGPWPINGNPNALASALENIVRNALRYSHT-KIEV-AFSVDKDGL 384
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489115238 432 HFEVEDSGIGIPQDEQDKIFAMYYQV---KDSNGGkpatGTGIGLAV 475
Cdd:PRK09470 385 TITVDDDGPGVPEEEREQIFRPFYRVdeaRDRESG----GTGLGLAI 427
PRK10336 PRK10336
two-component system response regulator QseB;
526-640 1.36e-11

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 64.92  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 526 LNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREdlpPLVA 605
Cdd:PRK10336   1 MRILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQRE---PVLI 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 606 LTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK10336  78 LTArDALAERVEGLRLGADDYLCKPFALIEVAARLE 113
PRK10643 PRK10643
two-component system response regulator PmrA;
528-640 1.49e-11

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 64.67  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIEL---NVIVArsvLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKyaREDLPPLV 604
Cdd:PRK10643   3 ILIVEDDTLllqGLILA---LQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQK--KYTLPVLI 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489115238 605 aLTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK10643  78 -LTArDTLEDRVAGLDVGADDYLVKPFALEELHARIR 113
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-501 1.58e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 61.71  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFTQQ-GQVTVRARYDQGDmLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKPAtgTGIGLAVSK 477
Cdd:cd16945    5 LRQAINNLLDNAIDFSPEgGLIALQLEADTEG-IELLVFDEGSGIPDYALNRVFERFYSLPRPHSGQKS--TGLGLAFVQ 81
                         90       100
                 ....*....|....*....|....*
gi 489115238 478 RLAKNMGGDITVSS-QAGKGSIFTL 501
Cdd:cd16945   82 EVAQLHGGRITLRNrPDGVLAFLTL 106
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-496 1.77e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 61.19  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFTQQgQVTVRARYDqGDMLHFEVEDSGIGIPQDEQDKIFAMYYQV---KDSNGGkpatGTGIGLAV 475
Cdd:cd16949    1 LARALENVLRNALRYSPS-KILLDISQD-GDQWTITITDDGPGVPEDQLEQIFLPFYRVdsaRDRESG----GTGLGLAI 74
                         90       100
                 ....*....|....*....|.
gi 489115238 476 SKRLAKNMGGDITVSSQAGKG 496
Cdd:cd16949   75 AERAIEQHGGKIKASNRKPGG 95
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
528-640 1.82e-11

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 61.63  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELtqKYAREDLPPLVaLT 607
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRL--RAAGNDLPILV-LT 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489115238 608 A-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17627   78 ArDSVSDRVAGLDAGADDYLVKPFALEELLARVR 111
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
528-608 2.41e-11

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 61.44  E-value: 2.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQkyaREDLPPLVALT 607
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQE---RSLPTSVIVIT 77

                 .
gi 489115238 608 A 608
Cdd:cd17572   78 A 78
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
285-503 2.56e-11

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 67.08  E-value: 2.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  285 TFISTISHELRTPLnGIVGLSRILLDT-DLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFMA 363
Cdd:TIGR03785 487 NMSSRLSHELRTPV-AVVRSSLENLELqALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSEVLS 565
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  364 DLenLSGLQAQQKGLRFVLE-PTLPLPHKVItdGTRLRQILWNLISNAVKFTQQGQVTVRARYDQGDMLHFEVEDSGIGI 442
Cdd:TIGR03785 566 GC--MQGYQMTYPPQRFELNiPETPLVMRGS--PELIAQMLDKLVDNAREFSPEDGLIEVGLSQNKSHALLTVSNEGPPL 641
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489115238  443 PQDEQDKIFAMYYQVKDsNGGKPATGTGIGLAVSKRLAKNMGGDITVSSQA-GKGSIFTLTV 503
Cdd:TIGR03785 642 PEDMGEQLFDSMVSVRD-QGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRISL 702
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
528-629 6.63e-11

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 59.49  E-value: 6.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVED---IeLNVIvaRSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAredlPPLV 604
Cdd:cd17620    1 ILVIEDepqI-RRFL--RTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSA----VPVI 73
                         90       100
                 ....*....|....*....|....*.
gi 489115238 605 ALTA-NVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd17620   74 VLSArDEESDKIAALDAGADDYLTKP 99
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
528-640 7.28e-11

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 60.01  E-value: 7.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVED-IELNVIVARsVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQkyaREDLPPLVaL 606
Cdd:cd17623    1 ILLIDDdRELTELLTE-YLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRK---TSQVPVLM-L 75
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489115238 607 TANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17623   76 TARGDDiDRILGLELGADDYLPKPFNPRELVARIR 110
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-501 9.08e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 59.39  E-value: 9.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNA---VKFTQQGQVTVRARYdQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSngGKpatGTGIGLAV 475
Cdd:cd16976    1 IQQVLMNLLQNAldaMGKVENPRIRIAARR-LGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTKPV--GK---GTGLGLSI 74
                         90       100
                 ....*....|....*....|....*.
gi 489115238 476 SKRLAKNMGGDITVSSQAGKGSIFTL 501
Cdd:cd16976   75 SYGIVEEHGGRLSVANEEGAGARFTF 100
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
682-762 9.89e-11

Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 58.93  E-value: 9.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 682 ITDGLAVFEKMMPGYLSVLESNLTAR----DKKGVVEEGHKIKGAAGSVGLRHLQQLGQQIQS---------PDLPAWED 748
Cdd:cd00088    1 MEELLELFLEEAEELLEELERALLELedaeDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDlldalrdglEVTPELID 80
                         90
                 ....*....|....
gi 489115238 749 NVAEWIEEMKQEWQ 762
Cdd:cd00088   81 LLLDALDALKAELE 94
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
527-609 1.39e-10

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 58.96  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 527 NVLLVEDielNVIVA---RSVLEKLG-NSVDVAMTGKAALEMF---TPgeyDLVLLDIQLP-DMTGLDISRELTQKYare 598
Cdd:cd17534    2 KILIVED---EAIIAldlKEILESLGyEVVGIADSGEEAIELAeenKP---DLILMDINLKgDMDGIEAAREIREKF--- 72
                         90
                 ....*....|.
gi 489115238 599 DLpPLVALTAN 609
Cdd:cd17534   73 DI-PVIFLTAY 82
glnL PRK11073
nitrogen regulation protein NR(II);
273-501 1.61e-10

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 63.56  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 273 QDALERASRDkttFISTISHELRTPLNGIVG----LSRILLDTDLTaeqeKYLKTIHVSAVTLGNIFNDIIDMDKMERRK 348
Cdd:PRK11073 123 QHAQQVAARD---LVRGLAHEIKNPLGGLRGaaqlLSKALPDPALT----EYTKVIIEQADRLRNLVDRLLGPQRPGTHV 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 349 VQldnqpvdftSFMADLENLSGLQAQQKGLRFVLE----PTLP-LPHkvitDGTRLRQILWNLISNAVKFTQQ--GQVTV 421
Cdd:PRK11073 196 TE---------SIHKVAERVVQLVSLELPDNVRLIrdydPSLPeLAH----DPDQIEQVLLNIVRNALQALGPegGTITL 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 422 RARYDQGDMLH---------FEVEDSGIGIPQDEQDKIFamYYQVKDSNGgkpatGTGIGLAVSKRLAKNMGGDITVSSQ 492
Cdd:PRK11073 263 RTRTAFQLTLHgeryrlaarIDIEDNGPGIPPHLQDTLF--YPMVSGREG-----GTGLGLSIARNLIDQHSGKIEFTSW 335

                 ....*....
gi 489115238 493 AGKgSIFTL 501
Cdd:PRK11073 336 PGH-TEFSV 343
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
686-759 1.74e-10

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 57.75  E-value: 1.74e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489115238  686 LAVFEKMMPGYLSVLESNLTARDKKGVVEEGHKIKGAAGSVGLRHLQQLGQQIQS----PDLPAWEDNVAEWIEEMKQ 759
Cdd:pfam01627   3 LELFLEEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDllreGELPLDPELLEALRDLLEA 80
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
527-640 2.18e-10

