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Conserved domains on  [gi|446732494|ref|WP_000809750|]
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MULTISPECIES: aerobic respiration two-component sensor histidine kinase ArcB [Escherichia]

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: 1558.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494   1 MKQIRLLAQYYVDLMMKLGLVRFSMLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
Cdd:PRK11091   1 MKQIRLLAQYYVDLMVKLGLVRFSLLLALALVVLAMVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  81 EESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQLEQQSSFLRSF 160
Cdd:PRK11091  81 EESRQRLSRLVAKLEEMRERDLELNVQLKDNIAQLNQEIAEREKAEEARQEAFEQLKNEIKEREETQIELEQQSSLLRSF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 161 LDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDEKVFRHNVSLSYEQWLQYPDGRKA 240
Cdd:PRK11091 161 LDASPDLVYYRNEDGEFSGCNRAMELLTGKSEKQLIGLTPKDVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 241 CFEIRKVPYYDRVGKRHGLMGFGRDITERKHYQDALEQASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLNAEQEKY 320
Cdd:PRK11091 241 CFELRKVPFYDRVGKRHGLMGFGRDITERKRYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKY 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 321 LKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQPIDFTGFLADLENLSGLQAQQKGLRFVMEPTLPLPHQVITDGTRLR 400
Cdd:PRK11091 321 LKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLR 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 401 QVLWNLISNAVKFTQQGKVEVRVRYDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGKPATGTGIGLAVSRRLA 480
Cdd:PRK11091 401 QILWNLISNAVKFTQQGGVTVRVRYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKPATGTGIGLAVSKRLA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 481 RDMGGDISVSSVPGQGSVFTLTVRAPAVAEEVDDVFEEDDLPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKA 560
Cdd:PRK11091 481 QAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVEDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKE 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 561 ALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRDDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK11091 561 ALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 641 KFWDTQDEEESTVAPDDNSKS-QELLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYMSVLQSNLTARDQKGIVEEGHKI 719
Cdd:PRK11091 641 KFWDTQDDEESTVTTEESSKAnEALLDIPMLEQYVELVGPKLITDSLAVFEKMMPGYLSVLDSNLTARDQKGIVEEAHKI 720
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446732494 720 KGAAGSVGLRHLQQLGQQIQSPDLPAWEDNVGEWIEEMKQEWRHDVEVLKAWVAKNGKK 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: 1558.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494   1 MKQIRLLAQYYVDLMMKLGLVRFSMLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
Cdd:PRK11091   1 MKQIRLLAQYYVDLMVKLGLVRFSLLLALALVVLAMVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  81 EESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQLEQQSSFLRSF 160
Cdd:PRK11091  81 EESRQRLSRLVAKLEEMRERDLELNVQLKDNIAQLNQEIAEREKAEEARQEAFEQLKNEIKEREETQIELEQQSSLLRSF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 161 LDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDEKVFRHNVSLSYEQWLQYPDGRKA 240
Cdd:PRK11091 161 LDASPDLVYYRNEDGEFSGCNRAMELLTGKSEKQLIGLTPKDVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 241 CFEIRKVPYYDRVGKRHGLMGFGRDITERKHYQDALEQASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLNAEQEKY 320
Cdd:PRK11091 241 CFELRKVPFYDRVGKRHGLMGFGRDITERKRYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKY 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 321 LKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQPIDFTGFLADLENLSGLQAQQKGLRFVMEPTLPLPHQVITDGTRLR 400
Cdd:PRK11091 321 LKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLR 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 401 QVLWNLISNAVKFTQQGKVEVRVRYDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGKPATGTGIGLAVSRRLA 480
Cdd:PRK11091 401 QILWNLISNAVKFTQQGGVTVRVRYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKPATGTGIGLAVSKRLA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 481 RDMGGDISVSSVPGQGSVFTLTVRAPAVAEEVDDVFEEDDLPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKA 560
Cdd:PRK11091 481 QAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVEDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKE 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 561 ALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRDDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK11091 561 ALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 641 KFWDTQDEEESTVAPDDNSKS-QELLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYMSVLQSNLTARDQKGIVEEGHKI 719
Cdd:PRK11091 641 KFWDTQDDEESTVTTEESSKAnEALLDIPMLEQYVELVGPKLITDSLAVFEKMMPGYLSVLDSNLTARDQKGIVEEAHKI 720
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446732494 720 KGAAGSVGLRHLQQLGQQIQSPDLPAWEDNVGEWIEEMKQEWRHDVEVLKAWVAKNGKK 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 1.37e-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: 346.00  E-value: 1.37e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  277 EQASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQPI 356
Cdd:TIGR02956 458 EEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPF 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  357 DFTGFLADLENLSGLQAQQKGLRFVMEPTLPLPHQVITDGTRLRQVLWNLISNAVKFTQQGKVEVRVRYDKGEMLHFEVA 436
Cdd:TIGR02956 538 DLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDSSLLFEVE 617
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  437 DSGIGIPQEEQDKIFAMYYQVkdsQGGKPATGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLTVRAPaVAEEVDDVF 516
Cdd:TIGR02956 618 DTGCGIAEEEQATLFDAFTQA---DGRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLT-RGKPAEDSA 693
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  517 EEDDLPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYS 596
Cdd:TIGR02956 694 TLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIYG 773
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  597 RDDLPPLVALTANVLKDKKE-YLDAGMDDVLSKPLSVPALTAMIKKFWDTQ---------------------DEEESTVA 654
Cdd:TIGR02956 774 AKNEVKFIAFSAHVFNEDVAqYLAAGFDGFLAKPVVEEQLTAMIAVILAGGksnteapvlsaspsfdsasviENAQADDI 853
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  655 PDDNSKSQELLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYMSVLQSNLTARDQKGIVEEGHKIKGAAGSVGLRHLQQL 734
Cdd:TIGR02956 854 PESNQASEFLLDEEQLQQDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQL 933
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 446732494  735 GQQIQSPDLPAWEDnvGEWIEEMKQEWRHDVEVLKAW 771
Cdd:TIGR02956 934 CQQLEKQGKTGALE--LSDIDEIKQAWQASKTALDQW 968
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
275-502 2.93e-70

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 233.65  E-value: 2.93e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 275 ALEQASRDKTTFISTISHELRTPLNGIVGLSRILLDTdLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQ 354
Cdd:COG0642  102 LLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPE 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 355 PIDFTGFLADLENLSGLQAQQKGLRFVMEPTLPLPHqVITDGTRLRQVLWNLISNAVKFTQQG-KVEVRVRYDkGEMLHF 433
Cdd:COG0642  181 PVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPT-VRGDPDRLRQVLLNLLSNAIKYTPEGgTVTVSVRRE-GDRVRI 258
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446732494 434 EVADSGIGIPQEEQDKIFAMYYQVKDSQGGKpatGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLT 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 ...
399-503 1.15e-45

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: 158.81  E-value: 1.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVKFTQQGKVEVRVRYDKGE----MLHFEVADSGIGIPQEEQDKIFAMYYQVkDSQGGKPATGTGIGLA 474
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEedgvQLRFSVEDTGIGIPEEQQARLFEPFSQA-DSSTTRKYGGTGLGLA 79
                         90       100
                 ....*....|....*....|....*....
gi 446732494 475 VSRRLARDMGGDISVSSVPGQGSVFTLTV 503
Cdd:cd16922   80 ISKKLVELMGGDISVESEPGQGSTFTFTL 108
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
394-504 7.59e-35

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 128.15  E-value: 7.59e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494   394 TDGTRLRQVLWNLISNAVKFT-QQGKVEVRVRYDkGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGKPatGTGIG 472
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLERD-GDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIG--GTGLG 77
                           90       100       110
                   ....*....|....*....|....*....|..
gi 446732494   473 LAVSRRLARDMGGDISVSSVPGQGSVFTLTVR 504
Cdd:smart00387  78 LSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
394-506 1.02e-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: 122.09  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  394 TDGTRLRQVLWNLISNAVKFTQQGKvEVRVRYDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGkpatGTGIGL 473
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAG-EITVTLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGG----GTGLGL 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 446732494  474 AVSRRLARDMGGDISVSSVPGQGSVFTLTVRAP 506
Cdd:pfam02518  76 SIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
265-502 5.71e-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: 119.47  E-value: 5.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 265 DITErkhyQDALEQASRDkttFISTISHELRTPLNGIVGLSRILLDTDLNAEQ--EKYLKtihvsaVTLGN------IFN 336
Cdd:NF033092 361 DVTE----QEKIEQERRE---FVANVSHELRTPLTTMRSYLEALADGAWKDPElaPRFLG------VTQNEtermirLVN 427
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 337 DIIDMDKIERRKVQLDNQPIDFTGFLADLENLSGLQAQQKGLRFVMEptlpLPHQVIT---DGTRLRQVLWNLISNAVKF 413
Cdd:NF033092 428 DLLQLSRMDSKDYKLNKEWVNFNEFFNYIIDRFEMILKNKNITFKRE----FPKRDLWveiDTDKITQVLDNIISNAIKY 503
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 414 TQQ-GKVEVRVRyDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVkD-----SQGgkpatGTGIGLAVSRRLARDMGGDI 487
Cdd:NF033092 504 SPEgGTITFRLL-ETHNRIIISISDQGLGIPKKDLDKIFDRFYRV-DkarsrKMG-----GTGLGLAIAKEVVEAHGGRI 576
                        250
                 ....*....|....*
gi 446732494 488 SVSSVPGQGSVFTLT 502
Cdd:NF033092 577 WAESEEGKGTTIYFT 591
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
276-525 6.70e-20

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 93.94  E-value: 6.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 276 LEQASRDKTTFISTISHELRTPLNGIVGLSRILLDT--DLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDN 353
Cdd:NF040691 264 LEELSRLQQRFVSDVSHELRTPLTTIRMAADVIHDSrdDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAELDV 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 354 QPIDFTGFLAD-LENLSGLqAQQKGLRFVME-PTLPLPHQVitDGTRLRQVLWNLISNAVKFTQQGKVEVRVRYDKGEmL 431
Cdd:NF040691 344 EPVDLRPLVRRvVDALRQL-AERAGVELRVDaPGTPVVAEV--DPRRVERVLRNLVVNAIEHGEGKPVVVTVAQDDTA-V 419
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 432 HFEVADSGIGIPQEEQDKIFAMYYQVkDSQGGKPATGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLTVraPAVAee 511
Cdd:NF040691 420 AVTVRDHGVGLKPGEVALVFDRFWRA-DPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTL--PRVA-- 494
                        250
                 ....*....|....
gi 446732494 512 vDDVFEEDDLPLPA 525
Cdd:NF040691 495 -GDRLTTSPLPLVP 507
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
263-502 6.08e-17

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 84.11  E-value: 6.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 263 GRDITERKHYQDALEQASRDKTTFISTISHELRTPLngivglsrILLDTDLNAEQE-------KYLKTIHVSAVTLGNIF 335
Cdd:NF012163 220 GKLAQDFNQLASTLEKNEQMRRDFMADISHELRTPL--------AVLRAELEAIQDgirkftpESLDSLQAEVGTLTKLV 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 336 NDIIDMDKIERRKVQLDNQPIDFTGFLADLENLSGLQAQQKGLRfvMEPTLPLPHQVITDGTRLRQVLWNLISNAVKFTQ 415
Cdd:NF012163 292 DDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLE--LEVSLPDSSLVFGDRDRLMQLFNNLLENSLRYTD 369
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 416 Q-GKVEVRVRyDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGKPAtGTGIGLAVSRRLARDMGGDISVSSVPG 494
Cdd:NF012163 370 SgGSLHISAS-QRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASG-GSGLGLAISLNIVQAHGGTLHAAHSPL 447

                 ....*...
gi 446732494 495 QGSVFTLT 502
Cdd:NF012163 448 GGLRIVVT 455
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
290-505 7.90e-16

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: 79.65  E-value: 7.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 290 ISHELRTPLNGIVGLSRILLDTDLNAEqEKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQPIDFTGFLADLENLS 369
Cdd:NF012226 145 IAHELRTPITILQGRLQGILDGVFEPD-PALFKSLLNQVEGLSHLVEDLRTLSLVENQQLRLNYESVDLKDSIEKVLKMF 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 370 GLQAQQKGLRFVMEPTLPlphQVITDGTRLRQVLWNLISNAVKFTQQGKVEVRVRYDKGEMLhFEVADSGIGIPQEEQDK 449
Cdd:NF012226 224 EDRLEQAQLTIVLNLTAT---PVFCDRRRIEQVLIALIDNAIRYANAGKLKISSSVIQDDWI-LQIEDEGPGIAEEYQQD 299
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446732494 450 IFAMYYQVKDSQgGKPATGTGIGLAVSRRLARDMGGDISVSSvPGQGSVFTLTVRA 505
Cdd:NF012226 300 LFNPFFRLEQSR-NKEFGGTGLGLAVVHAIVIAHKGSIEYSN-SQGNSVFTIKLPA 353
 
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: 1558.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494   1 MKQIRLLAQYYVDLMMKLGLVRFSMLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
Cdd:PRK11091   1 MKQIRLLAQYYVDLMVKLGLVRFSLLLALALVVLAMVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  81 EESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQLEQQSSFLRSF 160
Cdd:PRK11091  81 EESRQRLSRLVAKLEEMRERDLELNVQLKDNIAQLNQEIAEREKAEEARQEAFEQLKNEIKEREETQIELEQQSSLLRSF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 161 LDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDEKVFRHNVSLSYEQWLQYPDGRKA 240
Cdd:PRK11091 161 LDASPDLVYYRNEDGEFSGCNRAMELLTGKSEKQLIGLTPKDVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 241 CFEIRKVPYYDRVGKRHGLMGFGRDITERKHYQDALEQASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLNAEQEKY 320
Cdd:PRK11091 241 CFELRKVPFYDRVGKRHGLMGFGRDITERKRYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKY 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 321 LKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQPIDFTGFLADLENLSGLQAQQKGLRFVMEPTLPLPHQVITDGTRLR 400
Cdd:PRK11091 321 LKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLR 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 401 QVLWNLISNAVKFTQQGKVEVRVRYDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGKPATGTGIGLAVSRRLA 480
Cdd:PRK11091 401 QILWNLISNAVKFTQQGGVTVRVRYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKPATGTGIGLAVSKRLA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 481 RDMGGDISVSSVPGQGSVFTLTVRAPAVAEEVDDVFEEDDLPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKA 560
Cdd:PRK11091 481 QAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVEDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKE 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 561 ALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRDDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK11091 561 ALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 641 KFWDTQDEEESTVAPDDNSKS-QELLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYMSVLQSNLTARDQKGIVEEGHKI 719
Cdd:PRK11091 641 KFWDTQDDEESTVTTEESSKAnEALLDIPMLEQYVELVGPKLITDSLAVFEKMMPGYLSVLDSNLTARDQKGIVEEAHKI 720
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446732494 720 KGAAGSVGLRHLQQLGQQIQSPDLPAWEDNVGEWIEEMKQEWRHDVEVLKAWVAKNGKK 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 1.37e-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: 346.00  E-value: 1.37e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  277 EQASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQPI 356
Cdd:TIGR02956 458 EEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPF 537
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  357 DFTGFLADLENLSGLQAQQKGLRFVMEPTLPLPHQVITDGTRLRQVLWNLISNAVKFTQQGKVEVRVRYDKGEMLHFEVA 436
Cdd:TIGR02956 538 DLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDSSLLFEVE 617
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  437 DSGIGIPQEEQDKIFAMYYQVkdsQGGKPATGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLTVRAPaVAEEVDDVF 516
Cdd:TIGR02956 618 DTGCGIAEEEQATLFDAFTQA---DGRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLT-RGKPAEDSA 693
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  517 EEDDLPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYS 596
Cdd:TIGR02956 694 TLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIYG 773
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  597 RDDLPPLVALTANVLKDKKE-YLDAGMDDVLSKPLSVPALTAMIKKFWDTQ---------------------DEEESTVA 654
Cdd:TIGR02956 774 AKNEVKFIAFSAHVFNEDVAqYLAAGFDGFLAKPVVEEQLTAMIAVILAGGksnteapvlsaspsfdsasviENAQADDI 853
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  655 PDDNSKSQELLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYMSVLQSNLTARDQKGIVEEGHKIKGAAGSVGLRHLQQL 734
Cdd:TIGR02956 854 PESNQASEFLLDEEQLQQDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQL 933
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 446732494  735 GQQIQSPDLPAWEDnvGEWIEEMKQEWRHDVEVLKAW 771
Cdd:TIGR02956 934 CQQLEKQGKTGALE--LSDIDEIKQAWQASKTALDQW 968
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
275-502 2.93e-70

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 233.65  E-value: 2.93e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 275 ALEQASRDKTTFISTISHELRTPLNGIVGLSRILLDTdLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQ 354
Cdd:COG0642  102 LLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPE 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 355 PIDFTGFLADLENLSGLQAQQKGLRFVMEPTLPLPHqVITDGTRLRQVLWNLISNAVKFTQQG-KVEVRVRYDkGEMLHF 433
Cdd:COG0642  181 PVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPT-VRGDPDRLRQVLLNLLSNAIKYTPEGgTVTVSVRRE-GDRVRI 258
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446732494 434 EVADSGIGIPQEEQDKIFAMYYQVKDSQGGKpatGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLT 502
Cdd:COG0642  259 SVEDTGPGIPPEDLERIFEPFFRTDPSRRGG---GTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVT 324
PRK15347 PRK15347
two component system sensor kinase;
277-732 6.92e-68

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 241.47  E-value: 6.92e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 277 EQASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQPI 356
Cdd:PRK15347 392 EQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEET 471
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 357 DFTGFLADLENLSGLQAQQKG--LRFVMEPTLPLphQVITDGTRLRQVLWNLISNAVKFTQQGKVEVRVRYdKGEMLHFE 434
Cdd:PRK15347 472 ALLPLLDQAMLTIQGPAQSKSltLRTFVGAHVPL--YLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVKR-HEQQLCFT 548
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 435 VADSGIGIPQEEQDKIFAMYYQVKDSQGgkpatGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTL------------- 501
Cdd:PRK15347 549 VEDTGCGIDIQQQQQIFTPFYQADTHSQ-----GTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLvlplneyappepl 623
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 502 --TVRAP-------------AVAEEVDDVFEEDDLP-LPA---------------------------LNVLLVEDIELNV 538
Cdd:PRK15347 624 kgELSAPlalhrqlsawgitCQPGHQNPALLDPELAyLPGrlydllqqiiqgapnepvinlplqpwqLQILLVDDVETNR 703
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 539 -IVARsVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLdisrELTRRYsRDDLP------PLVALTANVL 611
Cdd:PRK15347 704 dIIGM-MLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGL----ETTQLW-RDDPNnldpdcMIVALTANAA 777
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 612 KDKKEYL-DAGMDDVLSKPLSVPALTAMIkkfwdtqdeeESTVapddnsKSQELLDIPMLEQyLELVGPKLITDGLAVFE 690
Cdd:PRK15347 778 PEEIHRCkKAGMNHYLTKPVTLAQLARAL----------ELAA------EYQLLRGIELSPQ-DSSCSPLLDTDDMALNS 840
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 446732494 691 KMmpgYMSVL----QSNLTARDQKGIVEEGHKIKGAAGSVGLRHLQ 732
Cdd:PRK15347 841 KL---YQSLLlllaQIEQAVENQEVLSQLLHTLKGCAGQAGLTELQ 883
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
273-503 2.98e-66