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 58.80  E-value: 2.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLpPLVAL 606
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDI-PIIML 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489115238 607 TANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17618   81 TARGEEeDKVRGLEAGADDYITKPFSPRELVARIK 115
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
528-640 2.24e-10

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 58.59  E-value: 2.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYARedlpPLVALT 607
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSNV----PIIMLT 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489115238 608 ANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17614   77 AKDSEvDKVLGLELGADDYVTKPFSNRELLARVK 110
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
528-640 2.31e-10

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 58.57  E-value: 2.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDielNVIVARSV---LEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELtqKYAREDLPPLV 604
Cdd:cd17616    1 VLLIED---DSATAQSIelmLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTL--RLAKVKTPILI 75
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 605 ALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17616   76 LSGLADIEDKVKGLGFGADDYMTKPFHKDELVARIH 111
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-488 3.06e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Brucella abortus BvrS and Sinorhizobium meliloti ChvG; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Brucella abortus BvrS of the BvrR-BvrS two-component regulatory system (TCS), which controls cell invasion and intracellular survival, as well as Sinorhizobium meliloti and Agrobacterium tumefaciens ChvG of the ChvI-ChvG TCS necessary for endosymbiosis and pathogenicity in plants. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), an accessory HAMP sensor domain, a periplasmic stimulus-sensing domain, and some also have a sensor N-terminal transmembrane domain.


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 57.97  E-value: 3.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFT--QQGQVTVRaRYDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKpATGTGIGLAVS 476
Cdd:cd16953    1 LGQVLRNLIGNAISFSppDTGRITVS-AMPTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANEAF-GQHSGLGLSIS 78
                         90
                 ....*....|..
gi 489115238 477 KRLAKNMGGDIT 488
Cdd:cd16953   79 RQIIEAHGGISV 90
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
528-629 3.07e-10

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 57.59  E-value: 3.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTqkyAREDLPPLVALT 607
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLR---ARSNVPVIMVTA 77
                         90       100
                 ....*....|....*....|..
gi 489115238 608 ANVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd17621   78 KDSEIDKVVGLELGADDYVTKP 99
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
528-640 3.81e-10

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 58.13  E-value: 3.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDiELNVIVARSV-LEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELtqkyaREDLP--PLV 604
Cdd:cd17615    2 VLVVDD-EPNITELLSMaLRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRL-----RADGPdvPVL 75
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489115238 605 ALTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17615   76 FLTAkDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLR 112
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
275-506 4.12e-10

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 62.73  E-value: 4.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 275 ALERASRDKTTFISTISHELRTPLNGIVGLSRILLD--TDLTAEQekyLKTIHVSAVTLGNIFNDI-----IDMDKMERR 347
Cdd:PRK10549 232 TLEKNEQMRRDFMADISHELRTPLAVLRGELEAIQDgvRKFTPES---VASLQAEVGTLTKLVDDLhqlslSDEGALAYR 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 348 KVQLDNQPVdftsfmadLENLSGL---QAQQKGLRFVLEptLPLPHKVITDGTRLRQILWNLISNAVKFT-QQGQVTVRA 423
Cdd:PRK10549 309 KTPVDLVPL--------LEVAGGAfreRFASRGLTLQLS--LPDSATVFGDPDRLMQLFNNLLENSLRYTdSGGSLHISA 378
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 424 RY-DQGDMLHFEveDSGIGIPQDEQDKIFAMYYQVkDSNGGKPATGTGIGLAVSKRLAKNMGGDITVS-SQAGKGSIftl 501
Cdd:PRK10549 379 EQrDKTLRLTFA--DSAPGVSDEQLQKLFERFYRT-EGSRNRASGGSGLGLAICLNIVEAHNGRIIAAhSPFGGVSI--- 452

                 ....*
gi 489115238 502 TVHAP 506
Cdd:PRK10549 453 TVELP 457
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-502 4.58e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain.


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 57.44  E-value: 4.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFTQQgqvTVRARY-DQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNgGKPATGTGIGLAVSK 477
Cdd:cd16939    1 MARALDNLLRNALRYAHR---TVRIALlVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSR-DRATGGFGLGLAIVH 76
                         90       100
                 ....*....|....*....|....*
gi 489115238 478 RLAKNMGGDITVSSQAGKGSIFTLT 502
Cdd:cd16939   77 RVALWHGGHVECDDSELGGACFRLT 101
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
526-580 4.97e-10

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 55.65  E-value: 4.97e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 489115238   526 LNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLP 580
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
527-643 8.38e-10

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 57.43  E-value: 8.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 527 NVLLVEDIELNVIVARSVLEKLG--NSVDVAMTGKAALEM-FTPGEY------DLVLLDIQLPDMTGLDISRELTQkyaR 597
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDFlRGEGEYadaprpDLILLDLNMPRMDGFEVLREIKA---D 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489115238 598 EDLP--PLVALTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK---KYW 643
Cdd:cd17557   78 PDLRriPVVVLTTsDAEEDIERAYELGANSYIVKPVDFEEFVEAIRslgEYW 129
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-494 9.71e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII); This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s).


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 56.64  E-value: 9.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFT--QQGQVTVRARYDQGDMLH---------FEVEDSGIGIPQDEQDKIFamYYQVKdsngGKPaT 467
Cdd:cd16918    1 LIQVFLNLVRNAAQALagSGGEIILRTRTQRQVTLGhprhrlalrVSVIDNGPGIPPDLQDTIF--YPMVS----GRE-N 73
                         90       100
                 ....*....|....*....|....*..
gi 489115238 468 GTGIGLAVSKRLAKNMGGDITVSSQAG 494
Cdd:cd16918   74 GTGLGLAIAQNIVSQHGGVIECDSQPG 100
pleD PRK09581
response regulator PleD; Reviewed
528-640 1.04e-09

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 61.46  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNV--IVARSVLEKLgnSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLpPLVA 605
Cdd:PRK09581   5 ILVVDDIPANVklLEAKLLAEYY--TVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHI-PVVM 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 606 LTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK09581  82 VTAlDDPEDRVRGLEAGADDFLTKPINDVALFARVK 117
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
164-266 1.31e-09

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 56.10  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 164 SPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKACFE 243
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                         90       100
                 ....*....|....*....|...
gi 489115238 244 IRKVPYYDRVGKRHGLMGFGRDI 266
Cdd:cd00130   81 VSLTPIRDEGGEVIGLLGVVRDI 103
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
526-608 1.39e-09

DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms];


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 59.06  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 526 LNVLLVEDIELNVIVARSVLEKLGN--SVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYARedlPPL 603
Cdd:COG3279    2 MKILIVDDEPLARERLERLLEKYPDleVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPP---PPI 78

                 ....*
gi 489115238 604 VALTA 608
Cdd:COG3279   79 IFTTA 83
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
527-629 1.56e-09

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 55.55  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 527 NVLLVEDIELNVIVARSVLEKLGN--SVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYARedlPPLV 604
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEAGfeVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPD---TKII 77
                         90       100
                 ....*....|....*....|....*....
gi 489115238 605 ALTANvlkDKKEY----LDAGMDDVLSKP 629
Cdd:COG4753   78 ILSGY---SDFEYaqeaIKLGADDYLLKP 103
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
524-639 4.30e-09

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 56.89  E-value: 4.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 524 PALNVLLVEDIELNVIVARSVLEKLG-NSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYARedlpP 602
Cdd:COG3707    2 RGLRVLVVDDEPLRRADLREGLREAGyEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPA----P 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489115238 603 LVALTANVLKDKKEY-LDAGMDDVLSKPLSVPALTAMI 639
Cdd:COG3707   78 VILLTAYSDPELIERaLEAGVSAYLVKPLDPEDLLPAL 115
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
527-640 4.64e-09

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 57.51  E-value: 4.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAredLPPLVAL 606
Cdd:PRK10529   3 NVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWSA---IPVIVLS 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489115238 607 TANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK10529  80 ARSEESDKIAALDAGADDYLSKPFGIGELQARLR 113
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
528-640 6.17e-09

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 54.31  E-value: 6.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVED-IELNVIVArSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYARedlpPLVAL 606
Cdd:cd17622    3 ILLVEDdPKLARLIA-DFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG----PILLL 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 607 TANVlKDKKEY--LDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17622   78 TALD-SDIDHIlgLELGADDYVVKPVEPAVLLARLR 112
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
147-311 7.80e-09