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 219.78  E-value: 2.98e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 273 QDALEQASRDKTTFISTISHELRTPLNGIVGLSRILLD--TDLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQ 350
Cdd:COG2205    6 LEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDeeDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLESGKLS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 351 LDNQPIDFTGFLADLENLSGLQAQQKGLRFVMEPTLPLPHqVITDGTRLRQVLWNLISNAVKFTQQG-KVEVRVRYDkGE 429
Cdd:COG2205   86 LELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPL-VYADPELLEQVLANLLDNAIKYSPPGgTITISARRE-GD 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446732494 430 MLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGKpatGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLTV 503
Cdd:COG2205  164 GVRISVSDNGPGIPEEELERIFERFYRGDNSRGEG---GTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
247-502 1.29e-60

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 209.79  E-value: 1.29e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 247 VPYYDRVGKRHGLMGFGRDITErkhyqdaLEQASRDKTTFISTISHELRTPLNGIVGLSRILLD--TDLNAEQEKYLKTI 324
Cdd:COG5002  136 LRLSALLLGLLLLAAVERDITE-------LERLEQMRREFVANVSHELRTPLTSIRGYLELLLDgaADDPEERREYLEII 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 325 HVSAVTLGNIFNDIIDMDKIERRKVQLDNQPIDFTGFLADLENLSGLQAQQKGLRFVMEPTLPLPhQVITDGTRLRQVLW 404
Cdd:COG5002  209 LEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPL-LVLGDPDRLEQVLT 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 405 NLISNAVKFTQQG-KVEVRVRYDKGEmLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGKpATGTGIGLAVSRRLARDM 483
Cdd:COG5002  288 NLLDNAIKYTPEGgTITVSLREEDDQ-VRISVRDTGIGIPEEDLPRIFERFYRVDKSRSRE-TGGTGLGLAIVKHIVEAH 365
                        250
                 ....*....|....*....
gi 446732494 484 GGDISVSSVPGQGSVFTLT 502
Cdd:COG5002  366 GGRIWVESEPGKGTTFTIT 384
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
275-740 6.80e-58

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 212.79  E-value: 6.80e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 275 ALEqASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQ 354
Cdd:PRK11107 286 AQE-AARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENI 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 355 PIDFTGFLADLENLSGLQAQQKGLRFVMEPTLPLPHQVITDGTRLRQVLWNLISNAVKFTQQGKVEVRVRYDKGE----M 430
Cdd:PRK11107 365 PFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSntkvQ 444
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 431 LHFEVADSGIGIPQEEQDKIFAMYYQVkDSQGGKPATGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLTVRAPAVAE 510
Cdd:PRK11107 445 LEVQIRDTGIGISERQQSQLFQAFRQA-DASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPN 523
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 511 EVddvfeEDDLPLPAL---NVLLVE----------------------------------DIEL----------------- 536
Cdd:PRK11107 524 PI-----IDGLPTDCLagkRLLYVEpnsaaaqatldilsetplevtysptlsqlpeahyDILLlglpvtfrepltmlher 598
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 537 ---------NVIVA--------------RSV------------------------------------------------- 544
Cdd:PRK11107 599 lakaksmtdFLILAlpcheqvlaeqlkqDGAdaclskplshtrllpallepchhkqppllpptdesrlpltvmavddnpa 678
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 545 --------LEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISrELTRRYSRDDLPPLVALTANVLKDKKE 616
Cdd:PRK11107 679 nlkligalLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRAC-ELIRQLPHNQNTPIIAVTAHAMAGERE 757
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 617 -YLDAGMDDVLSKPLSVPALTAMIKKfWDTQDEEESTVAPDD----NSKSQELLDIPM-LEQylelVGPK--LITDGLAV 688
Cdd:PRK11107 758 rLLSAGMDDYLAKPIDEAMLKQVLLR-YKPGPKFTSRVVAPEppepVHFPNATLDWQLaLRQ----AAGKpdLARDMLQM 832
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446732494 689 FEKMMPGYMSVLQSNLTARDQKGIVEEGHKIKGAAGSVGLRHLQQLGQQIQS 740
Cdd:PRK11107 833 LLDFLPEVRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQ 884
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
266-774 2.80e-56

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 208.22  E-value: 2.80e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 266 ITERKHYQDALEQASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIE 345
Cdd:PRK11466 427 VIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIE 506
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 346 --RRKVQLDNQPIDFTGFLADLENLSGLQAQQKGLRFVMEPTLPLPHQVITDGTRLRQVLWNLISNAVKFTQQGKVEVRV 423
Cdd:PRK11466 507 agGKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRS 586
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 424 RYDkGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGgkpatGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLTV 503
Cdd:PRK11466 587 RTD-GEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGKRG-----GTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRL 660
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 504 ----RAPAVAEEVDDVFEEDDLPLpalnvLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGE-YDLVLLDIQ 578
Cdd:PRK11466 661 plrvATAPVPKTVNQAVRLDGLRL-----LLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEpFAAALVDFD 735
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 579 LPDMTGLDISRELTRRYsrddlPPL--VALTANVLKDKKEYLDAGM-DDVLSKPLSVPALTAMIKKFWDTQdeeestvap 655
Cdd:PRK11466 736 LPDYDGITLARQLAQQY-----PSLvlIGFSAHVIDETLRQRTSSLfRGIIPKPVPREVLGQLLAHYLQLQ--------- 801
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 656 ddnSKSQELLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYMSVLQSNLTARDQKGIVEEGHKIKGAAGSVGLRHLQQLG 735
Cdd:PRK11466 802 ---VNNDQPLDVSQLNEDAALMGTEKIHEWLALFKQHALPLLDEIDIARASQDSEKIKRAAHQLKSSCSSLGMRQASQAC 878
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 446732494 736 QQIQSPDLPAwednvgewiEEMKQEWRHDVEVLKAWVAK 774
Cdd:PRK11466 879 AQLEQQPLSA---------PLPHEEITRSVAALEAWLAK 908
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
140-760 3.12e-54

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 203.43  E-value: 3.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  140 IKEREETQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMElltgksekqlvHLKPQDVYAPdvAEKVIETDEKV 219
Cdd:PRK09959  561 VRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFE-----------HYFTADYYKN--AMLPLENSDSP 627
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  220 FRHNVSLSYEQWLQYPDGRK---ACFEI------RKVPYYDRV----GKRHGLMGFG-RDITERKHYQDALE-------Q 278
Cdd:PRK09959  628 FKDVFSNAHEVTAETKENRTiytQVFEIdngiekRCINHWHTLcnlpASDHAVYICGwQDITETRDLIHALEvernkaiN 707
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  279 ASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLNAEQE-KYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQPID 357
Cdd:PRK09959  708 ATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVD 787
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  358 FTGFLADLENLSGLQAQQKGLRFVMEPTLPLPHQVITDGTRLRQVLWNLISNAVKFTQQGKVEVRVRY----DKGEMLHF 433
Cdd:PRK09959  788 IPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLghidDNHAVIKM 867
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  434 EVADSGIGIPQEEQDKIFAMYYQvkdSQGGKPATGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLTVRAPAVAE-EV 512
Cdd:PRK09959  868 TIMDSGSGLSQEEQQQLFKRYSQ---TSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQvAT 944
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  513 DDVFEEDDLPLP-ALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISREL 591
Cdd:PRK09959  945 VEAKAEQPITLPeKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKL 1024
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  592 TRRYSRddlPPLVALTANVLKDKKEY-LDAGMDDVLSKPLSVPALTAMIkkfwdTQDEEESTVAPddnskSQELLDIPML 670
Cdd:PRK09959 1025 REQNSS---LPIWGLTANAQANEREKgLSCGMNLCLFKPLTLDVLKTHL-----SQLHQVAHIAP-----QYRHLDIEAL 1091
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  671 EQYLElVGPKLITDGLAVFEKMMPGYMSVLQSNLTARDQKGIVEEGHKIKGAAGSVGLRHLQQLGQQIQ--------SPD 742
Cdd:PRK09959 1092 KNNTA-NDLQLMQEILMTFQHETHKDLPAAFHALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLEitpvsddsKPE 1170
                         650
                  ....*....|....*...
gi 446732494  743 LPAWEDNVGEWIEEMKQE 760
Cdd:PRK09959 1171 ILQLLNSVKEHIAELDQE 1188
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
4-502 5.22e-49

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 180.75  E-value: 5.22e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494   4 IRLLAQYYVDLMMKLGLVRFSMLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQLEES 83
Cdd:COG4251    3 LLALLLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  84 RQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQLEQQSSFLRSFLDA 163
Cdd:COG4251   83 LLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 164 SPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDEKVFRHNVSLSYEQWLQYPDGRKACFE 243
Cdd:COG4251  163 LLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLI 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 244 IRKVPYYDRVGKRHGLMGFGRDITERKHYQDALEQASRDKTTFISTISHELRTPLNGIVGLSRILLD---TDLNAEQEKY 320
Cdd:COG4251  243 LLLLLLILVLELLELRLELEELEEELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEdygDKLDEEGREY 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 321 LKTIHVSAVTLGNIFNDIIDMDKIERRkvQLDNQPIDFTGFLADLENLSGLQAQQKGLRFVMEPtlpLPhQVITDGTRLR 400
Cdd:COG4251  323 LERIRDAAERMQALIDDLLAYSRVGRQ--ELEFEPVDLNELLEEVLEDLEPRIEERGAEIEVGP---LP-TVRGDPTLLR 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 401 QVLWNLISNAVKFT---QQGKVEVRVRyDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVkdsQGGKPATGTGIGLAVSR 477
Cdd:COG4251  397 QVFQNLISNAIKYSrpgEPPRIEIGAE-REGGEWVFSVRDNGIGIDPEYAEKIFEIFQRL---HSRDEYEGTGIGLAIVK 472
                        490       500
                 ....*....|....*....|....*
gi 446732494 478 RLARDMGGDISVSSVPGQGSVFTLT 502
Cdd:COG4251  473 KIVERHGGRIWVESEPGEGATFYFT 497
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
138-502 6.83e-49

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: 179.79  E-value: 6.83e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 138 IEIKEREETQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDE 217
Cdd:COG5809  124 RDITERKRMEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFIS 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 218 KVFRHNVSLSYEQWLQYPDGRKACFEIRKVPYyDRVGKRHGLMGFGRDITERKHYQDALEQAsrDKTTFIS----TISHE 293
Cdd:COG5809  204 QLLKDGGIAQGEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVIIFRDITERKKLEELLRKS--EKLSVVGelaaGIAHE 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 294 LRTPLNGIVGLSRILLDTDLNaEQEKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQldnqPIDFTGFLADLENLSGLQA 373
Cdd:COG5809  281 IRNPLTSLKGFIQLLKDTIDE-EQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYE----PKDLNTLIEEVIPLLQPQA 355
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 374 QQKGLRFVMEPTLPLPhQVITDGTRLRQVLWNLISNAVKFT-QQGKVEVRVRYDKGEMLHFEVADSGIGIPQEEQDKIFA 452
Cdd:COG5809  356 LLKNVQIELELEDDIP-DILGDENQLKQVFINLLKNAIEAMpEGGNITIETKAEDDDKVVISVTDEGCGIPEERLKKLGE 434
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 446732494 453 MYYQVKDsqggkpaTGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLT 502
Cdd:COG5809  435 PFYTTKE-------KGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSIT 477
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
149-501 1.75e-48

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 175.42  E-value: 1.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 149 QLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDvaEKVIETDEKVFRHNVSLS- 227
Cdd:COG3852    1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPED--SPLRELLERALAEGQPVTe 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 228 YEQWLQYPDGRKACFEIRKVPYYDRVGKRhGLMGFGRDITERKHYQDALEQASRDKT--TFISTISHELRTPLNGIVGLS 305
Cdd:COG3852   79 REVTLRRKDGEERPVDVSVSPLRDAEGEG-GVLLVLRDITERKRLERELRRAEKLAAvgELAAGLAHEIRNPLTGIRGAA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 306 RILLDTDLNAEQEKYLKTIHVSAVTLGNIfndiidMDKIER--RKVQLDNQPIDFTGFLADLENLSGLQAQqKGLRFVME 383
Cdd:COG3852  158 QLLERELPDDELREYTQLIIEEADRLNNL------VDRLLSfsRPRPPEREPVNLHEVLERVLELLRAEAP-KNIRIVRD 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 384 --PTLPLphqVITDGTRLRQVLWNLISNAVK-FTQQGKVEVRVRYD---------KGEMLHFEVADSGIGIPQEEQDKIF 451
Cdd:COG3852  231 ydPSLPE---VLGDPDQLIQVLLNLVRNAAEaMPEGGTITIRTRVErqvtlgglrPRLYVRIEVIDNGPGIPEEILDRIF 307
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446732494 452 amyyqvkdsqggKP-----ATGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTL 501
Cdd:COG3852  308 ------------EPffttkEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRI 350
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
59-502 3.68e-46

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: 170.53  E-value: 3.68e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  59 IFFGLLITPWAVYFLSVVVEQLeesRQRLSRLVQKLEEMRERDLSLNVQLKDNiaqlnQEIAvrekaeaELQETFEQLKI 138
Cdd:COG5000   12 LLIALLLLLLALWLALLLARRL---TRPLRRLAEATRAVAAGDLSVRLPVTGD-----DEIG-------ELARAFNRMTD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 139 EIKEREEtqiQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIEtdeK 218
Cdd:COG5000   77 QLKEQRE---ELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLR---E 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 219 VFRHNVSLSYEqwlqYPDGRKACFEIRKVPYYDRvgkrhGLMGFGRDITErkhyqdaLEQASRDKT--TFISTISHELRT 296
Cdd:COG5000  151 ALERGWQEEIE----LTRDGRRTLLVRASPLRDD-----GYVIVFDDITE-------LLRAERLAAwgELARRIAHEIKN 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 297 PLNGIVG----LSRILLD--TDLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIErrkvQLDNQPIDFTGFLADLENLSG 370
Cdd:COG5000  215 PLTPIQLsaerLRRKLADklEEDREDLERALDTIIRQVDRLKRIVDEFLDFARLP----EPQLEPVDLNELLREVLALYE 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 371 LQAQQKGLRFVMEPTLPLPhQVITDGTRLRQVLWNLISNAVKFT-QQGKVEVRVRYDkGEMLHFEVADSGIGIPQEEQDK 449
Cdd:COG5000  291 PALKEKDIRLELDLDPDLP-EVLADRDQLEQVLINLLKNAIEAIeEGGEIEVSTRRE-DGRVRIEVSDNGPGIPEEVLER 368
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446732494 450 IFAMYYQVKdsqggkpATGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLT 502
Cdd:COG5000  369 IFEPFFTTK-------PKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIR 414
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
399-503 1.15e-45

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: 158.81  E-value: 1.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVKFTQQGKVEVRVRYDKGE----MLHFEVADSGIGIPQEEQDKIFAMYYQVkDSQGGKPATGTGIGLA 474
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEedgvQLRFSVEDTGIGIPEEQQARLFEPFSQA-DSSTTRKYGGTGLGLA 79
                         90       100
                 ....*....|....*....|....*....
gi 446732494 475 VSRRLARDMGGDISVSSVPGQGSVFTLTV 503
Cdd:cd16922   80 ISKKLVELMGGDISVESEPGQGSTFTFTL 108
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
275-635 1.33e-41

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 163.99  E-value: 1.33e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 275 ALEQASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIERRkvQLDNQ 354
Cdd:PRK10841 439 AAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESE--QLKIE 516
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 355 PIDFtgflADLENLSGLQA--------QQKGLRFVMEPTLPLphQVITDGTRLRQVLWNLISNAVKFTQQGKVEVRVRYD 426
Cdd:PRK10841 517 PREF----SPREVINHITAnylplvvkKRLGLYCFIEPDVPV--ALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRVD 590
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 427 KGeMLHFEVADSGIGIPQEEQDKIFAMYYQVkdSQGG-KPATGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFT----- 500
Cdd:PRK10841 591 GD-YLSFRVRDTGVGIPAKEVVRLFDPFFQV--GTGVqRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTiripl 667
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 501 --------------------LTVR------------------------APAVAEEV---DDVFEED-------------- 519
Cdd:PRK10841 668 ygaqypqkkgveglqgkrcwLAVRnasleqfletllqrsgiqvqryegQEPTPEDVlitDDPVQKKwqgravitfcrrhi 747
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 520 -------------------DLPL----------------PALN-------------VLLVEDIELNVIVARSVLEKLGNS 551
Cdd:PRK10841 748 gipleiapgewvhstatphELPAllariyrielesddsaNALPstdkavsdnddmmILVVDDHPINRRLLADQLGSLGYQ 827
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 552 VDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDIS---RELTRRYsrddlpPLVALTANVLKDKKEY-LDAGMDDVLS 627
Cdd:PRK10841 828 CKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTqrlRQLGLTL------PVIGVTANALAEEKQRcLEAGMDSCLS 901

                 ....*...
gi 446732494 628 KPLSVPAL 635
Cdd:PRK10841 902 KPVTLDVL 909
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
150-500 3.97e-38

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: 145.04  E-value: 3.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  150 LEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTG-----KSEKQLVHLkpqdVYAPDVAEkvietdekvFRHNV 224
Cdd:TIGR02966   1 LSALLSRFRAAAQALPDAVVVLDEEGQIEWCNPAAERLLGlrwpdDLGQRITNL----IRHPEFVE---------YLAAG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  225 SLSYEQWLQYPDGRKACFEIRKVPYydrvGKRHGLMGFgRDITERKHyqdaLEQASRDkttFISTISHELRTPLNGIVGL 304
Cdd:TIGR02966  68 RFSEPLELPSPINSERVLEIRIAPY----GEEQKLLVA-RDVTRLRR----LEQMRRD---FVANVSHELRTPLTVLRGY 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  305 SRILLDT--DLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQPIDFTGFLADLENLSGLQAQQKGLRFVM 382
Cdd:TIGR02966 136 LETLADGpdEDPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEALSQGKNHQITF 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  383 EPTLPLPhqVITDGTRLRQVLWNLISNAVKFTQ-QGKVEVRVRYDKGeMLHFEVADSGIGIPQEEQDKIFAMYYQVkDSQ 461
Cdd:TIGR02966 216 EIDGGVD--VLGDEDELRSAFSNLVSNAIKYTPeGGTITVRWRRDGG-GAEFSVTDTGIGIAPEHLPRLTERFYRV-DKS 291
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 446732494  462 GGKPATGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFT 500
Cdd:TIGR02966 292 RSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFS 330
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
528-639 1.61e-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: 132.98  E-value: 1.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRDDLPPLVALT 607
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRRTPIIALT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446732494 608 ANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMI 639
Cdd:cd17546   81 ANALEeDREKCLEAGMDDYLSKPVKLDQLKEVL 113
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
264-502 1.88e-35

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 138.01  E-value: 1.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 264 RDITERKHYQDALEQASRDKT--TFISTISHELRTPLNGIVG----LSRILLDTDLNAEQEKYLKTIHVSAVTLGNIfnd 337
Cdd:COG4191  121 RAEEELRELQEQLVQSEKLAAlgELAAGIAHEINNPLAAILGnaelLRRRLEDEPDPEELREALERILEGAERAAEI--- 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 338 iidmdkIER-----RKVQLDNQPIDFTGFLADLENLSGLQAQQKGLRFVMEPTLPLPhQVITDGTRLRQVLWNLISN--- 409
Cdd:COG4191  198 ------VRSlrafsRRDEEEREPVDLNELIDEALELLRPRLKARGIEVELDLPPDLP-PVLGDPGQLEQVLLNLLINaid 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 410 AVKFTQQGKVEVRVRYDkGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGkpatgTGIGLAVSRRLARDMGGDISV 489
Cdd:COG4191  271 AMEEGEGGRITISTRRE-GDYVVISVRDNGPGIPPEVLERIFEPFFTTKPVGKG-----TGLGLSISYGIVEKHGGRIEV 344
                        250
                 ....*....|...
gi 446732494 490 SSVPGQGSVFTLT 502
Cdd:COG4191  345 ESEPGGGTTFTIT 357
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
394-504 7.59e-35

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 128.15  E-value: 7.59e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494   394 TDGTRLRQVLWNLISNAVKFT-QQGKVEVRVRYDkGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGKPatGTGIG 472
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLERD-GDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIG--GTGLG 77
                           90       100       110
                   ....*....|....*....|....*....|..
gi 446732494   473 LAVSRRLARDMGGDISVSSVPGQGSVFTLTVR 504
Cdd:smart00387  78 LSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
394-506 1.02e-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: 122.09  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  394 TDGTRLRQVLWNLISNAVKFTQQGKvEVRVRYDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGkpatGTGIGL 473
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAG-EITVTLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGG----GTGLGL 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 446732494  474 AVSRRLARDMGGDISVSSVPGQGSVFTLTVRAP 506
Cdd:pfam02518  76 SIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
399-502 5.34e-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: 119.63  E-value: 5.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVKFT-QQGKVEVRVRYDkGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGKpatGTGIGLAVSR 477
Cdd:cd00075    1 LEQVLSNLLDNALKYSpPGGTIEISLRQE-GDGVVLEVEDNGPGIPEEDLERIFERFYRGDKSREGG---GTGLGLAIVR 76
                         90       100
                 ....*....|....*....|....*
gi 446732494 478 RLARDMGGDISVSSVPGQGSVFTLT 502
Cdd:cd00075   77 RIVEAHGGRITVESEPGGGTTFTVT 101
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
522-648 4.56e-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: 118.03  E-value: 4.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 522 PLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRDDLp 601
Cdd:COG0784    2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDI- 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446732494 602 PLVALTANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIKKFWDTQDE 648
Cdd:COG0784   81 PIIALTAYADEeDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
264-513 9.27e-30

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 125.47  E-value: 9.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 264 RDITERKHYQDALEQASRDKT--TFISTISHELRTPLNGIVGLSRILLDTDLNAEQEKYLKTIHVSAVTLGNIFNDIIDM 341
Cdd:PRK11360 369 SDLTERKRLQRRVARQERLAAlgELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEF 448
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 342 DKieRRKVQldNQPIDFTGFLADLENLSGLQAQQKGLRFVM--EPTLPLphqVITDGTRLRQVLWNLISNAVK-FTQQGK 418
Cdd:PRK11360 449 SR--PRESQ--WQPVSLNALVEEVLQLFQTAGVQARVDFETelDNELPP---IWADPELLKQVLLNILINAVQaISARGK 521
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 419 VEVRVRYDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKdsqggkpATGTGIGLAVSRRLARDMGGDISVSSVPGQGSV 498
Cdd:PRK11360 522 IRIRTWQYSDGQVAVSIEDNGCGIDPELLKKIFDPFFTTK-------AKGTGLGLALSQRIINAHGGDIEVESEPGVGTT 594
                        250
                 ....*....|....*
gi 446732494 499 FtlTVRAPAVAEEVD 513
Cdd:PRK11360 595 F--TLYLPINPQGNQ 607
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
138-502 8.82e-29

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: 120.99  E-value: 8.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 138 IEIKEREETQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDE 217
Cdd:COG5805  140 RDITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIE 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 218 KVFRHNVSLSYEQWLQYPDGRKACFEIRKVPYYDRVGKRHGLMGFGRDITERKHYQDALEQAsrDKTTFI----STISHE 293
Cdd:COG5805  220 SITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEELMARS--EKLSIAgqlaAGIAHE 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 294 LRTPLNGIVGLSRILLdtdlnAEQEKYLKtihvsavtlgniFNDII--DMDKIER---------RKVQLDNQPIDFTGFL 362
Cdd:COG5805  298 IRNPLTSIKGFLQLLQ-----PGIEDKEE------------YFDIMlsELDRIESiiseflalaKPQAVNKEKENINELI 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 363 ADLENLSGLQAQQKGLRFVMEPTLPLPhQVITDGTRLRQVLWNLISNAVK-FTQQGKVEVRVrYDKGEMLHFEVADSGIG 441
Cdd:COG5805  361 QDVVTLLETEAILHNIQIRLELLDEDP-FIYCDENQIKQVFINLIKNAIEaMPNGGTITIHT-EEEDNSVIIRVIDEGIG 438
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446732494 442 IPQEEQDKIFAMYYQVKDSqggkpatGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLT 502
Cdd:COG5805  439 IPEERLKKLGEPFFTTKEK-------GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTIT 492
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
265-502 5.71e-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: 119.47  E-value: 5.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 265 DITErkhyQDALEQASRDkttFISTISHELRTPLNGIVGLSRILLDTDLNAEQ--EKYLKtihvsaVTLGN------IFN 336
Cdd:NF033092 361 DVTE----QEKIEQERRE---FVANVSHELRTPLTTMRSYLEALADGAWKDPElaPRFLG------VTQNEtermirLVN 427
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 337 DIIDMDKIERRKVQLDNQPIDFTGFLADLENLSGLQAQQKGLRFVMEptlpLPHQVIT---DGTRLRQVLWNLISNAVKF 413
Cdd:NF033092 428 DLLQLSRMDSKDYKLNKEWVNFNEFFNYIIDRFEMILKNKNITFKRE----FPKRDLWveiDTDKITQVLDNIISNAIKY 503
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 414 TQQ-GKVEVRVRyDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVkD-----SQGgkpatGTGIGLAVSRRLARDMGGDI 487
Cdd:NF033092 504 SPEgGTITFRLL-ETHNRIIISISDQGLGIPKKDLDKIFDRFYRV-DkarsrKMG-----GTGLGLAIAKEVVEAHGGRI 576
                        250
                 ....*....|....*
gi 446732494 488 SVSSVPGQGSVFTLT 502
Cdd:NF033092 577 WAESEEGKGTTIYFT 591
HKR_ArcB_TM pfam18415
Histidine kinase receptor ArcB trans-membrane domain; Histidine kinase receptors (HKRs) are ...
15-89 3.85e-27

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: 104.92  E-value: 3.85e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446732494   15 MMKLGLVRFSMLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQLEESRQRLSR 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 6.77e-26

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: 102.61  E-value: 6.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRrysRDDLPPLVALT 607
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRR---RDPTTPVIILT 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 446732494  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 1.70e-24

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: 101.14  E-value: 1.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 525 ALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSRDDLPPLV 604
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRL-RADPRTADIPII 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446732494 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 5.85e-24

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: 100.42  E-value: 5.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSRDdlPPLVALT 607
Cdd:COG0745    4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRL-RARPSD--IPIIMLT 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446732494 608 A-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:COG0745   81 ArDDEEDRVRGLEAGADDYLTKPFDPEELLARIR 114
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
131-503 2.05e-23

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 103.39  E-value: 2.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 131 ETFEQLKIEIKEREETQIQLEQQSSFLRSFLDAspdlVFYRNEDKEFSGCNR-AMELLTGKSEKQLVHLKPQDVYAPDVA 209
Cdd:COG3290   64 LLLLLAALLLKLLEEIARLVEEREAVLESIREG----VIAVDRDGRITLINDaARRLLGLDAIGRPIDEVLAEVLETGER 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 210 EKVIETDEKVFRHNVslsyeqwlqypdgrkacfeirkVPYYDRvGKRHGLMGFGRDITERKHYQDALEQAsRDKTTFIST 289
Cdd:COG3290  140 DEEILLNGRVLVVNR----------------------VPIRDD-GRVVGAVATFRDRTELERLEEELEGV-KELAEALRA 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 290 ISHELRTPLNGIVGLsrilLDTDLNAEQEKYLKTIHVSAVTLgnifndiidmdkIERRKVQLDNQPIDftGFLADLENls 369
Cdd:COG3290  196 QRHDFRNHLHTISGL----LQLGEYDEALEYIDEISEELQEL------------IDSLLSRIGNPVLA--ALLLGKAA-- 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 370 glQAQQKGLRFVMEPTLPLPHQVITDGTrLRQVLWNLISNAV-----KFTQQGKVEVRVRYDKGEmLHFEVADSGIGIPQ 444
Cdd:COG3290  256 --RARERGIDLTIDIDSDLPDLPLSDTD-LVTILGNLLDNAIeavekLPEEERRVELSIRDDGDE-LVIEVEDSGPGIPE 331
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446732494 445 EEQDKIFAMYYQVKDSQGgkpatgTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLTV 503
Cdd:COG3290  332 ELLEKIFERGFSTKLGEG------RGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
1-775 4.02e-22

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


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 102.05  E-value: 4.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494   1 MKQIRLLAQYYVDLMMKLGLVRFSMLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
Cdd:COG2198  104 LLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLLLLALLLALLLLVLLVLLLLLLL 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  81 EESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQLEQQSSFLRSF 160
Cdd:COG2198  184 LLLLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAELAALLLLLLLLLLLLILLLLLLL 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 161 LDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDEKVFRHNVSLSYEQWLQYPDGRKA 240
Cdd:COG2198  264 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 241 CFEIRKVPYYDRVGKRHGLMGFGRDITERKHYQDALEQASRDKTTFISTISHELRTPLNGIVGLSRILLDTDLNAEQEKY 320
Cdd:COG2198  344 LLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSLLLLLLLLLLLLLL 423
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 321 LKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQPIDFTGFLADLENLSGLQAQQKGLRFVMEPTLPLPHQVITDGTRLR 400
Cdd:COG2198  424 LLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 503
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 401 QVLWNLISNAVKFTQQGKVEVRVRYDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGKPATGTGIGLAVSRRLA 480
Cdd:COG2198  504 LLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALLLGLGLLLGLLLGGLLLLLLLLL 583
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 481 RDMGGDISVSSVPGQGSVFTLTVRAPAVAEEVDDVFEEDDLPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKA 560
Cdd:COG2198  584 LLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAVLLAAAAAAA 663
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 561 ALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRDDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAmik 640
Cdd:COG2198  664 ALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLAALLLLLLLLLLLLLLL--- 740
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 641 kfWDTQDEEESTVAPDDNSKSQELLDIPMLEQYLElvGPKLITDGLAVFEKMMPGYMSVLQSNLTARDQKGIVEEGHKIK 720
Cdd:COG2198  741 --LLLLLAAAAAAAASPAAPALPVLDLEALRRLGG--DPELLRELLELFLEELPELLAELRQALAAGDLEALARLAHKLK 816
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446732494 721 GAAGSVGLRHLQQLGQQIQSPDLPAWEDNVGEWIEEMKQEWRHDVEVLKAWVAKN 775
Cdd:COG2198  817 GSAGNLGAPRLAELAAELEQAARAGDLEEAEELLAELEAELERVLAALEALLAEE 871
PRK09303 PRK09303
histidine kinase;
343-503 6.75e-22

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 98.48  E-value: 6.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 343 KIERRKVQLDN--QPIdftgfLADLENLsgLQAQQKGLRFVMEPTLPLphqVITDGTRLRQVLWNLISNAVKFTQ-QGKV 419
Cdd:PRK09303 225 RFNPQKLDLGSlcQEV-----ILELEKR--WLAKSLEIQTDIPSDLPS---VYADQERIRQVLLNLLDNAIKYTPeGGTI 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 420 EVrvrydkgEMLH-------FEVADSGIGIPQEEQDKIFAMYYQVKDSQGgkpATGTGIGLAVSRRLARDMGGDISVSSV 492
Cdd:PRK09303 295 TL-------SMLHrttqkvqVSICDTGPGIPEEEQERIFEDRVRLPRDEG---TEGYGIGLSVCRRIVRVHYGQIWVDSE 364
                        170
                 ....*....|.
gi 446732494 493 PGQGSVFTLTV 503
Cdd:PRK09303 365 PGQGSCFHFTL 375
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
527-641 8.82e-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: 91.06  E-value: 8.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISREL-----TRRYsrddlp 601
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLkedpaTRDI------ 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446732494 602 PLVALTANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIKK 641
Cdd:cd17548   75 PVIALTAYAMKgDREKILEAGCDGYISKPIDTREFLETVAK 115
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
524-642 1.46e-21

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: 94.08  E-value: 1.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 524 PALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRDDLpPL 603
Cdd:COG3437    5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDI-PV 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446732494 604 VALTANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIKKF 642
Cdd:COG3437   84 IFLTALAdPEDRERALEAGADDYLTKPFDPEELLARVRNA 123
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
289-502 1.51e-21

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 98.76  E-value: 1.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 289 TISHELRTPLNGIVGLSRiLLDTDLNAEQ-EKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQPIDFTGFLADLEN 367
Cdd:PRK11100 262 TLTHELKSPLAAIRGAAE-LLQEDPPPEDrARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVE 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 368 LSGLQAQQKGLRFVMEPTlplPHQVITDGTRLRQVLWNLISNAVKFT-QQGKVEVRVRYDKGEmLHFEVADSGIGIPQEE 446
Cdd:PRK11100 341 AREAQAAAKGITLRLRPD---DARVLGDPFLLRQALGNLLDNAIDFSpEGGTITLSAEVDGEQ-VALSVEDQGPGIPDYA 416
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446732494 447 QDKIFAMYYQVKDSQGGKpaTGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLT 502
Cdd:PRK11100 417 LPRIFERFYSLPRPANGR--KSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLT 470
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
290-514 7.71e-21

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 96.39  E-value: 7.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 290 ISHELRTPLNGIVGLSRILLDTDLNAEQEKYLKTIHVSAVT-LGNIFNDIIDMdkieRRKVQLDNQPIDFTGFLADLENL 368
Cdd:PRK10364 244 VAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADrLNRVVSELLEL----VKPTHLALQAVDLNDLINHSLQL 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 369 SGLQAQQKG--LRFVMEPTLPLphqVITDGTRLRQVLWNLISNAVK-FTQQGKVEVRVRyDKGEMLHFEVADSGIGIPQE 445
Cdd:PRK10364 320 VSQDANSREiqLRFTANDTLPE---IQADPDRLTQVLLNLYLNAIQaIGQHGVISVTAS-ESGAGVKISVTDSGKGIAAD 395
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446732494 446 EQDKIFAMYYQVKdsqggkpATGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLTVraPAVAEEVDD 514
Cdd:PRK10364 396 QLEAIFTPYFTTK-------AEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWL--PVNITRRDP 455
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
274-503 4.34e-20

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: 93.99  E-value: 4.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  274 DALEQASRDKTTFISTISHELRTPLNGIVGLSRILLDTDlnAEQEKYLKTIHVSAVT---LGNIFNDIIDMDKIERRKVQ 350
Cdd:TIGR01386 232 GRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQVALSQP--RTGEEYREVLESNLEElerLSRMVSDMLFLARADNGQLA 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  351 LDNQPIDFTGFLADLENLSGLQAQQKGLRFVMEPTLplphQVITDGTRLRQVLWNLISNAVKFTQQG-KVEVRVRYDKGE 429
Cdd:TIGR01386 310 LERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEG----LVRGDPQMFRRAISNLLSNALRHTPDGgTITVRIERRSDE 385
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446732494  430 MLhFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGKPAtGTGIGLAVSRRLARDMGGDISVSSvPGQGSVFTLTV 503
Cdd:TIGR01386 386 VR-VSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGE-GTGLGLAIVRSIMEAHGGRASAES-PDGKTRFILRF 456
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
276-525 6.70e-20

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 93.94  E-value: 6.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 276 LEQASRDKTTFISTISHELRTPLNGIVGLSRILLDT--DLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDN 353
Cdd:NF040691 264 LEELSRLQQRFVSDVSHELRTPLTTIRMAADVIHDSrdDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAELDV 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 354 QPIDFTGFLAD-LENLSGLqAQQKGLRFVME-PTLPLPHQVitDGTRLRQVLWNLISNAVKFTQQGKVEVRVRYDKGEmL 431
Cdd:NF040691 344 EPVDLRPLVRRvVDALRQL-AERAGVELRVDaPGTPVVAEV--DPRRVERVLRNLVVNAIEHGEGKPVVVTVAQDDTA-V 419
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 432 HFEVADSGIGIPQEEQDKIFAMYYQVkDSQGGKPATGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLTVraPAVAee 511
Cdd:NF040691 420 AVTVRDHGVGLKPGEVALVFDRFWRA-DPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTL--PRVA-- 494
                        250
                 ....*....|....
gi 446732494 512 vDDVFEEDDLPLPA 525
Cdd:NF040691 495 -GDRLTTSPLPLVP 507
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-504 9.54e-20

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: 85.64  E-value: 9.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVKFTQQGKVEVRVRYDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGgKPATGTGIGLAVSRR 478
Cdd:cd16947   21 LQRILKNLISNAIKYGSDGKFLGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRN-SAKQGNGLGLTITKR 99
                         90       100
                 ....*....|....*....|....*.
gi 446732494 479 LARDMGGDISVSSVPGQGSVFTLTVR 504
Cdd:cd16947  100 LAESMGGSIYVNSKPYEKTVFTVTLK 125
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-502 9.94e-20