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


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 58.63  E-value: 7.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 147 QIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETDEKVFRHNVSL 226
Cdd:COG3829    3 ELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSPLLEVLKTGKPVTGVIQKT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 227 tyeqwldypDGRKACFEIRKVPYYDRvGKRHGLMGFGRDITERKRYQDALERASRDKttfistiSHELRTPLNGIVGLSR 306
Cdd:COG3829   83 ---------GGKGKTVIVTAIPIFED-GEVIGAVETFRDITELKRLERKLREEELER-------GLSAKYTFDDIIGKSP 145

                 ....*
gi 489115238 307 ILLDT 311
Cdd:COG3829  146 AMKEL 150
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
57-510 8.23e-09

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 58.76  E-value: 8.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  57 RSIFFGLLITPWAVYFLSVVVEQLEESRQRLSRLVQKLEEMRERDLKLNVQLKDNIAQLNQEIVEREKAEAERQETFEQL 136
Cdd:COG3920   70 ALAAAVGAAAALLALLVLLLLLLLAAAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAEL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 137 KVEIKEREEAQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETD 216
Cdd:COG3920  150 AVALAELAAALLLLAEELAALRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAA 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 217 EKVFRHNVSLTYEQWLDyPDGRKACFEIRKVPYYDRVGKRHGLMGFGRDITERKRYQDALERASRDKTTFISTISHELRT 296
Cdd:COG3920  230 LLRLRAAVLEELERRRR-ARGLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKELLLRELHHRVKN 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 297 PLNGIVGLSRIlldtdltaeQEKYLKTIHVSAVtlgnifndiidMDKMERR-----KVQ------LDNQPVDFTSFMADL 365
Cdd:COG3920  309 NLQVVSSLLRL---------QARRADDPEAREA-----------LEESQNRiqalaLVHellyqsEDWEGVDLRDYLREL 368
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 366 ENLSGLQAQQKGLRFVLE-PTLPLPhkvITDGTRLRQILWNLISNAVKF----TQQGQVTVRARYDqGDMLHFEVEDSGI 440
Cdd:COG3920  369 LEPLRDSYGGRGIRIELDgPDVELP---ADAAVPLGLILNELVTNALKHaflsGEGGRIRVSWRRE-DGRLRLTVSDNGV 444
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 441 GIPQDEQdkifamyyqvkdsnggkPATGTGIGLAVSKRLAKNMGGDITVSSqaGKGSIFTLTVHAPAVAE 510
Cdd:COG3920  445 GLPEDVD-----------------PPARKGLGLRLIRALVRQLGGTLELDR--PEGTRVRITFPLAELAA 495
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
528-641 8.88e-09

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 54.09  E-value: 8.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGN-SVDVAMTGKAALEM---FTPgeyDLVLLDIQLPDMTGLDISRELTQKYAREDLpPL 603
Cdd:cd17552    4 ILVIDDEEDIREVVQACLEKLAGwEVLTASSGQEGLEKaatEQP---DAILLDVMMPDMDGLATLKKLQANPETQSI-PV 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489115238 604 VALTANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIKK 641
Cdd:cd17552   80 ILLTAKAqPSDRQRFASLGVAGVIAKPFDPLTLAEQIAK 118
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
406-503 1.01e-08

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 58.49  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 406 LISNAVKF-----TQQGQVTVRARYDqGDMLHFEVEDSGIGIPQDEQDKIFAMYyqvkdsngGKPATGTGIGLA-VSKRL 479
Cdd:COG2972  344 LVENAIEHgiepkEGGGTIRISIRKE-GDRLVITVEDNGVGMPEEKLEKLLEEL--------SSKGEGRGIGLRnVRERL 414
                         90       100
                 ....*....|....*....|....*.
gi 489115238 480 AKNMGGD--ITVSSQAGKGSIFTLTV 503
Cdd:COG2972  415 KLYYGEEygLEIESEPGEGTTVTIRI 440
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
526-640 1.19e-08

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 56.09  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 526 LNVLLVED-IELNVIVARSVLEKlGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELtqKYAREDLPPLV 604
Cdd:PRK09836   1 MKLLIVEDeKKTGEYLTKGLTEA-GFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRML--RSANKGMPILL 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 605 ALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK09836  78 LTALGTIEHRVKGLELGADDYLVKPFAFAELLARVR 113
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
364-499 1.33e-08

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: 54.18  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 364 DLENL-SGLQA--QQKGLRFVLEptLPLPHKVITDGTRLRQILWNLISNAVKFTQqGQVTVRARYDQGdMLHFEVEDSGI 440
Cdd:cd16954    2 LLDSLcSALNKvyQRKGVSISLD--ISPELRFPGERNDLMELLGNLLDNACKWCL-EFVEVTARQTDG-GLHLIVDDDGP 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489115238 441 GIPQDEQDKIFAMYYQVKDSNGGKpatgtGIGLAVSKRLAKNMGGDITVSSQAGKGSIF 499
Cdd:cd16954   78 GVPESQRSKIFQRGQRLDEQRPGQ-----GLGLAIAKEIVEQYGGELSLSDSPLGGARF 131
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
528-629 1.37e-08

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 52.90  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLpPLVALT 607
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHI-PVIFLT 79
                         90       100
                 ....*....|....*....|...
gi 489115238 608 A-NVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd19920   80 AlTDTEDKVKGFELGAVDYITKP 102
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
399-501 1.42e-08

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 53.54  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFTQQ-GQVTVRAR-----------YDQ---GDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSngG 463
Cdd:cd16919    1 LELAILNLAVNARDAMPEgGRLTIETSnqrvdadyalnYRDlipGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEV--G 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489115238 464 KpatGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTL 501
Cdd:cd16919   79 K---GTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRI 113
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
545-631 1.67e-08

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 53.36  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 545 LEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKyaREDLPPLVALTANVLKDKKEYLDAGMDD 624
Cdd:cd17555   20 LEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKE--SPDTPVIVVSGAGVMSDAVEALRLGAWD 97

                 ....*..
gi 489115238 625 VLSKPLS 631
Cdd:cd17555   98 YLTKPIE 104
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
395-494 2.23e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals.


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 52.46  E-value: 2.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 395 DGTRLRQILWNLISNAVKFTQQGQVTVRARYDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKpaTGTGIGLA 474
Cdd:cd16975    1 DTLLLSRALINIISNACQYAPEGGTVSISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSG--GHYGMGLY 78
                         90       100
                 ....*....|....*....|.
gi 489115238 475 VSKRLAKNMGGDITVS-SQAG 494
Cdd:cd16975   79 IAKNLVEKHGGSLIIEnSQKG 99
PRK10337 PRK10337
sensor protein QseC; Provisional
271-504 2.47e-08

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 56.97  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 271 RYQDALERASRdkttFISTISHELRTPLNGI-VGLSRILLDTDLTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKV 349
Cdd:PRK10337 229 RTHAMMVRERR----FTSDAAHELRSPLAALkVQTEVAQLSDDDPQARKKALLQLHAGIDRATRLVDQLLTLSRLDSLDN 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 350 QLDNQPVDFtsfmADLenlsgLQ---------AQQKGLrfvlEPTLPLP-HKVITDGTRLRQILW--NLISNAVKFTQQG 417
Cdd:PRK10337 305 LQDVAEIPL----EDL-----LQsavmdiyhtAQQAGI----DVRLTLNaHPVIRTGQPLLLSLLvrNLLDNAIRYSPQG 371
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 418 ---QVTVRARydqgdmlHFEVEDSGIGIPQDEQDKIFAMYYQVKdsngGKPATGTGIGLAVSKRLAKNMGGDITVSSQAG 494
Cdd:PRK10337 372 svvDVTLNAR-------NFTVRDNGPGVTPEALARIGERFYRPP----GQEATGSGLGLSIVRRIAKLHGMNVSFGNAPE 440
                        250
                 ....*....|
gi 489115238 495 KGsiFTLTVH 504
Cdd:PRK10337 441 GG--FEAKVS 448
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
156-276 3.63e-08

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 52.29  E-value: 3.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  156 FLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETDEKVFRHNVSLTYEQ-WLDY 234
Cdd:TIGR00229   4 RYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEErRVRR 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 489115238  235 PDGRKACFEIRKVPYYdRVGKRHGLMGFGRDITERKRYQDAL 276
Cdd:TIGR00229  84 KDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEAL 124
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
527-601 3.82e-08

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 52.22  E-value: 3.82e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489115238 527 NVLLVEDiELNV-IVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYarEDLP 601
Cdd:cd17554    2 KILVVDD-EENIrELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKK--PDLP 74
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
527-642 3.89e-08

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 53.77  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELtqKYAREDLPPLVaL 606
Cdd:COG4567    6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEAL--RERDPDARIVV-L 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489115238 607 T-----ANVLkdkkEYLDAGMDDVLSKPLSVPALTAMIKKY 642
Cdd:COG4567   83 TgyasiATAV----EAIKLGADDYLAKPADADDLLAALERA 119
PRK11517 PRK11517
DNA-binding response regulator HprR;
526-640 4.56e-08

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 54.52  E-value: 4.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 526 LNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAredlPPLVA 605
Cdd:PRK11517   1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQ----TPVIC 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 606 LTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK11517  77 LTArDSVDDRVRGLDSGANDYLVKPFSFSELLARVR 112
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
526-641 5.76e-08

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 51.96  E-value: 5.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 526 LNVLLVEDIELNVIVARSVLEKLG-NSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLPPLV 604
Cdd:cd19923    1 MKVLVVDDFSTMRRIIKNLLKELGfNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLM 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489115238 605 ----ALTANVLKDKKeyldAGMDDVLSKPLSVPALTAMIKK 641
Cdd:cd19923   81 vtaeAKKENVIAAAQ----AGVNNYIVKPFTAATLKEKLEK 117
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
528-639 6.68e-08

phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; Helicobacter pylori response regulator hp1043 (HP-RR) is an orphan response regulator which is phosphorylation-independent and is essential for growth. HP-RR functions as a cell growth-associated regulator in the absence of post-translational modification. Members of this subfamily contain REC and DNA-binding output domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 51.28  E-value: 6.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVED-IELNVIVARSVLEKlGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREdlpPLVAL 606
Cdd:cd17573    1 ILLIEDdSTLGKEISKGLNEK-GYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSI---VVIVL 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489115238 607 TANVLKDKK-EYLDAGMDDVLSKPLSVPALTAMI 639
Cdd:cd17573   77 SDNPKTEQEiEAFKEGADDYIAKPFDFKVLVARI 110
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
528-640 1.07e-07

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 53.65  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTpGEYDLVLLDIQLPDMTGLDISRELTQKYARedlpPLVALT 607
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELRQTHQT----PVIMLT 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489115238 608 ANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK10955  79 ARGSElDRVLGLELGADDYLPKPFNDRELVARIR 112
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
527-640 1.24e-07

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 50.46  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQkyaREDLPPLVAL 606
Cdd:cd17619    2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELRE---QSEVGIILVT 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489115238 607 TANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17619   79 GRDDEVDRIVGLEIGADDYVTKPFNPRELLVRAK 112
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
388-503 1.30e-07

Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 51.30  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 388 LPHKVITDGTRLRQILWNLISNAVKFTQQ-GQVTVRA--------RYD----------QGDMLH--FEVEDSGIGIPQDE 446
Cdd:cd16938    1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGgGNITFRVfleggsedRSDrdwgpwrpsmSDESVEirFEVEINDSGSPSIE 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489115238 447 QDKIFAmyYQVKDSNGGKPatGTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTV 503
Cdd:cd16938   81 SASMRN--SLNRRYNLSEL--GEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
528-640 1.90e-07

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 50.06  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYARedlpPLVALT 607
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHSHV----PILMLT 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489115238 608 ANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd19939   78 ARTEEmDRVLGLEMGADDYLCKPFSPRELLARVR 111
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
528-629 2.08e-07

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators similar to Pseudomonas savastanoi blue-light-activated histidine kinase; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase (HK)/response regulators contain all the elements of a classical TCS in a single polypeptide chain. Pseudomonas savastanoi blue-light-activated histidine kinase is a photosensitive HK and RR that is involved in increased bacterial virulence upon exposure to light. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 49.65  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPG-EYDLVLLDIQLPD-MTGLDISRELTQKyaREDLPPLVA 605
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPGgMNGSQLAEEARRR--RPDLKVLLT 78
                         90       100
                 ....*....|....*....|....
gi 489115238 606 LTANVLKDKKEYLDAGMdDVLSKP 629
Cdd:cd18161   79 SGYAENAIEGGDLAPGV-DVLSKP 101
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
528-595 2.55e-07

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 49.80  E-value: 2.55e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489115238 528 VLLVEDiELNVIVARS-VLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKY 595
Cdd:cd17550    1 ILIVDD-EEDIRESLSgILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKY 68
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
526-642 3.81e-07

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 49.36  E-value: 3.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 526 LNVLLVEDIELNVIVARSVLEKLGN-SVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLPPLV 604
Cdd:cd17530    1 LRVLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMS 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489115238 605 ALTANVLKDKKEYLDA-GMD--DVLSKPLSVPALTAMIKKY 642
Cdd:cd17530   81 GLDGGILESAETLAGAnGLNllGTLSKPFSPEELTELLTKY 121
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
544-640 4.91e-07

phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is part of MtrA/MtrB (or MtrAB), a highly conserved two-component system (TCS) implicated in the regulation of cell division in the actinobacteria. In unicellular Mycobacterium tuberculosis, MtrAB coordinates DNA replication with cell division and regulates the transcription of resuscitation-promoting factor B. In filamentous Streptomyces venezuelae, it links antibiotic production to sporulation. MtrA belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 49.01  E-value: 4.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 544 VLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQkyarEDLPPLVALTANV-LKDKKEYLDAGM 622
Cdd:cd17626   19 VLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA----ESGVPIVMLTAKSdTVDVVLGLESGA 94
                         90
                 ....*....|....*...
gi 489115238 623 DDVLSKPLSVPALTAMIK 640
Cdd:cd17626   95 DDYVAKPFKPKELVARIR 112
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
527-641 5.76e-07

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 48.81  E-value: 5.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 527 NVLLVEDIELNVIVARSVLEKLG-NSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQ--KYARedlppL 603
Cdd:cd17542    2 KVLIVDDAAFMRMMLKDILTKAGyEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKidPNAK-----V 76
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489115238 604 VALTANVLKDK-KEYLDAGMDDVLSKPLSVPALTAMIKK 641
Cdd:cd17542   77 IMCSAMGQEEMvKEAIKAGAKDFIVKPFQPERVLEAVEK 115
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
528-640 5.86e-07

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 48.91  E-value: 5.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKyarEDLpPLVALT 607
Cdd:cd19938    2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRF---SDV-PIIMVT 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489115238 608 ANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd19938   78 ARVEEiDRLLGLELGADDYICKPYSPREVVARVK 111
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
521-631 8.58e-07

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 50.73  E-value: 8.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 521 MPLPalNVLLVED---IELNVIVArsvLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAr 597
Cdd:PRK11083   1 MQQP--TILLVEDeqaIADTLVYA---LQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHP- 74
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489115238 598 eDLpPLVALTA-NVLKDKKEYLDAGMDDVLSKPLS 631
Cdd:PRK11083  75 -AL-PVIFLTArSDEVDRLVGLEIGADDYVAKPFS 107
orf27 CHL00148
Ycf27; Reviewed
529-640 1.18e-06

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 50.49  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 529 LLVEDIELNVivaRSVLEK----LGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLdisrELTQKYAREDLPPLV 604
Cdd:CHL00148   9 ILVVDDEAYI---RKILETrlsiIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGY----GVCQEIRKESDVPII 81
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489115238 605 ALTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:CHL00148  82 MLTAlGDVSDRITGLELGADDYVVKPFSPKELEARIR 118
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
395-503 1.38e-06

Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana Phytochrome A, B, C, D and E; This family includes the histidine kinase-like ATPase (HATPase) domains of plant red/far-red photoreceptors, the phytochromes, and includes the Arabidopsis thaliana phytochrome family phyA-phyE. Following red light absorption, biologically inactive forms of phytochromes convert to active forms, which rapidly convert back to inactive forms upon far-red light irradiation. Phytochromes can be considered as having an N-terminal photosensory region to which a bilin chromophore is bound, and a C-terminal output region, which includes the HATPase domain represented here, and is involved in dimerization and presumably contributes to relaying the light signal to downstream signaling events.