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: 9.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVKFTQQGKV-EVRVRYDKGEMLH-FEVADSGIGIPQEEQDKIFAMYYQVkDSQGGKPatGTGIGLAVS 476
Cdd:cd16921    1 LGQVLTNLLGNAIKFRRPRRPpRIEVGAEDVGEEWtFYVRDNGIGIDPEYAEKVFGIFQRL-HSREEYE--GTGVGLAIV 77
                         90       100
                 ....*....|....*....|....*.
gi 446732494 477 RRLARDMGGDISVSSVPGQGSVFTLT 502
Cdd:cd16921   78 RKIIERHGGRIWLESEPGEGTTFYFT 103
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-501 3.02e-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: 83.63  E-value: 3.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVK-FTQQGKVEVRVrYDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKdsqggKPATGTGIGLAVSR 477
Cdd:cd16943    4 LNQVLLNLLVNAAQaMEGRGRITIRT-WAHVDQVLIEVEDTGSGIDPEILGRIFDPFFTTK-----PVGEGTGLGLSLSY 77
                         90       100
                 ....*....|....*....|....
gi 446732494 478 RLARDMGGDISVSSVPGQGSVFTL 501
Cdd:cd16943   78 RIIQKHGGTIRVASVPGGGTRFTI 101
PRK10490 PRK10490
sensor protein KdpD; Provisional
268-514 5.03e-19

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 92.41  E-value: 5.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 268 ERKHYQDALEQASRD------KTTFISTISHELRTPLNGIVGLSRILLdTDLNAEQEKYlkTIHVSAV---TLGNI--FN 336
Cdd:PRK10490 643 ERLTLTASEEQARLAsereqlRNALLAALSHDLRTPLTVLFGQAEILT-LDLASEGSPH--ARQASEIrqqVLNTTrlVN 719
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 337 DIIDMDKIERRKVQLDNQpidftgFLAdLENLSG--LQAQQKGL-RFVMEPTLPLPHQVI-TDGTRLRQVLWNLISNAVK 412
Cdd:PRK10490 720 NLLDMARIQSGGFNLRKE------WLT-LEEVVGsaLQMLEPGLsGHPINLSLPEPLTLIhVDGPLFERVLINLLENAVK 792
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 413 FT-QQGKVEVRVRYDkGEMLHFEVADSGIGIPQEEQDKIFAmyyqvKDSQGGKPAT--GTGIGLAVSRRLARDMGGDISV 489
Cdd:PRK10490 793 YAgAQAEIGIDAHVE-GERLQLDVWDNGPGIPPGQEQLIFD-----KFARGNKESAipGVGLGLAICRAIVEVHGGTIWA 866
                        250       260
                 ....*....|....*....|....*..
gi 446732494 490 SSVPGQGSVF--TLTVRAPAVAEEVDD 514
Cdd:PRK10490 867 ENRPEGGACFrvTLPLETPPELEEFHE 893
PAS COG2202
PAS domain [Signal transduction mechanisms];
145-281 6.30e-19

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 87.39  E-value: 6.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 145 ETQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDEKVFRHNV 224
Cdd:COG2202    1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446732494 225 SLSYEQWLQYPDGRKACFEIRKVPYYDRVGKRHGLMGFGRDITERKHYQDALEQASR 281
Cdd:COG2202   81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEE 137
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
243-502 7.46e-19

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 90.07  E-value: 7.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 243 EIRKVPYYDRvgkrHGLMgFGRDITERKHyqdaLEQASRDkttFISTISHELRTPLNGIVGLSRILLDTDLN-AEQEKYL 321
Cdd:PRK11006 176 EIRVMPYTEG----QLLM-VARDVTQMHQ----LEGARRN---FFANVSHELRTPLTVLQGYLEMMQDQPLEgALREKAL 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 322 KTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQPIDFTGFLADLE----NLSglQAQQKgLRFVMEPTLplphQVITDGT 397
Cdd:PRK11006 244 HTMREQTQRMEGLVKQLLTLSKIEAAPTIDLNEKVDVPMMLRVLEreaqTLS--QGKHT-ITFEVDNSL----KVFGNED 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 398 RLRQVLWNLISNAVKFTQQG-KVEVR-VRYDKGEmlHFEVADSGIGIPQEEQDKIFAMYYQVkDSQGGKPATGTGIGLAV 475
Cdd:PRK11006 317 QLRSAISNLVYNAVNHTPEGtHITVRwQRVPQGA--EFSVEDNGPGIAPEHIPRLTERFYRV-DKARSRQTGGSGLGLAI 393
                        250       260
                 ....*....|....*....|....*..
gi 446732494 476 SRRLARDMGGDISVSSVPGQGSVFTLT 502
Cdd:PRK11006 394 VKHALSHHDSRLEIESEVGKGTRFSFV 420
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
526-635 1.18e-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: 82.06  E-value: 1.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 526 LNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGE--YDLVLLDIQLPDMTGLDISRELTRRYSRDDLPPL 603
Cdd:cd19933    1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEhsFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPLI 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446732494 604 VALTANVLKDKKEY-LDAGMDDVLSKPLSVPAL 635
Cdd:cd19933   81 VALTANTDDSTREKcLSLGMNGVITKPVSLHAL 113
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
528-640 1.22e-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: 82.15  E-value: 1.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDielNVIVARSV---LEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSrdDLPPLV 604
Cdd:cd17624    1 ILLVED---DALLGDGLktgLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQ--SLPVLI 75
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446732494 605 aLTAN-VLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17624   76 -LTARdGVDDRVAGLDAGADDYLVKPFALEELLARLR 111
PRK13557 PRK13557
histidine kinase; Provisional
248-629 1.55e-18

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 89.73  E-value: 1.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 248 PYYDRVGKRHGLMGFGRDITERKHYQDALEQASRDKTTFIST--ISHELRTPLNGIVGLSRILLdtdLNAEQEKYLKTIH 325
Cdd:PRK13557 126 PVYNDAGDLVYFFGSQLDVSRRRDAEDALRQAQKMEALGQLTggIAHDFNNLLQVMSGYLDVIQ---AALSHPDADRGRM 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 326 VSAVtlGNIfndiidMDKIER------------RKVQLDNQPIDFTGFLADLENLSGlqaQQKG----LRFVMEPTLPlP 389
Cdd:PRK13557 203 ARSV--ENI------RAAAERaatltqqllafaRKQRLEGRVLNLNGLVSGMGELAE---RTLGdavtIETDLAPDLW-N 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 390 HQVitDGTRLRQVLWNLISNAVK-FTQQGKVEVRVR-----------YDK---GEMLHFEVADSGIGIPQEEQDKIFAMY 454
Cdd:PRK13557 271 CRI--DPTQAEVALLNVLINARDaMPEGGRVTIRTRnveiededlamYHGlppGRYVSIAVTDTGSGMPPEILARVMDPF 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 455 YQVKDSqgGKpatGTGIGLAVSRRLARDMGGDISVSSVPGQGSvfTLTVRAPAVAEEVDDVFEEddlPLPALN------V 528
Cdd:PRK13557 349 FTTKEE--GK---GTGLGLSMVYGFAKQSGGAVRIYSEVGEGT--TVRLYFPASDQAENPEQEP---KARAIDrggtetI 418
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 529 LLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPG-EYDLVLLDIQLP-DMTGLDISRELTRRYsrddlPPL-VA 605
Cdd:PRK13557 419 LIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHpEVDLLFTDLIMPgGMNGVMLAREARRRQ-----PKIkVL 493
                        410       420
                 ....*....|....*....|....*.
gi 446732494 606 LTANVLKDKKEYLDAGMD--DVLSKP 629
Cdd:PRK13557 494 LTTGYAEASIERTDAGGSefDILNKP 519
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
529-640 1.61e-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: 81.88  E-value: 1.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 529 LLVED-IELNVIVARSvLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtrRYSRDDLPPLVaLT 607
Cdd:cd17625    1 LVVEDeKDLSEAITKH-LKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSL--REEGIETPVLL-LT 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446732494 608 A-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17625   77 AlDAVEDRVKGLDLGADDYLPKPFSLAELLARIR 110
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
529-629 6.84e-18

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: 79.37  E-value: 6.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 529 LLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSRDdlPPLVALTA 608
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRL-REKGSD--IPIIMLTA 77
                         90       100
                 ....*....|....*....|..
gi 446732494 609 -NVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd17574   78 kDEEEDKVLGLELGADDYITKP 99
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
264-639 7.56e-18

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 88.20  E-value: 7.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 264 RDITERKHYQDALEQASRDKT--TFISTISHELRTPLNGIVGLSRILLDT-DLNAEQEKYLKTIhVSAvtlGNIFNDIID 340
Cdd:PRK13837 429 RLETERDALERRLEHARRLEAvgTLASGIAHNFNNILGAILGYAEMALNKlARHSRAARYIDEI-ISA---GARARLIID 504
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 341 MDKIERRKVQLDNQPIDFTGFLADLENLsglqaqqkgLRFVMEPTLPL-------PHQVITDGTRLRQVLWNLISNAVK- 412
Cdd:PRK13837 505 QILAFGRKGERNTKPFDLSELVTEIAPL---------LRVSLPPGVELdfdqdqePAVVEGNPAELQQVLMNLCSNAAQa 575
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 413 FTQQGKVEVRVRYDK--------------GEMLHFEVADSGIGIPQEEQDKIFAMYYQVKdsqggkpATGTGIGLAVSRR 478
Cdd:PRK13837 576 MDGAGRVDISLSRAKlrapkvlshgvlppGRYVLLRVSDTGAGIDEAVLPHIFEPFFTTR-------AGGTGLGLATVHG 648
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 479 LARDMGGDISVSSVPGQGSVFT--LTVRAPaVAEEVDDVFEEDDLPLPA-LNVLLVEDIELNVIVARSVLEKLG------ 549
Cdd:PRK13837 649 IVSAHAGYIDVQSTVGRGTRFDvyLPPSSK-VPVAPQAFFGPGPLPRGRgETVLLVEPDDATLERYEEKLAALGyepvgf 727
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 550 ----NSVDVAMTGKAAlemfkpgeYDLVLLDIQLPDMTGLDISRELTRRysrdDLPPLVAltANVLKDK-KEYLDAGMDD 624
Cdd:PRK13837 728 stlaAAIAWISKGPER--------FDLVLVDDRLLDEEQAAAALHAAAP----TLPIILG--GNSKTMAlSPDLLASVAE 793
                        410
                 ....*....|....*
gi 446732494 625 VLSKPLSVPALTAMI 639
Cdd:PRK13837 794 ILAKPISSRTLAYAL 808
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
529-629 1.33e-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: 78.42  E-value: 1.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 529 LLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSRDdlPPLVALTA 608
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKL-RELPPD--IPVIVLTA 77
                         90       100
                 ....*....|....*....|..
gi 446732494 609 NV-LKDKKEYLDAGMDDVLSKP 629
Cdd:cd00156   78 KAdEEDAVRALELGADDYLVKP 99
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
526-642 1.57e-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: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 526 LNVLLVEDIELNVIVARSVLEKLGN--SVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRddlPPL 603
Cdd:COG4565    4 IRVLIVEDDPMVAELLRRYLERLPGfeVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPD---VDV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446732494 604 VALTANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIKKF 642
Cdd:COG4565   81 IVITAARdPETVREALRAGVVDYLIKPFTFERLREALERY 120
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
290-502 2.67e-17

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: 84.92  E-value: 2.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 290 ISHELRTPLNGIVGLSRILLDTDLNAE-QEKYLKTIhvsavtlgnifndIIDMDKIER--------RKVQLDN-QPIDF- 358
Cdd:COG5806  208 IAHEVRNPLTVVRGFIQLLQEPELSDEkRKQYIRIA-------------LEELDRAEAiitdyltfAKPQPEKlEKIDVs 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 359 ------TGFLADLENLSGLQAQQKglrfvMEPTLplphQVITDGTRLRQVLWNLISNAVKFTQQ-GKVEVRVRYDKGEML 431
Cdd:COG5806  275 eelehvIDVLSPYANMNNVEIQTE-----LEPGL----YIEGDRQKLQQCLINIIKNGIEAMPNgGTLTIDVSIDKNKVI 345
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446732494 432 hFEVADSGIGIPQEEQDKIFAMYYQVKDsqggkpaTGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLT 502
Cdd:COG5806  346 -ISIKDTGVGMTKEQLERLGEPYFSTKE-------KGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTIT 408
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
263-502 6.08e-17

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 84.11  E-value: 6.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 263 GRDITERKHYQDALEQASRDKTTFISTISHELRTPLngivglsrILLDTDLNAEQE-------KYLKTIHVSAVTLGNIF 335
Cdd:NF012163 220 GKLAQDFNQLASTLEKNEQMRRDFMADISHELRTPL--------AVLRAELEAIQDgirkftpESLDSLQAEVGTLTKLV 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 336 NDIIDMDKIERRKVQLDNQPIDFTGFLADLENLSGLQAQQKGLRfvMEPTLPLPHQVITDGTRLRQVLWNLISNAVKFTQ 415
Cdd:NF012163 292 DDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLE--LEVSLPDSSLVFGDRDRLMQLFNNLLENSLRYTD 369
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 416 Q-GKVEVRVRyDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGKPAtGTGIGLAVSRRLARDMGGDISVSSVPG 494
Cdd:NF012163 370 SgGSLHISAS-QRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASG-GSGLGLAISLNIVQAHGGTLHAAHSPL 447

                 ....*...
gi 446732494 495 QGSVFTLT 502
Cdd:NF012163 448 GGLRIVVT 455
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
395-501 9.19e-17

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: 76.76  E-value: 9.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 395 DGTRLRQVLWNLISNAVKFTQQG-KVEVRVRYDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGKPAtGTGIGL 473
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTPDGgRIRCILEKFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHG-GTGLGL 79
                         90       100
                 ....*....|....*....|....*...
gi 446732494 474 AVSRRLARDMGGDISVSSVPGQGSVFTL 501
Cdd:cd16925   80 SIVKEFVELHGGTVTVSDAPGGGALFQV 107
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
283-345 9.31e-17

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 74.94  E-value: 9.31e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446732494  283 KTTFISTISHELRTPLNGIVGLSRILLDTDLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIE 345
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIE 64
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
283-345 1.92e-16

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 74.14  E-value: 1.92e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446732494   283 KTTFISTISHELRTPLNGIVGLSRILLDTDLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIE 345
Cdd:smart00388   2 KREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIE 64
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
527-657 2.17e-16

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: 82.32  E-value: 2.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRddlPPLVAL 606
Cdd:COG2204    4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPD---LPVILL 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446732494 607 TANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIKKFWDTQDEEESTVAPDD 657
Cdd:COG2204   81 TGYGdVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSG 132
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
156-266 4.79e-16

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: 74.76  E-value: 4.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  156 FLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDEKVFRH-NVSLSYEQWLQY 234
Cdd:pfam00989   2 DLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQgEESRGFEVSFRV 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 446732494  235 PDGRKACFEIRKVPYYDRVGKRHGLMGFGRDI 266
Cdd:pfam00989  82 PDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-504 6.53e-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: 73.97  E-value: 6.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVKFTQQGKVE-----VRVRYDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKdsqggkpATGTGIGL 473
Cdd:cd16920    1 IQQVLINLVRNGIEAMSEGGCErreltIRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFYTTK-------SEGLGMGL 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446732494 474 AVSRRLARDMGGDISVSSVPGQGSVFTLTVR 504
Cdd:cd16920   74 SICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
290-505 7.90e-16

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: 79.65  E-value: 7.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 290 ISHELRTPLNGIVGLSRILLDTDLNAEqEKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQPIDFTGFLADLENLS 369
Cdd:NF012226 145 IAHELRTPITILQGRLQGILDGVFEPD-PALFKSLLNQVEGLSHLVEDLRTLSLVENQQLRLNYESVDLKDSIEKVLKMF 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 370 GLQAQQKGLRFVMEPTLPlphQVITDGTRLRQVLWNLISNAVKFTQQGKVEVRVRYDKGEMLhFEVADSGIGIPQEEQDK 449
Cdd:NF012226 224 EDRLEQAQLTIVLNLTAT---PVFCDRRRIEQVLIALIDNAIRYANAGKLKISSSVIQDDWI-LQIEDEGPGIAEEYQQD 299
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446732494 450 IFAMYYQVKDSQgGKPATGTGIGLAVSRRLARDMGGDISVSSvPGQGSVFTLTVRA 505
Cdd:NF012226 300 LFNPFFRLEQSR-NKEFGGTGLGLAVVHAIVIAHKGSIEYSN-SQGNSVFTIKLPA 353
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
528-639 7.99e-16

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: 74.03  E-value: 7.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSRDDLPPLVALT 607
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRL-RELPWLANTPAIALT 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446732494 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 8.64e-16

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: 73.78  E-value: 8.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVKFTQQGKvEVRVRYDKGEM-LHFEVADSGIGIPQEEQDKIFAMYYQVkDSQGGKPATGTGIGLAVSR 477
Cdd:cd16952    1 LRSAFSNLVSNAVKYTPPSD-TITVRWSQEESgARLSVEDTGPGIPPEHIPRLTERFYRV-DIERCRNTGGTGLGLAIVK 78
                         90       100
                 ....*....|....*....|...
gi 446732494 478 RLARDMGGDISVSSVPGQGSVFT 500
Cdd:cd16952   79 HVMSRHDARLLIASELGKGSRFT 101
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
395-502 9.49e-16

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: 73.65  E-value: 9.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 395 DGTRLRQVLWNLISNAVKFTQQG-KVEVRV-RYDKGEMLHFEvaDSGIGIPQEEQDKIFAMYYQVKDSQGgKPATGTGIG 472
Cdd:cd16946    1 DRDRLQQLFVNLLENSLRYTDTGgKLRIRAaQTPQEVRLDVE--DSAPGVSDDQLARLFERFYRVESSRN-RASGGSGLG 77
                         90       100       110
                 ....*....|....*....|....*....|
gi 446732494 473 LAVSRRLARDMGGDISVSSVPGQGSVFTLT 502
Cdd:cd16946   78 LAICHNIALAHGGTISAEHSPLGGLRLVLT 107
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
528-629 9.73e-16

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: 73.24  E-value: 9.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtrRYSRDDLPPLVaLT 607
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRL--RAAGKQTPVLM-LT 77
                         90       100
                 ....*....|....*....|...
gi 446732494 608 A-NVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd19935   78 ArDSVEDRVKGLDLGADDYLVKP 100
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
527-640 3.81e-15

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: 72.09  E-value: 3.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMT-GKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSRDDLPPLVA 605
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSAGYLEVVSFTdPREALAWCRENPPDLILLDYMMPGMDGLEFIRRL-RALPGLEDVPIVM 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446732494 606 LTANVLKD-KKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17551   81 ITADTDREvRLRALEAGATDFLTKPFDPVELLARVR 116
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-496 6.05e-15

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: 70.94  E-value: 6.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVKFtqqGKVEVRVR-YDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGKpatGTGIGLAVSR 477
Cdd:cd16950    1 LKRVLSNLVDNALRY---GGGWVEVSsDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNARGTS---GTGLGLAIVQ 74
                         90
                 ....*....|....*....
gi 446732494 478 RLARDMGGDISVSSVPGQG 496
Cdd:cd16950   75 RISDAHGGSLTLANRAGGG 93
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
276-576 8.00e-15

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 78.82  E-value: 8.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 276 LEQASR--DKT-----TFISTISHELRTPLNGIVGLSRILLDTDLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIERRK 348
Cdd:PRK10618 436 LQQAQReyEKNqqarkAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQD 515
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 349 VQLDNQPIDFTGFLAD--LENLSGLQaqQKGLRFVMEPTLPLPHQVITDGTRLRQVLWNLISNAVKFTQQGKVEVRVRYD 426
Cdd:PRK10618 516 WKPEQELFSLQDLIDEvlPEVLPAIK--RKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEVDQD 593
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 427 KG--EMLHFEVADSGIGIPQEEQDKIfaMYYQVKDSQGGKPATGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLTVR 504
Cdd:PRK10618 594 ESspDRLTIRILDTGAGVSIKELDNL--HFPFLNQTQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLK 671
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446732494 505 APAVAEEVDdvfEEDDLPLPALNVLLveDI---ELNVIVARsVLEKLGNSVDVAMtgkaalEMFKPGEYDLVLLD 576
Cdd:PRK10618 672 MLAADPEVE---EEEEKLLDGVTVLL--DItseEVRKIVTR-QLENWGATCITPD------ERLISQEYDIFLTD 734
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
678-769 9.91e-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: 70.36  E-value: 9.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494   678 GPKLITDGLAVFEKMMPGYMSVLQSNLTARDQKGIVEEGHKIKGAAGSVGLRHLQQLGQQIQSPDLPAWEDNVgEWIEEM 757
Cdd:smart00073   2 GLELFREELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEV-ELTPDL 80
                           90
                   ....*....|..
gi 446732494   758 KQEWRHDVEVLK 769
Cdd:smart00073  81 LDLLLELVDVLK 92
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
402-503 1.07e-14

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: 70.39  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 402 VLWNLISNAV-----KFTQQGKVEVRVRYDkGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKdsqggkPATGTGIGLAVS 476
Cdd:cd16915    4 IVGNLIDNALdalaaTGAPNKQVEVFLRDE-GDDLVIEVRDTGPGIAPELRDKVFERGVSTK------GQGERGIGLALV 76
                         90       100
                 ....*....|....*....|....*..
gi 446732494 477 RRLARDMGGDISVSSVPGQGSVFTLTV 503
Cdd:cd16915   77 RQSVERLGGSITVESEPGGGTTFSIRI 103
PAS COG2202
PAS domain [Signal transduction mechanisms];
140-276 1.29e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 74.68  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 140 IKEREETQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDEKV 219
Cdd:COG2202  122 ITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRL 201
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446732494 220 FRHNVSlSYEQWLQYPDGRKACFEIR-KVPYYDRVGKRHGLMGFGRDITERKHYQDAL 276
Cdd:COG2202  202 LEGGRE-SYELELRLKDGDGRWVWVEaSAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
PRK10604 PRK10604
sensor protein RstB; Provisional
283-501 1.57e-14

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 76.57  E-value: 1.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 283 KTTFISTISHELRTPLngiVGLS-RILLDTDLNAEQEKYLKTihvsavTLGNIfNDIID----MDKIERRKVQLDNQPID 357
Cdd:PRK10604 212 KKQLIDGIAHELRTPL---VRLRyRLEMSDNLSAAESQALNR------DIGQL-EALIEelltYARLDRPQNELHLSEPD 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 358 FTGFLADleNLSGLQAQQKGLRFVMEPtlPLPHQVITDGTRL-RQVLWNLISNAVKFTQQgKVEVRVRYDKGEMLhFEVA 436
Cdd:PRK10604 282 LPAWLST--HLADIQAVTPEKTVRLDT--PHQGDYGALDMRLmERVLDNLLNNALRYAHS-RVRVSLLLDGNQAC-LIVE 355
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446732494 437 DSGIGIPQEEQDKIFAMYYQVKDSQGGKPAtGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTL 501
Cdd:PRK10604 356 DDGPGIPPEERERVFEPFVRLDPSRDRATG-GCGLGLAIVHSIALAMGGSVNCDESELGGARFSF 419
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
528-640 2.09e-14

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: 70.00  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDielNVIVARSV---LEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSRdDLPPLV 604
Cdd:cd19934    1 LLLVED---DALLAAQLkeqLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRW-RSEGR-ATPVLI 75
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446732494 605 aLTANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd19934   76 -LTARDsWQDKVEGLDAGADDYLTKPFHIEELLARLR 111
envZ PRK09467
osmolarity sensor protein; Provisional
276-496 2.61e-14

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 75.72  E-value: 2.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 276 LEQasrDKTTFISTISHELRTPlngivgLSRILLDTDLNAEQEKYLKTihvsavtlgNIFNDIIDMDKI-------ERRK 348
Cdd:PRK09467 225 LED---DRTLLMAGVSHDLRTP------LTRIRLATEMMSEEDGYLAE---------SINKDIEECNAIieqfidyLRTG 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 349 VQLDNQPIDFTGFLADLENLSGLQAQQKGLRFVMEPtLPLPHQVITdgtrLRQVLWNLISNAVKFTqQGKVEVRVRYDkG 428
Cdd:PRK09467 287 QEMPMEMADLNALLGEVIAAESGYEREIETALQPGP-IEVPMNPIA----IKRALANLVVNAARYG-NGWIKVSSGTE-G 359
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446732494 429 EMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGkpaTGTGIGLAVSRRLARDMGGDISVSSVPGQG 496
Cdd:PRK09467 360 KRAWFQVEDDGPGIPPEQLKHLFQPFTRGDSARGS---SGTGLGLAIVKRIVDQHNGKVELGNSEEGG 424
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
528-629 2.96e-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: 69.06  E-value: 2.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRDDLpPLVALT 607
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHI-PVIMIT 80
                         90       100
                 ....*....|....*....|...
gi 446732494 608 A-NVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd17538   81 AlDDREDRIRGLEAGADDFLSKP 103
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
394-502 2.98e-14

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: 69.24  E-value: 2.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 394 TDGTRLRQVLWNLISNAVKFTQQ-GKVEVRVrYDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQvkDSQGGKPATGTGIG 472
Cdd:cd16948    1 TDAKWLSFIIGQIVSNALKYSKQgGKIEIYS-ETNEQGVVLSIKDFGIGIPEEDLPRVFDKGFT--GENGRNFQESTGMG 77
                         90       100       110
                 ....*....|....*....|....*....|
gi 446732494 473 LAVSRRLARDMGGDISVSSVPGQGSVFTLT 502
Cdd:cd16948   78 LYLVKKLCDKLGHKIDVESEVGEGTTFTIT 107
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
389-501 6.09e-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 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: 68.59  E-value: 6.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 389 PHQVITDGTRLRQVLWNLISNAVKFTQQG-KVEVRVRYDKGEMlhFEVADSGIGIPQEEQDKIFAMYYQVkDSQGGKpat 467
Cdd:cd16940    4 DIQVQGDALLLFLLLRNLVDNAVRYSPQGsRVEIKLSADDGAV--IRVEDNGPGIDEEELEALFERFYRS-DGQNYG--- 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446732494 468 GTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTL 501
Cdd:cd16940   78 GSGLGLSIVKRIVELHGGQIFLGNAQGGGLEAWV 111
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
529-640 1.59e-13

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: 67.68  E-value: 1.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 529 LLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSRDDLPPLVALTA 608
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRIL-RSDPKTSSIPIIMLTA 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446732494 609 NVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd19937   80 KGEEfDKVLGLELGADDYITKPFSPRELLARVK 112
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-502 4.97e-13

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: 65.81  E-value: 4.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVKFTQQgKVEVRVRYDKGEmLHFEVADSGIGIPQEEQDKIFAMYYQVkDSQGGKPATGTGIGLAVSRR 478
Cdd:cd16949    1 LARALENVLRNALRYSPS-KILLDISQDGDQ-WTITITDDGPGVPEDQLEQIFLPFYRV-DSARDRESGGTGLGLAIAER 77
                         90       100
                 ....*....|....*....|....
gi 446732494 479 LARDMGGDISVSSVPGQGSVFTLT 502
Cdd:cd16949   78 AIEQHGGKIKASNRKPGGLRVRIW 101
PRK13560 PRK13560
hypothetical protein; Provisional
122-270 1.16e-12

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 71.63  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 122 REKAEAELQETFEQLKIEIKEREETQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQ 201
Cdd:PRK13560 171 RFERHAHADDQVDGFAEDITERKRAEERIDEALHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIH 250
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446732494 202 DVYAPDVAEKVIETDEKVFRHNVSLSYEQWLQYPDGRKACFEIR--KVPYYDRVGKRHGLMGFGRDITERK 270
Cdd:PRK13560 251 DFAPAQPADDYQEADAAKFDADGSQIIEAEFQNKDGRTRPVDVIfnHAEFDDKENHCAGLVGAITDISGRR 321
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
395-503 1.72e-12

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: 64.48  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 395 DGTRLRQVLWNLISNAVKFTQ-----QGKVEVRVRYDKGEMLHFEVADSGIGIPQEEQDKIFAMYyqVKDSqggkpATGT 469
Cdd:cd16944    1 DTTQISQVLTNILKNAAEAIEgrpsdVGEVRIRVEADQDGRIVLIVCDNGKGFPREMRHRATEPY--VTTR-----PKGT 73
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446732494 470 GIGLAVSRRLARDMGGDISVSSVPGQGSVFTLTV 503
Cdd:cd16944   74 GLGLAIVKKIMEEHGGRISLSNREAGGACIRIIL 107
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
264-503 2.71e-12

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 69.94  E-value: 2.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 264 RDITERKH----------YQDAL-EQasrdkttfistiSHELRTPLNGIVGLsrilLDTDLNAEQEKY-LKTIHVSAVTL 331
Cdd:PRK11086 321 RDKTEVRQlaqrldgmvnYADALrAQ------------SHEFMNKLHVILGL----LHLKSYDQLEDYiLKTANNYQEEI 384
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 332 GNIFNDIIDmdkierrkvqldnqPIdFTGFLadlenLSGLQ-AQQKGLRFVMEPTLPLP----HQVITDgtrLRQVLWNL 406
Cdd:PRK11086 385 GSLLGKIKS--------------PV-IAGFL-----LGKISrARELGITLIISEDSQLPdsgdEDQVHE---LITILGNL 441
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 407 ISN---AVKFTQQGKVEVRVRYDKGEmLHFEVADSGIGIPQEEQDKIFAMYYQVKdsqggkpATGTGIGLAVSRRLARDM 483
Cdd:PRK11086 442 IENaleAVGGEEGGEISVSLHYRNGW-LHCEVSDDGPGIAPDEIDAIFDKGYSTK-------GSNRGVGLYLVKQSVENL 513
                        250       260
                 ....*....|....*....|
gi 446732494 484 GGDISVSSVPGQGSVFTLTV 503
Cdd:PRK11086 514 GGSIAVESEPGVGTQFFVQI 533
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
285-503 3.28e-12

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: 70.16  E-value: 3.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  285 TFISTISHELRTPLnGIVGLSRILLDT-DLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQPIDFTGFLA 363
Cdd:TIGR03785 487 NMSSRLSHELRTPV-AVVRSSLENLELqALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSEVLS 565
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  364 DLenLSGLQAQQKGLRFVME-PTLPLPHQVItdGTRLRQVLWNLISNAVKFTQQGKV-EVRVRYDKGEMLhFEVADSGIG 441
Cdd:TIGR03785 566 GC--MQGYQMTYPPQRFELNiPETPLVMRGS--PELIAQMLDKLVDNAREFSPEDGLiEVGLSQNKSHAL-LTVSNEGPP 640
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446732494  442 IPQEEQDKIFAMYYQVKDsQGGKPATGTGIGLAVSRRLARDMGGDISVSSVP-GQGSVFTLTV 503
Cdd:TIGR03785 641 LPEDMGEQLFDSMVSVRD-QGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRISL 702
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
280-341 6.08e-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: 61.46  E-value: 6.08e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446732494 280 SRDKTTFISTISHELRTPLNGIVGLSRILLDTDL-NAEQEKYLKTIHVSAVTLGNIFNDIIDM 341
Cdd:cd00082    1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLdDEEQREYLERIREEAERLLRLINDLLDL 63
glnL PRK11073
nitrogen regulation protein NR(II);
273-494 9.37e-12

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 67.41  E-value: 9.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 273 QDALEQASRDkttFISTISHELRTPLNGIVG----LSRILLDTDLNaeqeKYLKTIHVSAVTLGNIFNDIIDMDKIERRK 348
Cdd:PRK11073 123 QHAQQVAARD---LVRGLAHEIKNPLGGLRGaaqlLSKALPDPALT----EYTKVIIEQADRLRNLVDRLLGPQRPGTHV 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 349 VQLDNQPIDFTGFLADLEnlsgLQAQQKGLRfVMEPTLP-LPHqvitDGTRLRQVLWNLISNAVKFTQQ--GKVEVRVRY 425
Cdd:PRK11073 196 TESIHKVAERVVQLVSLE----LPDNVRLIR-DYDPSLPeLAH----DPDQIEQVLLNIVRNALQALGPegGTITLRTRT 266
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446732494 426 DKGEMLH---------FEVADSGIGIPQEEQDKIFamYYQVKDSQGGkpatgTGIGLAVSRRLARDMGGDISVSSVPG 494
Cdd:PRK11073 267 AFQLTLHgeryrlaarIDIEDNGPGIPPHLQDTLF--YPMVSGREGG-----TGLGLSIARNLIDQHSGKIEFTSWPG 337
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
528-640 1.09e-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: 62.40  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtrRYSRDDLPPLVaLT 607
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRL--RAAGNDLPILV-LT 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446732494 608 A-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17627   78 ArDSVSDRVAGLDAGADDYLVKPFALEELLARVR 111
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
528-640 1.16e-11

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: 62.04  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDielNVIVARSV---LEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtrRYSRDDLPPLV 604
Cdd:cd17616    1 VLLIED---DSATAQSIelmLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTL--RLAKVKTPILI 75
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446732494 605 ALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17616   76 LSGLADIEDKVKGLGFGADDYMTKPFHKDELVARIH 111
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
286-503 1.60e-11

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 67.49  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 286 FISTISHELRTPLNGIVGLSRILLDTDlnaEQEKYLKTIHVSAVT----LGNIFNDIIDMDKIERRKVQLDNQPIDFTGF 361
Cdd:PRK09835 265 FSADIAHEIRTPITNLITQTEIALSQS---RSQKELEDVLYSNLEeltrMAKMVSDMLFLAQADNNQLIPEKKMLDLADE 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 362 LADLENLSGLQAQQKGLRFVMEPTlplPHQVITDGTRLRQVLWNLISNAVKFTQQGK-VEVRVRyDKGEMLHFEVADSGI 440
Cdd:PRK09835 342 VGKVFDFFEAWAEERGVELRFVGD---PCQVAGDPLMLRRAISNLLSNALRYTPAGEaITVRCQ-EVDHQVQLVVENPGT 417
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446732494 441 GIPQEEQDKIFAMYYQVKDSQGGKpATGTGIGLAVSRRLARDMGGDISVSSVPgQGSVFTLTV 503
Cdd:PRK09835 418 PIAPEHLPRLFDRFYRVDPSRQRK-GEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVISL 478
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
266-491 2.06e-11

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 67.40  E-value: 2.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 266 ITERKHYQDALEQA-SRDKTTF--------ISTISHELRTPLNGIvglSRILLDTDLNAEQEKYLKTIHvsavTLGNIFN 336
Cdd:COG4192  407 IEERKRIEKNLRQTqDELIQAAkmavvgqtMTSLAHELNQPLNAM---SMYLFSAKKALEQENYAQLPT----SLDKIEG 479
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 337 DIIDMDKIER------RKVQLDNQPIDFTGFLADLENLSGLQA--QQKGLrfvmepTLPLPHQVITDGTRLRQVLWNLIS 408
Cdd:COG4192  480 LIERMDKIIKslrqfsRKSDTPLQPVDLRQVIEQAWELVESRAkpQQITL------HIPDDLMVQGDQVLLEQVLVNLLV 553
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 409 NAVKFTQQGKVEVRVRYDKGEMLHFEVADSGIGIPqeEQDKIFAMYYQVKDsqggkpaTGTGIGLAVSRRLARDMGGDIS 488
Cdd:COG4192  554 NALDAVATQPQISVDLLSNAENLRVAISDNGNGWP--LVDKLFTPFTTTKE-------VGLGLGLSICRSIMQQFGGDLY 624

                 ...
gi 446732494 489 VSS 491
Cdd:COG4192  625 LAS 627
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
527-640 2.60e-11

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: 61.11  E-value: 2.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRDDLpPLVAL 606
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDI-PIIML 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446732494 607 TANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17618   81 TARGEEeDKVRGLEAGADDYITKPFSPRELVARIK 115
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
527-609 3.50e-11

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: 60.88  E-value: 3.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVEDielNVIVA---RSVLEKLG-NSVDVAMTGKAALEMFKPGEYDLVLLDIQLP-DMTGLDISRELTRRYSrddlP 601
Cdd:cd17534    2 KILIVED---EAIIAldlKEILESLGyEVVGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKFD----I 74

                 ....*...
gi 446732494 602 PLVALTAN 609
Cdd:cd17534   75 PVIFLTAY 82
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-494 4.27e-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: 60.17  E-value: 4.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVKFTQQ-GKVEVRVRYDkGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGGKPAtgTGIGLAVSR 477
Cdd:cd16945    5 LRQAINNLLDNAIDFSPEgGLIALQLEAD-TEGIELLVFDEGSGIPDYALNRVFERFYSLPRPHSGQKS--TGLGLAFVQ 81
                         90
                 ....*....|....*..
gi 446732494 478 RLARDMGGDISVSSVPG 494
Cdd:cd16945   82 EVAQLHGGRITLRNRPD 98
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
528-640 4.29e-11

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: 60.51  E-value: 4.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRddlpPLVALT 607
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSNV----PIIMLT 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446732494 608 ANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17614   77 AKDSEvDKVLGLELGADDYVTKPFSNRELLARVK 110
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-501 4.58e-11

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: 60.49  E-value: 4.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVKFT--QQGKVEVRVRYDKGEMLH---------FEVADSGIGIPQEEQDKIFamYYQVKDSQGGkpat 467
Cdd:cd16918    1 LIQVFLNLVRNAAQALagSGGEIILRTRTQRQVTLGhprhrlalrVSVIDNGPGIPPDLQDTIF--YPMVSGRENG---- 74
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446732494 468 gTGIGLAVSRRLARDMGGDISVSSVPGQgSVFTL 501
Cdd:cd16918   75 -TGLGLAIAQNIVSQHGGVIECDSQPGH-TVFSV 106
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
161-270 5.19e-11

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: 60.12  E-value: 5.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  161 LDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDEKVFRHNVSLSYEQwLQYPDGRKA 240
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLE-ELLLNGEER 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 446732494  241 CFEIRKVPYYDRVGKRHGLMGFGRDITERK 270
Cdd:pfam08448  80 HYELRLTPLRDPDGEVIGVLVISRDITERR 109
PRK10643 PRK10643
two-component system response regulator PmrA;
528-640 6.22e-11