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 47.65  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 395 DGTRLRQILWNLISNAVKFTQ--QGQVTVRARYDQ---GDMLH-----FEVEDSGIGIPQDEQDKIFamyyqvkdsNGGK 464
Cdd:cd16932    3 DQIRLQQVLADFLLNAVRFTPspGGWVEIKVSPTKkqiGDGVHvihleFRITHPGQGLPEELVQEMF---------EENQ 73
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489115238 465 PATGTGIGLAVSKRLAKNMGGDITVSSQAGKgSIFTLTV 503
Cdd:cd16932   74 WTTQEGLGLSISRKLVKLMNGDVRYLREAGR-SYFLITL 111
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
155-221 1.83e-06

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 45.85  E-value: 1.83e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489115238   155 SFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETDEKVFR 221
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
528-640 2.17e-06

phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains; Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 47.24  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFT--PGEYDLVLLDIQLPDMTGLDIsreltQKYARE--DLpPL 603
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRenKDEFDLVITDVHMPDMDGFEF-----LELIRLemDL-PV 74
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489115238 604 VALTANVLKDK-KEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17584   75 IMMSADGSTSTvMKGLAHGACDYLLKPVSIEDLKNIWQ 112
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
528-628 2.23e-06

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 47.12  E-value: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELnVIVA-RSVLEKLGNS--VDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYARedlPPLV 604
Cdd:cd17535    1 VLIVDDHPL-VREGlRRLLESEPDIevVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPD---LKVI 76
                         90       100
                 ....*....|....*....|....*
gi 489115238 605 ALTANVLKDK-KEYLDAGMDDVLSK 628
Cdd:cd17535   77 VLTAHDDPEYvLRALKAGAAGYLLK 101
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
416-503 2.26e-06

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: 48.73  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 416 QGQVTVRARYdQGDMLHFEVEDSGIGI-----------------------PQDEQDKI-----FAMYYQVKDsnggkpAT 467
Cdd:cd16916   69 EGTITLRAEH-QGNQVVIEVSDDGRGIdrekirekaierglitadeaatlSDDEVLNLifapgFSTAEQVTD------VS 141
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 468 GTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTV 503
Cdd:cd16916  142 GRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRL 177
PRK15479 PRK15479
transcriptional regulator TctD;
526-640 2.39e-06

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 49.33  E-value: 2.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 526 LNVLLVED-IELNVIVARSVLEKlGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKyaREDLPPLV 604
Cdd:PRK15479   1 MRLLLAEDnRELAHWLEKALVQN-GFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKR--GQTLPVLL 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489115238 605 aLTANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK15479  78 -LTARSaVADRVKGLNVGADDYLPKPFELEELDARLR 113
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
528-640 2.41e-06

phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase/response regulators; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase/response regulators contain all the elements of a classical TCS in a single polypeptide chain. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 46.94  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLPPLVALT 607
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489115238 608 ANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIK 113
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
545-593 2.47e-06

receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus pneumoniae RitR (Repressor of iron transport Regulator, formerly RR489) is an orphan two-component signal transduction response regulator that is required for lung pathogenicity. It acts to repress iron uptake via binding the pneumococcal iron uptake (Piu) transporter promoter. Members of this subfamily contain REC and DNA-binding output domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. However, members of this family do not contain the phosphorylatable aspartic acid residue and are phosphorylation-independent.


Pssm-ID: 381149 [Multi-domain]  Cd Length: 110  Bit Score: 46.70  E-value: 2.47e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489115238 545 LEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQ 593
Cdd:cd19922   18 LQKEGYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAEKLSR 66
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
526-641 2.57e-06

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 50.80  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 526 LNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELtqKYAREDLPPLVA 605
Cdd:PRK10365   6 IDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEI--KALNPAIPVLIM 83
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 606 LTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIKK 641
Cdd:PRK10365  84 TAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
350-510 4.47e-06

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 48.85  E-value: 4.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 350 QLDNQPVDFTSFMADLENLSGLQAQQKGLRFVLE---PTLPLPHKVITDGTRlrqILWNLISNAVKFTQQGQVTVRARYD 426
Cdd:COG4585  114 GLRPPALDDLGLAAALEELAERLLRAAGIRVELDvdgDPDRLPPEVELALYR---IVQEALTNALKHAGATRVTVTLEVD 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 427 qGDMLHFEVEDSGIGIPQDEqdkifamyyqvkdsnggkpATGTGIGLAVSKRLAKNMGGDITVSSQAGKGsiFTLTVHAP 506
Cdd:COG4585  191 -DGELTLTVRDDGVGFDPEA-------------------APGGGLGLRGMRERAEALGGTLTIGSAPGGG--TRVRATLP 248

                 ....
gi 489115238 507 AVAE 510
Cdd:COG4585  249 LAAA 252
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
544-641 4.93e-06

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 46.14  E-value: 4.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 544 VLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLPPLVALTANVLKDKKEYLDAGMD 623
Cdd:cd17562   19 TLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILMLTTESSDEKKQEGKAAGAT 98
                         90
                 ....*....|....*...
gi 489115238 624 DVLSKPLSVPALTAMIKK 641
Cdd:cd17562   99 GWLVKPFDPEQLLEVVKK 116
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
528-642 5.11e-06

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 46.01  E-value: 5.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELtqKYAREDLPPLVALT 607
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRM--KVIDENIRVIIMTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489115238 608 ANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIKKY 642
Cdd:cd17553   81 YGELDMIQESKELGALTHFAKPFDIDEIRDAVKKY 115
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
395-501 5.51e-06

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 49.83  E-value: 5.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 395 DGTRLRQILWNLISNAVKF---TQQGQVTVRARY-DQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSNGGKpatgTG 470
Cdd:PRK15053 429 DSTEFAAIVGNLLDNAFEAslrSDEGNKIVELFLsDEGDDVVIEVADQGCGVPESLRDKIFEQGVSTRADEPGE----HG 504
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489115238 471 IGLAVSKRLAKNMGGDITVSSQAGKGSIFTL 501
Cdd:PRK15053 505 IGLYLIASYVTRCGGVITLEDNDPCGTLFSI 535
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
528-641 5.77e-06

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 45.90  E-value: 5.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTqkyAREDLpPLVALT 607
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIR---ARSDV-PIIIIS 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 608 ANVLK--DKKEYLDAGMDDVLSKPLSVPALTAMIKK 641
Cdd:cd17594   78 GDRRDeiDRVVGLELGADDYLAKPFGLRELLARVRA 113
PRK10610 PRK10610
chemotaxis protein CheY;
526-644 7.84e-06

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 46.12  E-value: 7.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 526 LNVLLVEDIELNVIVARSVLEKLG-NSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLPPLV 604
Cdd:PRK10610   6 LKFLVVDDFSTMRRIVRNLLKELGfNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLM 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489115238 605 aLTANVlkdKKEYL----DAGMDDVLSKPLSVPALTAMIKKYWD 644
Cdd:PRK10610  86 -VTAEA---KKENIiaaaQAGASGYVVKPFTAATLEEKLNKIFE 125
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
528-629 8.73e-06

phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR and similar proteins; Pseudomonas aeruginosa PilR is the response regulator of the PilS/PilR two-component regulatory system (PilSR TCS) that acts in conjunction with sigma-54 to regulate the expression of type 4 pilus (T4P) major subunit PilA. In addition, the PilSR TCS regulates flagellum-dependent swimming motility and pilus-dependent twitching motility. PilR contains an N-terminal REC domain, a central sigma-54 interaction domain, and a C-terminal Fis-type helix-turn-helix DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 44.84  E-value: 8.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDiELNVI-VARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAreDLPPLVAL 606
Cdd:cd19926    1 VLVVDD-EPDIReLLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLP--QTPVAVIT 77
                         90       100
                 ....*....|....*....|...
gi 489115238 607 TANVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd19926   78 AYGSLDTAIEALKAGAFDFLTKP 100
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
528-629 8.74e-06