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 62.75  E-value: 6.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIEL---NVIVArsvLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtrRYSRDDLPPLV 604
Cdd:PRK10643   3 ILIVEDDTLllqGLILA---LQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRW--RQKKYTLPVLI 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446732494 605 aLTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK10643  78 -LTArDTLEDRVAGLDVGADDYLVKPFALEELHARIR 113
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
528-608 7.58e-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: 59.90  E-value: 7.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDIsreLTRRYSRDDLPPLVALT 607
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEI---LKWIQERSLPTSVIVIT 77

                 .
gi 446732494 608 A 608
Cdd:cd17572   78 A 78
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
528-629 7.60e-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: 7.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVED---IeLNVIvaRSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSRddlPPLV 604
Cdd:cd17620    1 ILVIEDepqI-RRFL--RTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRL-REWSA---VPVI 73
                         90       100
                 ....*....|....*....|....*.
gi 446732494 605 ALTA-NVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd17620   74 VLSArDEESDKIAALDAGADDYLTKP 99
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-501 8.24e-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: 8.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNA---VKFTQQGKVEVRVRYDKGEMLhFEVADSGIGIPQEEQDKIFAMYYQVKDSqgGKpatGTGIGLAV 475
Cdd:cd16976    1 IQQVLMNLLQNAldaMGKVENPRIRIAARRLGGRLV-LVVRDNGPGIAEEHLSRVFDPFFTTKPV--GK---GTGLGLSI 74
                         90       100
                 ....*....|....*....|....*.
gi 446732494 476 SRRLARDMGGDISVSSVPGQGSVFTL 501
Cdd:cd16976   75 SYGIVEEHGGRLSVANEEGAGARFTF 100
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-506 1.13e-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: 59.12  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVKFTQQGKVEVRVRY-DKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKdSQGGKPATGTGIGLAVSR 477
Cdd:cd16953    1 LGQVLRNLIGNAISFSPPDTGRITVSAmPTGKMVTISVEDEGPGIPQEKLESIFDRFYTER-PANEAFGQHSGLGLSISR 79
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446732494 478 RLARDMGGDISVSSV--PGQGSVFTLTVRAP 506
Cdd:cd16953   80 QIIEAHGGISVAENHnqPGQVIGARFTVQLP 110
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-502 1.51e-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: 58.60  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVKFTQQgkvEVRVRY-DKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSQGgKPATGTGIGLAVSR 477
Cdd:cd16939    1 MARALDNLLRNALRYAHR---TVRIALlVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRD-RATGGFGLGLAIVH 76
                         90       100
                 ....*....|....*....|....*
gi 446732494 478 RLARDMGGDISVSSVPGQGSVFTLT 502
Cdd:cd16939   77 RVALWHGGHVECDDSELGGACFRLT 101
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
526-660 2.03e-10

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 61.76  E-value: 2.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 526 LNVLLVEDIELNVIVARSVLEKLGN--SVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTrrySRDDLPPL 603
Cdd:COG3279    2 MKILIVDDEPLARERLERLLEKYPDleVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLR---ELDPPPPI 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446732494 604 VALTANvlkdkKEYLDAGMD----DVLSKPLSVPALTAMIKKFWDTQDEEESTVAPDDNSK 660
Cdd:COG3279   79 IFTTAY-----DEYALEAFEvnavDYLLKPIDEERLAKALEKAKERLEAKAAAEASPEEKD 134
PRK10336 PRK10336
two-component system response regulator QseB;
526-640 2.41e-10

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 61.06  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 526 LNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRDdlpPLVA 605
Cdd:PRK10336   1 MRILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQRE---PVLI 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446732494 606 LTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK10336  78 LTArDALAERVEGLRLGADDYLCKPFALIEVAARLE 113
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
526-580 2.53e-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: 56.42  E-value: 2.53e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 446732494   526 LNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLP 580
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
527-629 3.30e-10

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: 57.48  E-value: 3.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVEDIELNVIVARSVLEKLGN--SVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRddlPPLV 604
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEAGfeVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPD---TKII 77
                         90       100
                 ....*....|....*....|....*....
gi 446732494 605 ALTANvlkDKKEY----LDAGMDDVLSKP 629
Cdd:COG4753   78 ILSGY---SDFEYaqeaIKLGADDYLLKP 103
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
528-629 3.35e-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: 3.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSrddlPPLVALT 607
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSN----VPVIMVT 76
                         90       100
                 ....*....|....*....|...
gi 446732494 608 ANVLK-DKKEYLDAGMDDVLSKP 629
Cdd:cd17621   77 AKDSEiDKVVGLELGADDYVTKP 99
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
528-640 4.43e-10

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: 57.70  E-value: 4.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVED-IELNVIVARsVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTrrySRDDLPPLVaL 606
Cdd:cd17623    1 ILLIDDdRELTELLTE-YLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELR---KTSQVPVLM-L 75
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446732494 607 TANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17623   76 TARGDDiDRILGLELGADDYLPKPFNPRELVARIR 110
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
686-759 6.13e-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: 56.21  E-value: 6.13e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446732494  686 LAVFEKMMPGYMSVLQSNLTARDQKGIVEEGHKIKGAAGSVGLRHLQQLGQQIQS----PDLPAWEDNVGEWIEEMKQ 759
Cdd:pfam01627   3 LELFLEEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDllreGELPLDPELLEALRDLLEA 80
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
287-475 7.87e-10

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 61.87  E-value: 7.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 287 ISTISHELRTPLngivglSRILLDTDL----NAEqEKYLKTIHVSAVTLGNIFNDIIDMDKIE-RRKVQLDNQPID--FT 359
Cdd:PRK09470 247 LSDISHELRTPL------TRLQLATALlrrrQGE-SKELERIETEAQRLDSMINDLLVLSRNQqKNHLERETFKANslWS 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 360 GFLADlenlSGLQAQQKGLRFVMePTLPLPHQVITDGTRLRQVLWNLISNAVKFTQQgKVEVRVrYDKGEMLHFEVADSG 439
Cdd:PRK09470 320 EVLED----AKFEAEQMGKSLTV-SAPPGPWPINGNPNALASALENIVRNALRYSHT-KIEVAF-SVDKDGLTITVDDDG 392
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446732494 440 IGIPQEEQDKIFAMYYQV---KDSQGGkpatGTGIGLAV 475
Cdd:PRK09470 393 PGVPEEEREQIFRPFYRVdeaRDRESG----GTGLGLAI 427
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
528-640 8.68e-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: 56.98  E-value: 8.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDiELNVIVARSV-LEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtrrysRDDLP--PLV 604
Cdd:cd17615    2 VLVVDD-EPNITELLSMaLRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRL-----RADGPdvPVL 75
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446732494 605 ALTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17615   76 FLTAkDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLR 112
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
682-762 9.13e-10

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: 56.24  E-value: 9.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 682 ITDGLAVFEKMMPGYMSVLQSNLTAR----DQKGIVEEGHKIKGAAGSVGLRHLQQLGQQIQS---------PDLPAWED 748
Cdd:cd00088    1 MEELLELFLEEAEELLEELERALLELedaeDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDlldalrdglEVTPELID 80
                         90
                 ....*....|....
gi 446732494 749 NVGEWIEEMKQEWR 762
Cdd:cd00088   81 LLLDALDALKAELE 94
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
527-643 1.13e-09

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: 57.04  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVEDIELNVIVARSVLEKLG--NSVDVAMTGKAALEM-FKPGEY------DLVLLDIQLPDMTGLDISRELTrrySR 597
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDFlRGEGEYadaprpDLILLDLNMPRMDGFEVLREIK---AD 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446732494 598 DDLP--PLVALTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK---KFW 643
Cdd:cd17557   78 PDLRriPVVVLTTsDAEEDIERAYELGANSYIVKPVDFEEFVEAIRslgEYW 129
pleD PRK09581
response regulator PleD; Reviewed
528-640 1.15e-09

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 61.46  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNV--IVARSVLEKLgnSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtrrysRDDlP---- 601
Cdd:PRK09581   5 ILVVDDIPANVklLEAKLLAEYY--TVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRL-----KSD-Patth 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446732494 602 -PLVALTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK09581  77 iPVVMVTAlDDPEDRVRGLEAGADDFLTKPINDVALFARVK 117
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
524-639 1.44e-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: 58.43  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 524 PALNVLLVEDIELNVIVARSVLEKLGNSV-DVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtrrySRDDLPP 602
Cdd:COG3707    2 RGLRVLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQI----SEERPAP 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446732494 603 LVALTANVLKDKKEY-LDAGMDDVLSKPLSVPALTAMI 639
Cdd:COG3707   78 VILLTAYSDPELIERaLEAGVSAYLVKPLDPEDLLPAL 115
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
57-510 1.99e-09

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 60.69  E-value: 1.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  57 RSIFFGLLITPWAVYFLSVVVEQLEESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFEQL 136
Cdd:COG3920   70 ALAAAVGAAAALLALLVLLLLLLLAAAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAEL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 137 KIEIKEREETQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETD 216
Cdd:COG3920  150 AVALAELAAALLLLAEELAALRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAA 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 217 EKVFRHNVSLSYEQWLQyPDGRKACFEIRKVPYYDRVGKRHGLMGFGRDITERKHYQDALEQASRDKTTFISTISHELRT 296
Cdd:COG3920  230 LLRLRAAVLEELERRRR-ARGLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKELLLRELHHRVKN 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 297 PLNGIVGLSRIlldtdlnaeQEKYLKTIHVSAVtlgniFNDIID----MDKIERRKVQLDN-QPIDFTGFLADLENLSGL 371
Cdd:COG3920  309 NLQVVSSLLRL---------QARRADDPEAREA-----LEESQNriqaLALVHELLYQSEDwEGVDLRDYLRELLEPLRD 374
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 372 QAQQKGLRFVME-PTLPLPhqvITDGTRLRQVLWNLISNAVKF----TQQGKVEVRVRYDkGEMLHFEVADSGIGIPQee 446
Cdd:COG3920  375 SYGGRGIRIELDgPDVELP---ADAAVPLGLILNELVTNALKHaflsGEGGRIRVSWRRE-DGRLRLTVSDNGVGLPE-- 448
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446732494 447 qdkifamyyqvkdsqGGKPATGTGIGLAVSRRLARDMGGDISVSSvpGQGSVFTLTVRAPAVAE 510
Cdd:COG3920  449 ---------------DVDPPARKGLGLRLIRALVRQLGGTLELDR--PEGTRVRITFPLAELAA 495
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
277-475 2.06e-09

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 60.42  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 277 EQASRDkttFISTISHELRTPLNgivglsriLLDTDLNAEQE-------KYLKTIHVSAVTLGNIFNDI-----IDMDKI 344
Cdd:PRK10549 237 EQMRRD---FMADISHELRTPLA--------VLRGELEAIQDgvrkftpESVASLQAEVGTLTKLVDDLhqlslSDEGAL 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 345 ERRKVQLDNQPIdftgfladLENLSGL---QAQQKGLRFvmepTLPLPHQ--VITDGTRLRQVLWNLISNAVKFT-QQGK 418
Cdd:PRK10549 306 AYRKTPVDLVPL--------LEVAGGAfreRFASRGLTL----QLSLPDSatVFGDPDRLMQLFNNLLENSLRYTdSGGS 373
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446732494 419 VEVR-VRYDKGEMLHFEvaDSGIGIPQEEQDKIFAMYYQVKDSQgGKPATGTGIGLAV 475
Cdd:PRK10549 374 LHISaEQRDKTLRLTFA--DSAPGVSDEQLQKLFERFYRTEGSR-NRASGGSGLGLAI 428
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
545-631 3.27e-09

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: 55.28  E-value: 3.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 545 LEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRysRDDLPPLVALTANVLKDKKEYLDAGMDD 624
Cdd:cd17555   20 LEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKE--SPDTPVIVVSGAGVMSDAVEALRLGAWD 97

                 ....*..
gi 446732494 625 VLSKPLS 631
Cdd:cd17555   98 YLTKPIE 104
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
147-311 4.43e-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: 59.40  E-value: 4.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 147 QIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDEKVFRHnvsl 226
Cdd:COG3829    3 ELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSPLLEVLKTGKPVTGV---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 227 syeqwLQYPDGRKACFEIRKVPYYDRvGKRHGLMGFGRDITERKHYQDALEQASRDKttfistiSHELRTPLNGIVGLSR 306
Cdd:COG3829   79 -----IQKTGGKGKTVIVTAIPIFED-GEVIGAVETFRDITELKRLERKLREEELER-------GLSAKYTFDDIIGKSP 145

                 ....*
gi 446732494 307 ILLDT 311
Cdd:COG3829  146 AMKEL 150
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
527-601 6.15e-09

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: 54.53  E-value: 6.15e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446732494 527 NVLLVEDiELNV-IVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSrdDLP 601
Cdd:cd17554    2 KILVVDD-EENIrELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKP--DLP 74
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
528-640 6.29e-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: 6.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVED-IELNVIVArSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRddlpPLVAL 606
Cdd:cd17622    3 ILLVEDdPKLARLIA-DFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG----PILLL 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446732494 607 TANVlKDKKEY--LDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17622   78 TALD-SDIDHIlgLELGADDYVVKPVEPAVLLARLR 112
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
527-657 7.57e-09

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: 55.69  E-value: 7.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtrRYSRDDLPPLVaL 606
Cdd:COG4567    6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEAL--RERDPDARIVV-L 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446732494 607 T-----ANVLkdkkEYLDAGMDDVLSKPLSVPALTAMIkkfwdTQDEEESTVAPDD 657
Cdd:COG4567   83 TgyasiATAV----EAIKLGADDYLAKPADADDLLAAL-----ERAEGDAPAPPEN 129
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
526-641 7.66e-09

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: 54.27  E-value: 7.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 526 LNVLLVEDIELNVIVARSVLEKLG-NSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRDDLPPLV 604
Cdd:cd19923    1 MKVLVVDDFSTMRRIIKNLLKELGfNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLM 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446732494 605 ----ALTANVLKDKKeyldAGMDDVLSKPLSVPALTAMIKK 641
Cdd:cd19923   81 vtaeAKKENVIAAAQ----AGVNNYIVKPFTAATLKEKLEK 117
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
164-266 1.01e-08

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: 53.41  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 164 SPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDEKVFRHNVSLSYEQWLQYPDGRKACFE 243
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                         90       100
                 ....*....|....*....|...
gi 446732494 244 IRKVPYYDRVGKRHGLMGFGRDI 266
Cdd:cd00130   81 VSLTPIRDEGGEVIGLLGVVRDI 103
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
527-640 1.24e-08

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 56.35  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSRddLPPLVAL 606
Cdd:PRK10529   3 NVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDL-RQWSA--IPVIVLS 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446732494 607 TANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK10529  80 ARSEESDKIAALDAGADDYLSKPFGIGELQARLR 113
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
527-631 1.64e-08

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 55.74  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVED---IELNVIVArsvLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSrdDLpPL 603
Cdd:PRK11083   5 TILLVEDeqaIADTLVYA---LQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHP--AL-PV 78
                         90       100
                 ....*....|....*....|....*....
gi 446732494 604 VALTA-NVLKDKKEYLDAGMDDVLSKPLS 631
Cdd:PRK11083  79 IFLTArSDEVDRLVGLEIGADDYVAKPFS 107
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
528-644 1.77e-08

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: 53.32  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGN-SVDVAMTGKAALEM---FKPgeyDLVLLDIQLPDMTGLDISREL-----TRRYsrd 598
Cdd:cd17552    4 ILVIDDEEDIREVVQACLEKLAGwEVLTASSGQEGLEKaatEQP---DAILLDVMMPDMDGLATLKKLqanpeTQSI--- 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446732494 599 dlpPLVALTANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIKKFWD 644
Cdd:cd17552   78 ---PVILLTAKAqPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLLG 121
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
528-629 2.29e-08

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: 52.35  E-value: 2.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPG-EYDLVLLDIQLPD-MTGLDISRELTRRYSrdDLPPLVA 605
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPGgMNGSQLAEEARRRRP--DLKVLLT 78
                         90       100
                 ....*....|....*....|....
gi 446732494 606 LTANVLKDKKEYLDAGMdDVLSKP 629
Cdd:cd18161   79 SGYAENAIEGGDLAPGV-DVLSKP 101
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
526-640 2.30e-08

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 55.32  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 526 LNVLLVED-IELNVIVARSVLEKlGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtrRYSRDDLPPLV 604
Cdd:PRK09836   1 MKLLIVEDeKKTGEYLTKGLTEA-GFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRML--RSANKGMPILL 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446732494 605 ALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK09836  78 LTALGTIEHRVKGLELGADDYLVKPFAFAELLARVR 113
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
388-503 2.96e-08

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: 52.85  E-value: 2.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 388 LPHQVITDGTRLRQVLWNLISNAVKFTQQ-GKVEVRV--------RYDKGEMLH------------FEVADSGIGIPQEE 446
Cdd:cd16938    1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGgGNITFRVfleggsedRSDRDWGPWrpsmsdesveirFEVEINDSGSPSIE 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446732494 447 QDKIFAmyYQVKDSQGGKPatGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLTV 503
Cdd:cd16938   81 SASMRN--SLNRRYNLSEL--GEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
PRK10337 PRK10337
sensor protein QseC; Provisional
286-504 3.53e-08

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 56.58  E-value: 3.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 286 FISTISHELRTPLNGI-VGLSRILLDTDLNAEQEKYLKTIHVSAVTLGNIFNDIIDMDKIERRKVQLDNQPIDftgfLAD 364
Cdd:PRK10337 240 FTSDAAHELRSPLAALkVQTEVAQLSDDDPQARKKALLQLHAGIDRATRLVDQLLTLSRLDSLDNLQDVAEIP----LED 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 365 LenlsgLQ---------AQQKGLrfvmEPTLPLP-HQVITDGTRLRQVLW--NLISNAVKFTQQG-KVEVRVRYDkgeml 431
Cdd:PRK10337 316 L-----LQsavmdiyhtAQQAGI----DVRLTLNaHPVIRTGQPLLLSLLvrNLLDNAIRYSPQGsVVDVTLNAR----- 381
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446732494 432 HFEVADSGIGIPQEEQDKIFAMYYQVKdsqgGKPATGTGIGLAVSRRLARDMGGDISVSSVPGQGsvFTLTVR 504
Cdd:PRK10337 382 NFTVRDNGPGVTPEALARIGERFYRPP----GQEATGSGLGLSIVRRIAKLHGMNVSFGNAPEGG--FEAKVS 448
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
406-503 5.03e-08