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 45.13  E-value: 8.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDiELNVIVARS-VLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKyarEDLPPLVAL 606
Cdd:cd19936    1 IALVDD-DRNILTSVSmALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQK---STLPVIFLT 76
                         90       100
                 ....*....|....*....|...
gi 489115238 607 TANVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd19936   77 SKDDEIDEVFGLRMGADDYITKP 99
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
527-629 1.21e-05

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 45.08  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 527 NVLLVEDielnVIVARSVLEKLGNS------VDVAMTGKAALEM---FTPgeyDLVLLDIQLPDMTGLdisrELTQKYAR 597
Cdd:cd17541    2 RVLIVDD----SAVMRKLLSRILESdpdievVGTARDGEEALEKikeLKP---DVITLDIEMPVMDGL----EALRRIMA 70
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489115238 598 EDLPPLVALTANVLKDKK---EYLDAGMDDVLSKP 629
Cdd:cd17541   71 ERPTPVVMVSSLTEEGAEitlEALELGAVDFIAKP 105
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
286-480 1.22e-05

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 48.04  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 286 FISTISHELRTPLNGIvglsRILLdtdltaeqEKYLKTIHVSAVTLgnifndIIDMDKMERRKVQL-------------D 352
Cdd:PRK10755 140 FTADVAHELRTPLAGI----RLHL--------ELLEKQHHIDVAPL------IARLDQMMHTVEQLlqlaragqsfssgH 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 353 NQPVDFTS--FMADLENLSGLqAQQKGLRFVLePTLPLPHKVITDGTRLRQILWNLISNAVKFTQQG-QVTVRARYDQGd 429
Cdd:PRK10755 202 YQTVKLLEdvILPSQDELSEM-LEQRQQTLLL-PESAADITVQGDATLLRLLLRNLVENAHRYSPEGsTITIKLSQEDG- 278
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489115238 430 MLHFEVEDSGIGIPQD---EQDKIFamyyQVKDSNGGkpatGTGIGLAVSKRLA 480
Cdd:PRK10755 279 GAVLAVEDEGPGIDESkcgELSKAF----VRMDSRYG----GIGLGLSIVSRIT 324
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
526-591 1.52e-05

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 45.27  E-value: 1.52e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489115238 526 LNVLLVEDIELNVIVARSVLEKLGN--SVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISREL 591
Cdd:COG2197    2 IRVLIVDDHPLVREGLRALLEAEPDieVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
528-629 1.60e-05

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 44.82  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFT--PgEYDLVLLDIQLPDMTGLDISRELTQKYAREDLPPL-- 603
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEqhP-DIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIgi 81
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489115238 604 -----VALTANVLKdkkeyldAGMDDVLSKP 629
Cdd:cd17544   82 sasgdNALSARFIK-------AGANDFLTKP 105
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
526-629 1.72e-05

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 44.54  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 526 LNVLLVEDIELNVIVARSVLEKLG--NSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLppL 603
Cdd:cd19925    1 INVLIVEDDPMVAEIHRAYVEQVPgfTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDV--I 78
                         90       100
                 ....*....|....*....|....*.
gi 489115238 604 VALTANVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd19925   79 VVTAANDVETVREALRLGVVDYLIKP 104
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
180-268 1.85e-05

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


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 43.99  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  180 CNRAMELLTGKSEKQLVNLKPADVYSPEAAEKVIETDEKVFRHNVSLTYEqwLDYPDGRKACFEIRKVPYYDRVGKRHGL 259
Cdd:pfam13426   7 VNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVREFEVV--LYRKDGEPFPVLVSLAPIRDDGGELVGI 84

                  ....*....
gi 489115238  260 MGFGRDITE 268
Cdd:pfam13426  85 IAILRDITE 93
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-503 2.11e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain.


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 43.91  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFTQQGQVTVRARYDQGDMLHFEVEDSGIGIPQDEQDKIFAMYYQVKDSnggKPATGTGIGLAVSKR 478
Cdd:cd16923    1 LQRVFSNLLSNAIKYSPENTRIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS---RNTEGAGLGLSIAKA 77
                         90       100
                 ....*....|....*....|....*
gi 489115238 479 LAKNMGGDITVSSQaGKGSIFTLTV 503
Cdd:cd16923   78 IIELHGGSASAEYD-DNHDLFKVRL 101
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
524-641 2.26e-05

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 47.54  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 524 PALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTqkyAREDLPPL 603
Cdd:PRK11361   3 AINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMR---SHETRTPV 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489115238 604 VALTANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIKK 641
Cdd:PRK11361  80 ILMTAYAeVETAVEALRCGAFDYVIKPFDLDELNLIVQR 118
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
528-629 2.81e-05

phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 43.91  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPG---------EYDLVLLDIQLPDMTGLDISRELTQKYARE 598
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLakegndlskELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489115238 599 DLPPLVALTANVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
526-639 3.95e-05

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 43.56  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 526 LNVLLVEDIELNVIVARSVLEKLGNSV-DVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQkyarEDLPPLV 604
Cdd:cd19932    1 VRVLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITS----ENIAPIV 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 605 ALTANVLKDKKEYL-DAGMDDVLSKPLSVPALTAMI 639
Cdd:cd19932   77 LLTAYSQQDLVERAkEAGAMAYLVKPFSESDLIPAI 112
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
77-153 4.06e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.68  E-value: 4.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489115238  77 VEQLEESRQRLSRLVQKLEEMRERDLKLNVQLKDNIAQLNQEIVEREKAEAERQETFEQLKVEIKEREEAQIQLEQQ 153
Cdd:COG4942  152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
527-596 4.49e-05

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 43.20  E-value: 4.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489115238 527 NVLLVEDIE-LNVIVARSvLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYA 596
Cdd:cd17563    2 SLLLVDDDEvFAERLARA-LERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQP 71
PRK10766 PRK10766
two-component system response regulator TorR;
527-640 4.95e-05

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 45.41  E-value: 4.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 527 NVLLVEDiELnVIVARSV--LEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTqkyAREDLPPLV 604
Cdd:PRK10766   4 HILVVED-EP-VTRARLQgyFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELR---SRSTVGIIL 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 605 ALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK10766  79 VTGRTDSIDRIVGLEMGADDYVTKPLELRELLVRVK 114
ompR PRK09468
osmolarity response regulator; Provisional
518-640 5.53e-05

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 45.35  E-value: 5.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 518 DDDMPLPALnvllvedielnvivARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKyar 597
Cdd:PRK09468  12 DDDMRLRAL--------------LERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQ--- 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489115238 598 EDLPPLVALTANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK09468  75 NNPTPIIMLTAKGEEvDRIVGLEIGADDYLPKPFNPRELLARIR 118
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
528-641 8.53e-05

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 42.71  E-value: 8.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELnvivARSVL------EKLG-NSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYARedl 600
Cdd:cd17536    1 VLIVDDEPL----IREGLkklidwEELGfEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPD--- 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489115238 601 PPLVALTANvlkDKKEY----LDAGMDDVLSKPLSVPALTAMIKK 641
Cdd:cd17536   74 IKIIILSGY---DDFEYaqkaIRLGVVDYLLKPVDEEELEEALEK 115
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
555-604 9.78e-05

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 42.52  E-value: 9.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489115238 555 AMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQkyarEDLPPLV 604
Cdd:cd17532   30 AENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSK----LAKPPLI 75
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-506 9.95e-05

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: 41.77  E-value: 9.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 399 LRQILWNLISNAVKFTQQGQVTVRARYDqGDMLHFEVEDSGIGIPqdeqdkifamyyqvkdsnGGKPATGTGIGLAVSK- 477
Cdd:cd16917    1 LYRIVQEALTNALKHAGASRVRVTLSYT-ADELTLTVVDDGVGFD------------------GPAPPGGGGFGLLGMRe 61
                         90       100
                 ....*....|....*....|....*....
gi 489115238 478 RLAKnMGGDITVSSQAGKGsiFTLTVHAP 506
Cdd:cd16917   62 RAEL-LGGTLTIGSRPGGG--TRVTARLP 87
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
525-640 1.13e-04

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 44.32  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 525 ALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAREDLPPLV 604
Cdd:PRK10161   2 ARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVM 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115238 605 ALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK10161  82 LTARGEEEDRVRGLETGADDYITKPFSPKELVARIK 117
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
401-491 1.41e-04

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 45.01  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 401 QILWNLISNAVKFTQQGqVTVRARYDqGDMLHFEVEDSGIGIPQDEQDKIFAmyyqvkdsNGGKPAT---GTGIGLAVSK 477
Cdd:PRK10815 381 EVMGNVLDNACKYCLEF-VEISARQT-DEHLHIVVEDDGPGIPESKRELIFD--------RGQRADTlrpGQGLGLSVAR 450
                         90
                 ....*....|....
gi 489115238 478 RLAKNMGGDITVSS 491
Cdd:PRK10815 451 EITEQYEGKISAGD 464
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
78-153 2.32e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 2.32e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489115238  78 EQLEESRQRLSRLVQKLEEM---RERDLKLNVQLKDNIAQLNQEIVEREKAEAERQETFEQLKVEIKEREEAQIQLEQQ 153
Cdd:COG1196  281 LELEEAQAEEYELLAELARLeqdIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
77-153 2.46e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.46e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489115238  77 VEQLEESRQRLSRLVQKLEEMRERDLKLNVQLKDNIAQLNQEIVEREKAEAERQETFEQLKVEIKEREEAQIQLEQQ 153
Cdd:COG1196  297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
73-163 2.57e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  73 LSVVVEQLEESRQRLSRLVQKLEEMRERDLKLNVQLKDN---IAQLNQEIVEREKAEAERQETFEQlkveikereeaQIQ 149
Cdd:COG3883   25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALqaeIDKLQAEIAEAEAEIEERREELGE-----------RAR 93
                         90
                 ....*....|....
gi 489115238 150 LEQQSSFLRSFLDA 163
Cdd:COG3883   94 ALYRSGGSVSYLDV 107
PRK11173 PRK11173
two-component response regulator; Provisional
527-636 3.09e-04

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 43.08  E-value: 3.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQkyaREDLpPLVAL 606
Cdd:PRK11173   5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELRE---QANV-ALMFL 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489115238 607 TA---NVlkDKKEYLDAGMDDVLSKPLSVPALT 636
Cdd:PRK11173  81 TGrdnEV--DKILGLEIGADDYITKPFNPRELT 111
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
545-641 3.97e-04

phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response regulators contain an N-terminal receiver domain (REC) and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. The Sinorhizobium meliloti two-component system FixL/FixJ regulates nitrogen fixation in response to oxygen during symbiosis. Under microaerobic conditions, the kinase FixL phosphorylates the response regulator FixJ resulting in the regulation of nitrogen fixation genes such as nifA and fixK. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 40.65  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 545 LEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQkyaREDLPPLVALTAN------VlkdkkEYL 618
Cdd:cd17537   20 LRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLA---RGSNIPIIFITGHgdvpmaV-----EAM 91
                         90       100
                 ....*....|....*....|...
gi 489115238 619 DAGMDDVLSKPLSVPALTAMIKK 641
Cdd:cd17537   92 KAGAVDFLEKPFRDQVLLDAIEQ 114
PRK10816 PRK10816
two-component system response regulator PhoP;
526-640 4.77e-04

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 42.42  E-value: 4.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 526 LNVLLVEDielNVIVARSV---LEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKyaREDLPP 602
Cdd:PRK10816   1 MRVLVVED---NALLRHHLkvqLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSN--DVSLPI 75
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489115238 603 LVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK10816  76 LVLTARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQ 113
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
56-163 5.18e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 5.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  56 IRSIFFGLLITPWAVYFLSVVVEQLEESRQRLSRLVQKLEEMRERDLKLNVQLKDNIAQLNQEIVEREKA----EAERQE 131
Cdd:COG4942    1 MRKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiralEQELAA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489115238 132 TFEQLKVEIKEREEAQIQLEQQSSFLRSFLDA 163
Cdd:COG4942   81 LEAELAELEKEIAELRAELEAQKEELAELLRA 112
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
406-503 5.25e-04

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: 40.10  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 406 LISNAVK--FT---QQGQVTVRARYDQGdMLHFEVEDSGIGIPQDEQDKIfamyyqvkdsnGGKPAT---GTGIGLA-VS 476
Cdd:cd16957    9 LVENAIRhaFPkrkENNEVRVVVKKDQH-KVHVSVSDNGQGIPEERLDLL-----------GKTTVTsekGTGTALEnLN 76
                         90       100
                 ....*....|....*....|....*....
gi 489115238 477 KRLAKNMG--GDITVSSQAGKGSIFTLTV 503
Cdd:cd16957   77 RRLIGLFGseACLHIESEVHGGTEVWFVI 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
78-153 5.97e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 5.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489115238  78 EQLEESRQRLSRLVQKLEEMRERDLKLNVQlkdnIAQLNQEIVEREKAEAERQETFEQLKVEIKEREEAQIQLEQQ 153
Cdd:COG1196  267 AELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
73-153 7.90e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 7.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  73 LSVVVEQLEESRQRLSRLVQKLEEMRERDLKLNVQLKDNIAQLNQEIVEREKAEAERQETFEQLKVEIKEREEAQIQLEQ 152
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                 .
gi 489115238 153 Q 153
Cdd:COG1196  384 L 384
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
528-629 7.93e-04

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 39.67  E-value: 7.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDielNVIVARSV---LEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYaREDLPPLV 604
Cdd:cd19927    1 ILLVDD---DPGIRLAVkdyLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNA-DFDTIPVI 76
                         90       100
                 ....*....|....*....|....*.
gi 489115238 605 ALTANVL-KDKKEYLDAGMDDVLSKP 629
Cdd:cd19927   77 FLTAKGMtSDRIKGYNAGCDGYLSKP 102
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
360-504 8.54e-04

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 39.90  E-value: 8.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 360 SFMADLENLSglQAQQKGLRFVLEptLPLPHKVITDgtrLRQILWNLISNAVKFTQQ----GQVTVRARYDqGDMLHFEV 435
Cdd:COG2172    3 SLPADLEDLG--LARRAVRALLRE--LGLDEDDADD---LVLAVSEAVTNAVRHAYGgdpdGPVEVELELD-PDGLEIEV 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489115238 436 EDSGIGIPQDEqdkifamyyqVKDSNGgkPATGTGIGLAVSKRLAKnmggDITVSSQAGkGSIFTLTVH 504
Cdd:COG2172   75 RDEGPGFDPED----------LPDPYS--TLAEGGRGLFLIRRLMD----EVEYESDPG-GTTVRLVKR 126
PRK13435 PRK13435
response regulator; Provisional
521-631 8.77e-04

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 40.42  E-value: 8.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 521 MPLPALNVLLVEDIELNVIVARSVLEKLG-NSVDVAMTGKAALEMFTPGEYDLVLLDIQLPD-MTGLDISRELTQKYARE 598
Cdd:PRK13435   1 MFLRQLKVLIVEDEALIALELEKLVEEAGhEVVGIAMSSEQAIALGRRRQPDVALVDVHLADgPTGVEVARRLSADGGVE 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489115238 599 dlppLVALTANVlkDKKEYLDAGMDDVLSKPLS 631
Cdd:PRK13435  81 ----VVFMTGNP--ERVPHDFAGALGVIAKPYS 107
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
528-640 9.33e-04

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 39.57  E-value: 9.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQkyaREDLPPLVALT 607
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQ---ISNVPIIFISS 77
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489115238 608 ANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd18159   78 RDDNMDQVMAINMGGDDYITKPFDLDVLLAKIK 110
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
78-153 9.61e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 9.61e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489115238  78 EQLEESRQRLSRLVQKLEEMRERDLKLNVQLKD---NIAQLNQEIVEREKAEAERQETFEQLKVEIKEREEAQIQLEQQ 153
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEaeaELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
416-503 1.14e-03