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 56.18  E-value: 5.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 406 LISNAVKF-----TQQGKVEVRVRYDkGEMLHFEVADSGIGIPQEEQDKIFAMYyqvkdsqgGKPATGTGIGLA-VSRRL 479
Cdd:COG2972  344 LVENAIEHgiepkEGGGTIRISIRKE-GDRLVITVEDNGVGMPEEKLEKLLEEL--------SSKGEGRGIGLRnVRERL 414
                         90       100
                 ....*....|....*....|....*.
gi 446732494 480 AR--DMGGDISVSSVPGQGSVFTLTV 503
Cdd:COG2972  415 KLyyGEEYGLEIESEPGEGTTVTIRI 440
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
395-490 5.46e-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: 51.31  E-value: 5.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 395 DGTRLRQVLWNLISNAVKFTQQGK-VEVRVrYDKGEMLHFEVADSGIGIPQEEQDKIFAMYYqvKDSQGGKPATGTGIGL 473
Cdd:cd16975    1 DTLLLSRALINIISNACQYAPEGGtVSISI-YDEEEYLYFEIWDNGHGFSEQDLKKALELFY--RDDTSRRSGGHYGMGL 77
                         90
                 ....*....|....*..
gi 446732494 474 AVSRRLARDMGGDISVS 490
Cdd:cd16975   78 YIAKNLVEKHGGSLIIE 94
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
528-601 5.62e-08

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: 51.73  E-value: 5.62e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446732494 528 VLLVEDiELNVIVARS-VLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSrdDLP 601
Cdd:cd17550    1 ILIVDD-EEDIRESLSgILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYP--DLP 72
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
527-640 6.22e-08

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: 51.62  E-value: 6.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSRDDLPPLVAL 606
Cdd:cd17619    2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTREL-REQSEVGIILVTGR 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446732494 607 TANVlkDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17619   81 DDEV--DRIVGLEIGADDYVTKPFNPRELLVRAK 112
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
528-640 6.99e-08

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: 51.22  E-value: 6.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSrdDLpPLVALT 607
Cdd:cd19938    2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREI-RRFS--DV-PIIMVT 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446732494 608 ANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd19938   78 ARVEEiDRLLGLELGADDYICKPYSPREVVARVK 111
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
528-629 9.41e-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: 50.59  E-value: 9.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISREL-----TRRYsrddlpP 602
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLkadpaTRHI------P 74
                         90       100
                 ....*....|....*....|....*...
gi 446732494 603 LVALTA-NVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd19920   75 VIFLTAlTDTEDKVKGFELGAVDYITKP 102
PRK11517 PRK11517
DNA-binding response regulator HprR;
526-640 1.33e-07

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 52.98  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 526 LNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtrRYSRDDlpPLVA 605
Cdd:PRK11517   1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTL--RTAKQT--PVIC 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446732494 606 LTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK11517  77 LTArDSVDDRVRGLDSGANDYLVKPFSFSELLARVR 112
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
528-664 1.36e-07

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 53.27  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKpGEYDLVLLDIQLPDMTGLDISRELTRRYSRddlpPLVALT 607
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELRQTHQT----PVIMLT 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446732494 608 ANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIKKFWDTQDEEESTVAPDDNSKSQEL 664
Cdd:PRK10955  79 ARGSElDRVLGLELGADDYLPKPFNDRELVARIRAILRRSHWSEQQQNNDNGSPTLEV 136
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
407-506 1.60e-07

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: 49.47  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 407 ISNAVKFTQQGKVEVRVRYDKGEmLHFEVADSGIGIpqeeqdkifamyyqvkdsQGGKPATGTGIGLAVSRRLARDMGGD 486
Cdd:cd16917    9 LTNALKHAGASRVRVTLSYTADE-LTLTVVDDGVGF------------------DGPAPPGGGGFGLLGMRERAELLGGT 69
                         90       100
                 ....*....|....*....|
gi 446732494 487 ISVSSVPGQGsvFTLTVRAP 506
Cdd:cd16917   70 LTIGSRPGGG--TRVTARLP 87
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
156-276 1.86e-07

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: 50.37  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  156 FLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDEKVFRHNVSL-SYEQWLQY 234
Cdd:TIGR00229   4 RYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPvSEERRVRR 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 446732494  235 PDGRKACFEIRKVPYYdRVGKRHGLMGFGRDITERKHYQDAL 276
Cdd:TIGR00229  84 KDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEAL 124
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
528-628 1.96e-07

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: 50.20  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELnVIVA-RSVLEKLGNS--VDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRddlPPLV 604
Cdd:cd17535    1 VLIVDDHPL-VREGlRRLLESEPDIevVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPD---LKVI 76
                         90       100
                 ....*....|....*....|....*
gi 446732494 605 ALTANVLKDK-KEYLDAGMDDVLSK 628
Cdd:cd17535   77 VLTAHDDPEYvLRALKAGAAGYLLK 101
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
350-510 2.14e-07

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 52.70  E-value: 2.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 350 QLDNQPIDFTGFLADLENLSGLQAQQKGLRF---VMEPTLPLPHQVITDGTR-LRQvlwnLISNAVKFTQQGKVEVRVRY 425
Cdd:COG4585  114 GLRPPALDDLGLAAALEELAERLLRAAGIRVeldVDGDPDRLPPEVELALYRiVQE----ALTNALKHAGATRVTVTLEV 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 426 DKGEmLHFEVADSGIGIPQEEqdkifamyyqvkdsqggkpATGTGIGLAVSRRLARDMGGDISVSSVPGQGsvFTLTVRA 505
Cdd:COG4585  190 DDGE-LTLTVRDDGVGFDPEA-------------------APGGGLGLRGMRERAEALGGTLTIGSAPGGG--TRVRATL 247

                 ....*
gi 446732494 506 PAVAE 510
Cdd:COG4585  248 PLAAA 252
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
527-641 2.29e-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: 49.97  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVEDIELNVIVARSVLEKLG-NSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRrysRDDLPPLVA 605
Cdd:cd17542    2 KVLIVDDAAFMRMMLKDILTKAGyEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKK---IDPNAKVIM 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446732494 606 LTANVLKDK-KEYLDAGMDDVLSKPLSVPALTAMIKK 641
Cdd:cd17542   79 CSAMGQEEMvKEAIKAGAKDFIVKPFQPERVLEAVEK 115
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
528-639 2.32e-07

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: 49.74  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVED-IELNVIVARSVLEKlGNSVDVAmtgkaalEMFKPGEY-------DLVLLDIQLPDMTGLDISRELTRRYSRdd 599
Cdd:cd17573    1 ILLIEDdSTLGKEISKGLNEK-GYQADVA-------ESLKDGEYyidirnyDLVLVSDKLPDGNGLSIVSRIKEKHPS-- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446732494 600 lPPLVALTANVLKDKK-EYLDAGMDDVLSKPLSVPALTAMI 639
Cdd:cd17573   71 -IVVIVLSDNPKTEQEiEAFKEGADDYIAKPFDFKVLVARI 110
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
545-593 2.45e-07

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: 49.78  E-value: 2.45e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446732494 545 LEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTR 593
Cdd:cd19922   18 LQKEGYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAEKLSR 66
PRK15479 PRK15479
transcriptional regulator TctD;
526-640 3.23e-07

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 52.03  E-value: 3.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 526 LNVLLVED-IELNVIVARSVLEKlGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDIsreLTRRYSRDDLPPLV 604
Cdd:PRK15479   1 MRLLLAEDnRELAHWLEKALVQN-GFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEV---LQRLRKRGQTLPVL 76
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446732494 605 ALTANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK15479  77 LLTARSaVADRVKGLNVGADDYLPKPFELEELDARLR 113
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
526-642 3.26e-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: 49.75  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 526 LNVLLVEDIELNVIVARSVLEKLGN-SVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRDDLPPLV 604
Cdd:cd17530    1 LRVLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMS 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446732494 605 ALTANVLKDKKEYLDA-GMD--DVLSKPLSVPALTAMIKKF 642
Cdd:cd17530   81 GLDGGILESAETLAGAnGLNllGTLSKPFSPEELTELLTKY 121
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
528-640 3.61e-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: 49.29  E-value: 3.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRddlpPLVALT 607
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHSHV----PILMLT 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446732494 608 ANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd19939   78 ARTEEmDRVLGLEMGADDYLCKPFSPRELLARVR 111
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
395-488 4.18e-07

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: 49.19  E-value: 4.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 395 DGTRLRQVLWNLISNAVKFTQ--QGKVEVRVRY------DKGEMLHFE--VADSGIGIPQEEQDKIFamyyqvkdsQGGK 464
Cdd:cd16932    3 DQIRLQQVLADFLLNAVRFTPspGGWVEIKVSPtkkqigDGVHVIHLEfrITHPGQGLPEELVQEMF---------EENQ 73
                         90       100
                 ....*....|....*....|....
gi 446732494 465 PATGTGIGLAVSRRLARDMGGDIS 488
Cdd:cd16932   74 WTTQEGLGLSISRKLVKLMNGDVR 97
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
544-640 5.00e-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: 5.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 544 VLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtrrysRDDLP-PLVALTANV-LKDKKEYLDAG 621
Cdd:cd17626   19 VLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQI-----RAESGvPIVMLTAKSdTVDVVLGLESG 93
                         90
                 ....*....|....*....
gi 446732494 622 MDDVLSKPLSVPALTAMIK 640
Cdd:cd17626   94 ADDYVAKPFKPKELVARIR 112
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
364-499 7.26e-07

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: 49.17  E-value: 7.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 364 DLENL-SGLQA--QQKGLRFVMEptLPLPHQVITDGTRLRQVLWNLISNAVKFTQqGKVEVRVRYDKGeMLHFEVADSGI 440
Cdd:cd16954    2 LLDSLcSALNKvyQRKGVSISLD--ISPELRFPGERNDLMELLGNLLDNACKWCL-EFVEVTARQTDG-GLHLIVDDDGP 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446732494 441 GIPQEEQDKIFAMYYQVkDSQggkpATGTGIGLAVSRRLARDMGGDISVSSVPGQGSVF 499
Cdd:cd16954   78 GVPESQRSKIFQRGQRL-DEQ----RPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARF 131
orf27 CHL00148
Ycf27; Reviewed
529-640 8.06e-07

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 50.87  E-value: 8.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 529 LLVEDIELNVivaRSVLEK----LGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSrdDLpPLV 604
Cdd:CHL00148   9 ILVVDDEAYI---RKILETrlsiIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEI-RKES--DV-PII 81
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446732494 605 ALTA-NVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:CHL00148  82 MLTAlGDVSDRITGLELGADDYVVKPFSPKELEARIR 118
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
528-640 8.90e-07

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: 48.48  E-value: 8.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRDDLPPLVALT 607
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446732494 608 ANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIK 113
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
399-501 9.57e-07

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: 48.14  E-value: 9.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVKFTQQG-----KVEVRVRYDKGEMLH----------FEVADSGIGIPQEEQDKIFAMYYQVKDSqgG 463
Cdd:cd16919    1 LELAILNLAVNARDAMPEGgrltiETSNQRVDADYALNYrdlipgnyvcLEVSDTGSGMPAEVLRRAFEPFFTTKEV--G 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446732494 464 KpatGTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTL 501
Cdd:cd16919   79 K---GTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRI 113
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
518-629 1.19e-06

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: 48.01  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 518 EDDLPLPALNVLLVEDIELNVIVArsvleklgnsvdVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSR 597
Cdd:cd19925    7 EDDPMVAEIHRAYVEQVPGFTVIG------------TAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHD 74
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446732494 598 DDLppLVALTANVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd19925   75 VDV--IVVTAANDVETVREALRLGVVDYLIKP 104
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
528-640 1.46e-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: 47.62  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMF--KPGEYDLVLLDIQLPDMTGLDISRELTrrySRDDLpPLVA 605
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLreNKDEFDLVITDVHMPDMDGFEFLELIR---LEMDL-PVIM 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446732494 606 LTANVLKDK-KEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd17584   77 MSADGSTSTvMKGLAHGACDYLLKPVSIEDLKNIWQ 112
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
526-594 1.72e-06

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: 47.96  E-value: 1.72e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446732494 526 LNVLLVEDIELNVIVARSVLEKLGN--SVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLD-ISRELTRR 594
Cdd:COG2197    2 IRVLIVDDHPLVREGLRALLEAEPDieVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEaLRRLLTPR 73
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
528-629 1.93e-06

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: 47.51  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFK--PgEYDLVLLDIQLPDMTGLDISRELTRRYSRDDLPPL-- 603
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEqhP-DIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIgi 81
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446732494 604 -----VALTANVLKdkkeyldAGMDDVLSKP 629
Cdd:cd17544   82 sasgdNALSARFIK-------AGANDFLTKP 105
PRK10766 PRK10766
two-component system response regulator TorR;
527-657 3.27e-06

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 48.88  E-value: 3.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVEDiELnVIVARSV--LEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTrrySRDDLPPLV 604
Cdd:PRK10766   4 HILVVED-EP-VTRARLQgyFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELR---SRSTVGIIL 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446732494 605 ALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIKK-FWD---TQDEEESTVAPDD 657
Cdd:PRK10766  79 VTGRTDSIDRIVGLEMGADDYVTKPLELRELLVRVKNlLWRislARQAQPHAQEEDN 135
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
527-629 3.61e-06

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: 46.62  E-value: 3.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVEDielnVIVARSVLEKLGNS------VDVAMTGKAALEM---FKPgeyDLVLLDIQLPDMTGLdisrELTRRYSR 597
Cdd:cd17541    2 RVLIVDD----SAVMRKLLSRILESdpdievVGTARDGEEALEKikeLKP---DVITLDIEMPVMDGL----EALRRIMA 70
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446732494 598 DDLPPLVALTANVLKDKK---EYLDAGMDDVLSKP 629
Cdd:cd17541   71 ERPTPVVMVSSLTEEGAEitlEALELGAVDFIAKP 105
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
526-641 5.38e-06

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 49.64  E-value: 5.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 526 LNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtrRYSRDDLPPLVA 605
Cdd:PRK10365   6 IDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEI--KALNPAIPVLIM 83
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446732494 606 LTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIKK 641
Cdd:PRK10365  84 TAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
544-642 6.05e-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: 6.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 544 VLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSRDDLPPLVALTANVLKDKK-EYLDAGM 622
Cdd:cd17562   19 TLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKEL-RKLPAYKFTPILMLTTESSDEKKqEGKAAGA 97
                         90       100
                 ....*....|....*....|
gi 446732494 623 DDVLSKPLSVPALTAMIKKF 642
Cdd:cd17562   98 TGWLVKPFDPEQLLEVVKKV 117
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
401-493 6.60e-06

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 49.25  E-value: 6.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 401 QVLWNLISNAVKFTQQgKVEVRVRYDkGEMLHFEVADSGIGIPQEEQDKIFamyyqvkdsQGGKPA----TGTGIGLAVS 476
Cdd:PRK10815 381 EVMGNVLDNACKYCLE-FVEISARQT-DEHLHIVVEDDGPGIPESKRELIF---------DRGQRAdtlrPGQGLGLSVA 449
                         90
                 ....*....|....*..
gi 446732494 477 RRLARDMGGDISVSSVP 493
Cdd:PRK10815 450 REITEQYEGKISAGDSP 466
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
372-501 6.77e-06

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 49.45  E-value: 6.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 372 QAQQKGLRFVMEPTLPLpHQVIT--DGTRLRQVLWNLISNAVKF---TQQGKVEVRVRY-DKGEMLHFEVADSGIGIPQE 445
Cdd:PRK15053 405 RARELGLKMVIVPGSQL-SQLPPglDSTEFAAIVGNLLDNAFEAslrSDEGNKIVELFLsDEGDDVVIEVADQGCGVPES 483
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446732494 446 EQDKIFAMYYQVKDSQGGKpatgTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTL 501
Cdd:PRK15053 484 LRDKIFEQGVSTRADEPGE----HGIGLYLIASYVTRCGGVITLEDNDPCGTLFSI 535
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
528-641 7.11e-06

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: 45.79  E-value: 7.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELnvivARSVL------EKLG-NSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRddl 600
Cdd:cd17536    1 VLIVDDEPL----IREGLkklidwEELGfEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPD--- 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446732494 601 PPLVALTANvlkDKKEY----LDAGMDDVLSKPLSVPALTAMIKK 641
Cdd:cd17536   74 IKIIILSGY---DDFEYaqkaIRLGVVDYLLKPVDEEELEEALEK 115
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
419-496 7.67e-06

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: 46.95  E-value: 7.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 419 VEVRVRYDKgEMLHFEVADSGIGIPQEEQDKIFAMYY-----QVKDSQ-----GGKPAT--GTGIGLAVSRRLARDMGGD 486
Cdd:cd16929   73 IKVTVAKGD-EDLTIKISDRGGGIPREDLARLFSYMYstapqPSLDDFsdlisGTQPSPlaGFGYGLPMSRLYAEYFGGD 151
                         90
                 ....*....|
gi 446732494 487 ISVSSVPGQG 496
Cdd:cd16929  152 LDLQSMEGYG 161
PRK10610 PRK10610
chemotaxis protein CheY;
526-644 9.24e-06

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 45.74  E-value: 9.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 526 LNVLLVEDIELNVIVARSVLEKLG-NSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRDDLPPLV 604
Cdd:PRK10610   6 LKFLVVDDFSTMRRIVRNLLKELGfNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLM 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446732494 605 aLTANVlkdKKEYL----DAGMDDVLSKPLSVPALTAMIKKFWD 644
Cdd:PRK10610  86 -VTAEA---KKENIiaaaQAGASGYVVKPFTAATLEEKLNKIFE 125
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
524-641 9.66e-06

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 48.69  E-value: 9.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 524 PALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRddlPPL 603
Cdd:PRK11361   3 AINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETR---TPV 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446732494 604 VALTANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIKK 641
Cdd:PRK11361  80 ILMTAYAeVETAVEALRCGAFDYVIKPFDLDELNLIVQR 118
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
155-221 1.26e-05

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: 43.54  E-value: 1.26e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446732494   155 SFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDEKVFR 221
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-503 2.30e-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: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 399 LRQVLWNLISNAVKFTQQGKVEVRVRYDKGEMLHFEVADSGIGIPQEEQDKIFAMYYQVKDSqggKPATGTGIGLAVSRR 478
Cdd:cd16923    1 LQRVFSNLLSNAIKYSPENTRIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS---RNTEGAGLGLSIAKA 77
                         90       100
                 ....*....|....*....|....*
gi 446732494 479 LARDMGGDISVSSvPGQGSVFTLTV 503
Cdd:cd16923   78 IIELHGGSASAEY-DDNHDLFKVRL 101
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
527-591 2.37e-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: 43.97  E-value: 2.37e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446732494 527 NVLLVEDIE-LNVIVARSvLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISREL 591
Cdd:cd17563    2 SLLLVDDDEvFAERLARA-LERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPL 66
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
526-639 2.46e-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: 44.33  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 526 LNVLLVEDIELNVIVARSVLEKLGNSV-DVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRysrdDLPPLV 604
Cdd:cd19932    1 VRVLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSE----NIAPIV 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446732494 605 ALTANVLKDKKEYL-DAGMDDVLSKPLSVPALTAMI 639
Cdd:cd19932   77 LLTAYSQQDLVERAkEAGAMAYLVKPFSESDLIPAI 112
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
528-629 3.07e-05