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 42.48  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 416 QGQVTVRARYdQGDMLHFEVEDSGIGI---------------PQDEQDK---------IFAmyyqvkdsnggkP----AT 467
Cdd:COG0643  308 TGTITLSAYH-EGGRVVIEVSDDGRGLdlekirakaiekgliTAEEAAAlsdeellelIFA------------PgfstAE 374
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489115238 468 ------GTGIGLAVSKRLAKNMGGDITVSSQAGKGSIFTLTV 503
Cdd:COG0643  375 evtdlsGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRL 416
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
528-627 1.51e-03

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 41.16  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVED-IELNVIVArSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKYAredlPPLVAL 606
Cdd:PRK10701   4 IVFVEDdAEVGSLIA-AYLAKHDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQ----GPIVLL 78
                         90       100
                 ....*....|....*....|.
gi 489115238 607 TAnvlkdkkeyLDAGMDDVLS 627
Cdd:PRK10701  79 TS---------LDSDMNHILA 90
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
73-158 1.53e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  73 LSVVVEQLEESRQRLSRLVQKLEEMRERDLKLNVQ---LKDNIAQLNQEIVEREKAEAERQETFEQLKVEIKEREEAQIQ 149
Cdd:COG4372   75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEaeeLQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154

                 ....*....
gi 489115238 150 LEQQSSFLR 158
Cdd:COG4372  155 LEEQLESLQ 163
PRK12704 PRK12704
phosphodiesterase; Provisional
78-155 1.54e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  78 EQLE-ESRQRLSRLVQKLEEMRERDLKLNVQLkDNIAQLNQEIVEREKAEAERQETFEQLKVEIKEREEAQIQ-LEQQSS 155
Cdd:PRK12704  71 NEFEkELRERRNELQKLEKRLLQKEENLDRKL-ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQeLERISG 149
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
78-163 2.39e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  78 EQLEESRQRLSRLVQKLEEMRERDLKLNVQLKDNIAQLNQEIVEREKAEAERQETFEQLKVEIKEREEAQIQLEQQSSFL 157
Cdd:COG1196  403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                 ....*.
gi 489115238 158 RSFLDA 163
Cdd:COG1196  483 LEELAE 488
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
528-593 2.51e-03

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 38.25  E-value: 2.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489115238 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALE-MFTPGEYDLVLLDIQLPDMTGLDISRELTQ 593
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEkLQQGKDIDIVVTDIVMPEMDGIELAREARK 68
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
78-158 2.53e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 39.25  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238   78 EQLEESRQRLSRLVQKLEEMRERdlklnvQLKDNIAQLNQEIVEREKAEAERQETFEQLK--VEIKEREEA-QIQLEQQS 154
Cdd:pfam05672  50 RRAEEERARREEEARRLEEERRR------EEEERQRKAEEEAEEREQREQEEQERLQKQKeeAEAKAREEAeRQRQEREK 123

                  ....
gi 489115238  155 SFLR 158
Cdd:pfam05672 124 IMQQ 127
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
78-163 2.81e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238  78 EQLEESRQRLSRLVQKLEEMRERDLKLNVQLKDNIAQLNQEIVEREKAEAERQETFEQLKVEIKEREEAQIQLEQQSSFL 157
Cdd:COG1196  302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                 ....*.
gi 489115238 158 RSFLDA 163
Cdd:COG1196  382 EELAEE 387
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
397-496 3.07e-03

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 39.25  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 397 TRLRQILWNLISNAVKFTQQGQVT---------VRARYDQGDMLhFEVEDSGIGIPQDEQDKIFAMYY-----QVKDS-- 460
Cdd:cd16929   42 SHLYYILFELLKNAMRATVESHGDdsddlppikVTVAKGDEDLT-IKISDRGGGIPREDLARLFSYMYstapqPSLDDfs 120
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489115238 461 -----NGGKPATGTGIGLAVSKRLAKNMGGDITVSSQAGKG 496
Cdd:cd16929  121 dlisgTQPSPLAGFGYGLPMSRLYAEYFGGDLDLQSMEGYG 161
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
527-595 3.13e-03

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 38.15  E-value: 3.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 527 NVLLVEDiELNVIVA-RSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKY 595
Cdd:cd17569    2 TILLVDD-EPNILKAlKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERY 70
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
542-608 3.55e-03

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 39.31  E-value: 3.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489115238 542 RSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTqkyAREDLPPLVALTA 608
Cdd:COG4566   16 AFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELA---ARGSPLPVIFLTG 79
PRK10693 PRK10693
two-component system response regulator RssB;
554-631 3.72e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 39.97  E-value: 3.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489115238 554 VAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLDISRELTQKyaREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLS 631
Cdd:PRK10693   2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNR--GDQTPVLVISATENMADIAKALRLGVQDVLLKPVK 77
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
570-640 5.40e-03

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 39.28  E-value: 5.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489115238 570 YDLVLLDIQLPDMTGLDISRELTQkyaREDLpPLVALTANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK10710  55 PDLILLDLMLPGTDGLTLCREIRR---FSDI-PIVMVTAKIEEiDRLLGLEIGADDYICKPYSPREVVARVK 122
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
395-497 5.63e-03

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 37.35  E-value: 5.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 395 DGTRLRQILWNLISNAVKFTQQGQVTVRARYDQGDM-LHFEVEDSGIGIPQDEQdkifAMyyqvkdSNGGKPATGTGIGL 473
Cdd:cd16934   22 RQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVaLEILAVDQGPGIADVDE----AL------RDGFSTGGGLGLGL 91
                         90       100
                 ....*....|....*....|....
gi 489115238 474 AVSKRLAknmgGDITVSSQAGKGS 497
Cdd:cd16934   92 GGVRRLA----DEFDLHSAPGRGT 111
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
553-629 6.27e-03

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 36.71  E-value: 6.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489115238 553 DVAMTGKAALEM--FTPGEYDLVLLDIQLPDMTGLDISRELtqKYAREDLPPLVALTANVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd19928   24 EVRTTGNAATLWrwVEEGEGDLVITDVVMPDENGLDLIPRI--KKARPDLPIIVMSAQNTLMTAVKAAERGAFEYLPKP 100
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
528-630 6.95e-03

phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and similar proteins; Type-A response regulators of Arabidopsis (ARRs) are involved in cytokinin signaling, which involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Type-A ARRs function downstream of and are regulated by type-B ARRs, which are a class of MYB-type transcription factors. As primary cytokinin response genes, type-A ARRs act as redundant negative feedback regulators of cytokinin signaling by inactivating the phosphorelay. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-A ARRs are similar in domain structure to CheY, in that they lack a typical output domain and only contain a stand-alone receiver (REC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 37.35  E-value: 6.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 528 VLLVEDielnVIVARSVLEKLGNSVDVAMT----GKAALEM-----------FTPGEYDLVLLDIQLPDMTGLDISRELT 592
Cdd:cd17581    1 VLAVDD----SLVDRKVIERLLRISSCRVTavdsGKRALEFlgledeedssnFNEPKVNMIITDYCMPGMTGYDLLKKVK 76
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489115238 593 QKYAREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPL 630
Cdd:cd17581   77 ESSALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPV 114
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
540-642 7.28e-03

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 37.13  E-value: 7.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115238 540 VARSVLEKLGNSVDVAMTGKAALEMFTPGEYDLVLLDIQLPDMTGLdisrELTQKYAREDLPPLV-ALTANVLKDKKE-Y 617
Cdd:cd17593   16 LARALPADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGY----EVLEALPVEQLETKViVVSGDVQPEAKErV 91
                         90       100
                 ....*....|....*....|....*
gi 489115238 618 LDAGMDDVLSKPLSVPALTAMIKKY 642
Cdd:cd17593   92 LELGALAFLKKPFDPEKLAQLLEEL 116
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
78-153 8.48e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 8.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489115238  78 EQLEESRQRLSRLVQKLEEMRERDLKLNVQLKDNIAQLNQEIVEREKAEAER---QETFEQLKVEIKEREEAQIQLEQQ 153
Cdd:COG1196  253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIarlEERRRELEERLEELEEELAELEEE 331
 
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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