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: 43.30  E-value: 3.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDiELNVI-VARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSrdDLPPLVAL 606
Cdd:cd19926    1 VLVVDD-EPDIReLLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLP--QTPVAVIT 77
                         90       100
                 ....*....|....*....|...
gi 446732494 607 TANVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd19926   78 AYGSLDTAIEALKAGAFDFLTKP 100
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
528-641 3.61e-05

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: 43.59  E-value: 3.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRrysRDDLpPLVALT 607
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRA---RSDV-PIIIIS 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446732494 608 ANVLK--DKKEYLDAGMDDVLSKPLSVPALTAMIKK 641
Cdd:cd17594   78 GDRRDeiDRVVGLELGADDYLAKPFGLRELLARVRA 113
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
361-504 4.07e-05

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 43.75  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 361 FLADLENLSGLqaqqkgLRFVME--PTLPLPHQVITDgtrLRQVLWNLISNAVKFTQQ----GKVEVRVRYDKGEmLHFE 434
Cdd:COG2172    4 LPADLEDLGLA------RRAVRAllRELGLDEDDADD---LVLAVSEAVTNAVRHAYGgdpdGPVEVELELDPDG-LEIE 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 435 VADSGIGIPQEEQDkifamyyqvkdsQGGKPATGTGIGLAVSRRLARDMGgdisVSSVPGqGSVFTLTVR 504
Cdd:COG2172   74 VRDEGPGFDPEDLP------------DPYSTLAEGGRGLFLIRRLMDEVE----YESDPG-GTTVRLVKR 126
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
77-153 5.81e-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: 46.30  E-value: 5.81e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446732494  77 VEQLEESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQLEQQ 153
Cdd:COG4942  152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
555-608 5.86e-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: 43.30  E-value: 5.86e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446732494 555 AMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRddlPPLVALTA 608
Cdd:cd17532   30 AENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKP---PLIVFVTA 80
PRK10816 PRK10816
two-component system response regulator PhoP;
526-640 7.45e-05

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 44.73  E-value: 7.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 526 LNVLLVEDielNVIVARSV---LEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLdisrELTRRYSRDD--L 600
Cdd:PRK10816   1 MRVLVVED---NALLRHHLkvqLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGL----SLIRRWRSNDvsL 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446732494 601 PPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK10816  74 PILVLTARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQ 113
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
528-629 7.56e-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: 42.75  E-value: 7.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPG---------EYDLVLLDIQLPDMTGLDISRELTRRYSRD 598
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLakegndlskELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446732494 599 DLPPLVALTANVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
78-153 8.21e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 8.21e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446732494  78 EQLEESRQRLSRLVQKLEEMRERDLSLNVQlkdnIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQLEQQ 153
Cdd:COG1196  267 AELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
525-640 8.64e-05

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 44.71  E-value: 8.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 525 ALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRDDLPPLV 604
Cdd:PRK10161   2 ARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVM 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446732494 605 ALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK10161  82 LTARGEEEDRVRGLETGADDYITKPFSPKELVARIK 117
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
570-640 8.76e-05

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 44.68  E-value: 8.76e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446732494 570 YDLVLLDIQLPDMTGLDISRELtRRYSrdDLpPLVALTANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK10710  55 PDLILLDLMLPGTDGLTLCREI-RRFS--DI-PIVMVTAKIEEiDRLLGLEIGADDYICKPYSPREVVARVK 122
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
180-268 8.84e-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: 42.06  E-value: 8.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  180 CNRAMELLTGKSEKQLVHLKPQDVYAPDVAEKVIETDEKVFRHNVSlsYEQWLQYPDGRKACFEIRKVPYYDRVGKRHGL 259
Cdd:pfam13426   7 VNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVRE--FEVVLYRKDGEPFPVLVSLAPIRDDGGELVGI 84

                  ....*....
gi 446732494  260 MGFGRDITE 268
Cdd:pfam13426  85 IAILRDITE 93
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
528-629 1.41e-04

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: 41.66  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDiELNVIVARS-VLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRrysRDDLPPLVAL 606
Cdd:cd19936    1 IALVDD-DRNILTSVSmALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQ---KSTLPVIFLT 76
                         90       100
                 ....*....|....*....|...
gi 446732494 607 TANVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd19936   77 SKDDEIDEVFGLRMGADDYITKP 99
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
416-503 1.52e-04

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: 43.34  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 416 QGKVEVRVRYDkGEMLHFEVADSGIGIPQE-------EQDKI---------------------FAMYYQVKDsqggkpAT 467
Cdd:cd16916   69 EGTITLRAEHQ-GNQVVIEVSDDGRGIDREkirekaiERGLItadeaatlsddevlnlifapgFSTAEQVTD------VS 141
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446732494 468 GTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLTV 503
Cdd:cd16916  142 GRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRL 177
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
406-503 1.62e-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: 41.64  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 406 LISNAVK--FT---QQGKVEVRVrYDKGEMLHFEVADSGIGIPQEEQDKIfamyyqvkdsqGGKPAT---GTGIGLA-VS 476
Cdd:cd16957    9 LVENAIRhaFPkrkENNEVRVVV-KKDQHKVHVSVSDNGQGIPEERLDLL-----------GKTTVTsekGTGTALEnLN 76
                         90       100
                 ....*....|....*....|....*....
gi 446732494 477 RRLARDMG--GDISVSSVPGQGSVFTLTV 503
Cdd:cd16957   77 RRLIGLFGseACLHIESEVHGGTEVWFVI 105
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
395-503 1.91e-04

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: 41.59  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 395 DGTRLRQVLWNLISNAVKFTQQGKVEVRVRYDKGEM-LHFEVADSGIGIPQEEQdkifAMyyqvkdSQGGKPATGTGIGL 473
Cdd:cd16934   22 RQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVaLEILAVDQGPGIADVDE----AL------RDGFSTGGGLGLGL 91
                         90       100       110
                 ....*....|....*....|....*....|
gi 446732494 474 AVSRRLArdmgGDISVSSVPGQGSVFTLTV 503
Cdd:cd16934   92 GGVRRLA----DEFDLHSAPGRGTVVVARK 117
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
528-640 2.36e-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: 41.11  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSRddlPPLVALT 607
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREI-RQISN---VPIIFIS 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446732494 608 ANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:cd18159   77 SRDDNmDQVMAINMGGDDYITKPFDLDVLLAKIK 110
PRK13435 PRK13435
response regulator; Provisional
523-631 2.52e-04

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 41.96  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 523 LPALNVLLVEDIELNVIVARSVLEKLG-NSVDVAMTGKAALEMFKPGEYDLVLLDIQLPD-MTGLDISRELTRRYSRDdl 600
Cdd:PRK13435   3 LRQLKVLIVEDEALIALELEKLVEEAGhEVVGIAMSSEQAIALGRRRQPDVALVDVHLADgPTGVEVARRLSADGGVE-- 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446732494 601 ppLVALTANVlkDKKEYLDAGMDDVLSKPLS 631
Cdd:PRK13435  81 --VVFMTGNP--ERVPHDFAGALGVIAKPYS 107
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
528-642 2.73e-04

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: 41.39  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtrRYSRDDLPPLVALT 607
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRM--KVIDENIRVIIMTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446732494 608 ANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIKKF 642
Cdd:cd17553   81 YGELDMIQESKELGALTHFAKPFDIDEIRDAVKKY 115
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
78-153 2.80e-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: 2.80e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446732494  78 EQLEESRQRLSRLVQKLEEM---RERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQLEQQ 153
Cdd:COG1196  281 LELEEAQAEEYELLAELARLeqdIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
73-158 2.88e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  73 LSVVVEQLEESRQRLSRLVQKLEEMRERDLSLNVQ---LKDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQ 149
Cdd:COG4372   75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEaeeLQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154

                 ....*....
gi 446732494 150 LEQQSSFLR 158
Cdd:COG4372  155 LEEQLESLQ 163
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
56-163 4.35e-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: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  56 IRSIFFGLLITPWAVYFLSVVVEQLEESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFEQ 135
Cdd:COG4942    1 MRKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446732494 136 LKIEI----KEREETQIQLEQQSSFLRSFLDA 163
Cdd:COG4942   81 LEAELaeleKEIAELRAELEAQKEELAELLRA 112
ompR PRK09468
osmolarity response regulator; Provisional
570-640 4.59e-04

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 42.65  E-value: 4.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446732494 570 YDLVLLDIQLPDMTGLDISRELtrRYSRDDLpPLVALTANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIK 640
Cdd:PRK09468  50 FHLMVLDLMLPGEDGLSICRRL--RSQNNPT-PIIMLTAKGEEvDRIVGLEIGADDYLPKPFNPRELLARIR 118
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
73-163 5.62e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 5.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  73 LSVVVEQLEESRQRLSRLVQKLEEMRERDLSLNVQLKDN---IAQLNQEIAVREKAEAELQETFEQlkieikereetQIQ 149
Cdd:COG3883   25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALqaeIDKLQAEIAEAEAEIEERREELGE-----------RAR 93
                         90
                 ....*....|....
gi 446732494 150 LEQQSSFLRSFLDA 163
Cdd:COG3883   94 ALYRSGGSVSYLDV 107
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
545-641 6.13e-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: 40.27  E-value: 6.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 545 LEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRysRDDLPPL-------VALTANVLKdkkey 617
Cdd:cd17537   20 LRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLAR--GSNIPIIfitghgdVPMAVEAMK----- 92
                         90       100
                 ....*....|....*....|....
gi 446732494 618 ldAGMDDVLSKPLSVPALTAMIKK 641
Cdd:cd17537   93 --AGAVDFLEKPFRDQVLLDAIEQ 114
PRK15369 PRK15369
two component system response regulator;
526-685 6.70e-04

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 41.60  E-value: 6.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 526 LNVLLVEDIEL------NVIVARSVLEKLGNSVDvamtGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYsrdd 599
Cdd:PRK15369   4 YKILLVDDHELiingikNMLAPYPRYKIVGQVDN----GLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRW---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 600 lPPL--VALTANVL-KDKKEYLDAGMDDVLSKPLSVPALTAMI------KKFWD-TQDEEESTVAPDDNSKSQELLdIPM 669
Cdd:PRK15369  76 -PAMniLVLTARQEeHMASRTLAAGALGYVLKKSPQQILLAAIqtvavgKRYIDpALNREAILALLNADDTNPPLL-TPR 153
                        170
                 ....*....|....*.
gi 446732494 670 LEQYLelvgpKLITDG 685
Cdd:PRK15369 154 ERQIL-----KLITEG 164
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
78-153 7.70e-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: 7.70e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446732494  78 EQLEESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQLEQQ 153
Cdd:COG1196  288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
515-627 8.96e-04

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 41.55  E-value: 8.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 515 VFEEDDLPLPALNVLLVEDIELNVIVarsvlEKLGNsvdvamTGKAALEMFKPgeyDLVLLDIQLPDMTGLDISRELTRR 594
Cdd:PRK10701   5 VFVEDDAEVGSLIAAYLAKHDIDVTV-----EPRGD------RAEATILREQP---DLVLLDIMLPGKDGMTICRDLRPK 70
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446732494 595 YSrddlPPLVALTAnvlkdkkeyLDAGMDDVLS 627
Cdd:PRK10701  71 WQ----GPIVLLTS---------LDSDMNHILA 90
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
528-629 1.04e-03

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: 39.28  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 528 VLLVEDielNVIVARSV---LEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtRRYSRDDLPPLV 604
Cdd:cd19927    1 ILLVDD---DPGIRLAVkdyLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKL-RKNADFDTIPVI 76
                         90       100
                 ....*....|....*....|....*.
gi 446732494 605 ALTANVL-KDKKEYLDAGMDDVLSKP 629
Cdd:cd19927   77 FLTAKGMtSDRIKGYNAGCDGYLSKP 102
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
527-595 1.17e-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: 39.31  E-value: 1.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVEDiELNVIVA-RSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRY 595
Cdd:cd17569    2 TILLVDD-EPNILKAlKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERY 70
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
468-503 1.22e-03

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 42.09  E-value: 1.22e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446732494 468 GTGIGLAVSRRLARDMGGDISVSSVPGQGSVFTLTV 503
Cdd:COG0643  381 GRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRL 416
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
528-593 1.44e-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: 38.64  E-value: 1.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446732494 528 VLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPG-EYDLVLLDIQLPDMTGLDISRELTR 593
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGkDIDIVVTDIVMPEMDGIELAREARK 68
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
77-153 1.46e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446732494  77 VEQLEESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQLEQQ 153
Cdd:COG1196  297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
542-608 1.48e-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: 40.47  E-value: 1.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446732494 542 RSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRrysRDDLPPLVALTA 608
Cdd:COG4566   16 AFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAA---RGSPLPVIFLTG 79
PRK11173 PRK11173
two-component response regulator; Provisional
527-636 1.49e-03

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 41.15  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRYSRddlpPLVAL 606
Cdd:PRK11173   5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQANV----ALMFL 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446732494 607 TA---NVlkDKKEYLDAGMDDVLSKPLSVPALT 636
Cdd:PRK11173  81 TGrdnEV--DKILGLEIGADDYITKPFNPRELT 111
PRK09191 PRK09191
two-component response regulator; Provisional
527-608 1.61e-03

two-component response regulator; Provisional


Pssm-ID: 236402 [Multi-domain]  Cd Length: 261  Bit Score: 40.99  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494 527 NVLLVED-----IELNVIVarsvlEKLGNSV-DVAMTGKAALEMFKPGEYDLVLLDIQLPD-MTGLDISRELTRRYSRdd 599
Cdd:PRK09191 139 RVLIIEDepiiaMDLEQLV-----ESLGHRVtGIARTRAEAVALAKKTRPGLILADIQLADgSSGIDAVNDILKTFDV-- 211

                 ....*....
gi 446732494 600 lpPLVALTA 608
Cdd:PRK09191 212 --PVIFITA 218
PRK10693 PRK10693
two-component system response regulator RssB;
554-631 2.44e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 40.74  E-value: 2.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446732494 554 VAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTRRysRDDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLS 631
Cdd:PRK10693   2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNR--GDQTPVLVISATENMADIAKALRLGVQDVLLKPVK 77
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
73-161 2.48e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.77  E-value: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494    73 LSVVVEQLEESRQRLSRLVQKLE----EMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQI 148
Cdd:smart00787 170 LNSIKPKLRDRKDALEEELRQLKqledELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKS 249
                           90
                   ....*....|...
gi 446732494   149 QLEQQSSFLRSFL 161
Cdd:smart00787 250 ELNTEIAEAEKKL 262
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
78-163 3.75e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 3.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  78 EQLEESRQRLSRLVQKLEEMRERDLSLNVQLKD----------NIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQ 147
Cdd:COG4372   52 EELEQAREELEQLEEELEQARSELEQLEEELEElneqlqaaqaELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131
                         90
                 ....*....|....*.
gi 446732494 148 IQLEQQSSFLRSFLDA 163
Cdd:COG4372  132 KQLEAQIAELQSEIAE 147
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
73-153 4.26e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 4.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  73 LSVVVEQLEESRQRLSRLVQKLEEMRERDLslnvQLKDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQLEQ 152
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                 .
gi 446732494 153 Q 153
Cdd:COG1196  380 E 380
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
553-629 4.92e-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: 37.10  E-value: 4.92e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446732494 553 DVAMTGKAALEM--FKPGEYDLVLLDIQLPDMTGLDISRELTRRysRDDLPPLVALTANVLKDKKEYLDAGMDDVLSKP 629
Cdd:cd19928   24 EVRTTGNAATLWrwVEEGEGDLVITDVVMPDENGLDLIPRIKKA--RPDLPIIVMSAQNTLMTAVKAAERGAFEYLPKP 100
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
73-155 5.80e-03

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: 39.75  E-value: 5.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  73 LSVVVEQLEESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQLEQ 152
Cdd:COG4942  162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241

                 ...
gi 446732494 153 QSS 155
Cdd:COG4942  242 RTP 244
PRK12704 PRK12704
phosphodiesterase; Provisional
78-155 6.13e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  78 EQLE-ESRQRLSRLVQKLEEMRERDLSLNVQLkDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQ-LEQQSS 155
Cdd:PRK12704  71 NEFEkELRERRNELQKLEKRLLQKEENLDRKL-ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQeLERISG 149
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
78-163 6.30e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 6.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  78 EQLEESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQLEQQSSFL 157
Cdd:COG1196  403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                 ....*.
gi 446732494 158 RSFLDA 163
Cdd:COG1196  483 LEELAE 488
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
78-163 6.79e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 6.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494  78 EQLEESRQRLSRLVQKLEEMR-ERDLSlnvQLKDNIAQLNQEIAVREKAEAELQETFEQLKIEIKEREETQIQLEQQSSF 156
Cdd:COG1579   66 LEIEEVEARIKKYEEQLGNVRnNKEYE---ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE 142

                 ....*..
gi 446732494 157 LRSFLDA 163
Cdd:COG1579  143 KKAELDE 149
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
73-154 6.84e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 6.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494    73 LSVVVEQLEESRQRLSRLVQKLEEMRERDLSLNVQLKD---NIAQLNQEIAVREKAEAELQETFEQLKIEIkEREETQIQ 149
Cdd:TIGR02168  227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQEleeKLEELRLEVSELEEEIEELQKELYALANEI-SRLEQQKQ 305

                   ....*
gi 446732494   150 LEQQS 154
Cdd:TIGR02168  306 ILRER 310
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
528-579 7.88e-03

phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR)-containing response regulators; Response regulators share the common phosphoacceptor REC domain and different output domains. This subfamily contains uncharacterized response regulators with TPR repeats as the effector or output domain, which might contain between 3 to 16 TPR repeats (each about 34 amino acids). TPR-containing proteins occur in all domains of life and the abundance of TPR-containing proteins in a bacterial proteome is not indicative of virulence. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members in this subfamily may contain inactive REC domains lacking canonical metal-binding and active site residues.


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 36.86  E-value: 7.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446732494 528 VLLVEDIELNVIVARSVLEKLG-NSVDVAMTGKAALEMFKPGEYDLVLLDIQL 579
Cdd:cd17589    1 FLIVDDQPTFRSMLKSMLRSLGvTRIDTASSGEEALRMCENKTYDIVLCDYNL 53
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
73-153 7.98e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 38.26  E-value: 7.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446732494   73 LSVVVEQLEESRQRLSRLVQK-------LEEMRERDLSLNVQLKDNIAQ-------LNQEIAVREKAEAELQETFEQLKI 138
Cdd:pfam06785  85 FKILEETLEELQSEEERLEEElsqkeeeLRRLTEENQQLQIQLQQISQDfaefrleSEEQLAEKQLLINEYQQTIEEQRS 164
                          90
                  ....*....|....*
gi 446732494  139 EIKEREETQIQLEQQ 153
Cdd:pfam06785 165 VLEKRQDQIENLESK 179
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
528-601 9.03e-03

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 36.87  E-value: 9.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446732494 528 VLLVEDIELnVIVARSVLEKLGNSVDV---AMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELtrrysRDDLP 601
Cdd:cd19930    1 VLIAEDQEM-VRGALAALLELEDDLEVvaqASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAEL-----REELP 71
 
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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