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Conserved domains on  [gi|2027583119|ref|WP_210789385|]
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aerobic respiration two-component sensor histidine kinase ArcB [Providencia rettgeri]

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
1-780 0e+00

aerobic respiration control sensor protein ArcB; Provisional


:

Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 1469.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119   1 MKVLRGLAQYYVDLMMKLGLVRFSLLLASALVVLAMIMQMAVTIFLRGHVDSLDMVGSIFFGLIITPLAVYFLSVVVEQL 80
Cdd:PRK11091    1 MKQIRLLAQYYVDLMVKLGLVRFSLLLALALVVLAMVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  81 EESRQRLSRMVDKLEVMRKRDAELNIQLHGNIEQLNLEIQEREKAERAHLELLEQLKQEMKYREQTQVELEQQSVLLRSF 160
Cdd:PRK11091   81 EESRQRLSRLVAKLEEMRERDLELNVQLKDNIAQLNQEIAEREKAEEARQEAFEQLKNEIKEREETQIELEQQSSLLRSF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 161 LDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFRHNVSLTYEQWLVYPDGRKA 240
Cdd:PRK11091  161 LDASPDLVYYRNEDGEFSGCNRAMELLTGKSEKQLIGLTPKDVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 241 CFELRKVPFYDRVGKRHGLMGFGRDITERKRYQEALENASREKTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQSSY 320
Cdd:PRK11091  241 CFELRKVPFYDRVGKRHGLMGFGRDITERKRYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 321 LKTIHVSAVTLGNIFNDVIEMDKIERRKVQLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPKTVLTDGTRLR 400
Cdd:PRK11091  321 LKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLR 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 401 QVLWNLIGNAVKFTQQGEVKVSIWQEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGGKPATGTGIGLSVSRRLA 480
Cdd:PRK11091  401 QILWNLISNAVKFTQQGGVTVRVRYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKPATGTGIGLAVSKRLA 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 481 QNMGGDIQVESEIGQGSTFTLSITAPVVEEVAEHQDSDDDYPLPALHILLVEDIELNVVVACSVLENLGNTVDVAMNGKD 560
Cdd:PRK11091  481 QAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVEDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKE 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 561 ALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLPPLIALTANVLKDKKEYFDAGMDGVLSKPLSVPALTQVIE 640
Cdd:PRK11091  561 ALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 641 QFWGEHTSQnEEVENCDVTSQVDESILDCDMLEQYIELVGPKLIYDGLDVFEKMLPGYLAILDSNMVAKDQKGIVEEAHK 720
Cdd:PRK11091  641 KFWDTQDDE-ESTVTTEESSKANEALLDIPMLEQYVELVGPKLITDSLAVFEKMMPGYLSVLDSNLTARDQKGIVEEAHK 719
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 721 IKGAAGSVGLKNLQKIAQQIQSPDLPAWWDNVQEWVDELKQDWKADIETLRNWVDERTKK 780
Cdd:PRK11091  720 IKGAAGSVGLRHLQQLAQQIQSPDLPAWWDNVQDWVEELKNEWRHDVEVLKAWLAQAEKK 779
 
Name Accession Description Interval E-value
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
1-780 0e+00

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 1469.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119   1 MKVLRGLAQYYVDLMMKLGLVRFSLLLASALVVLAMIMQMAVTIFLRGHVDSLDMVGSIFFGLIITPLAVYFLSVVVEQL 80
Cdd:PRK11091    1 MKQIRLLAQYYVDLMVKLGLVRFSLLLALALVVLAMVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  81 EESRQRLSRMVDKLEVMRKRDAELNIQLHGNIEQLNLEIQEREKAERAHLELLEQLKQEMKYREQTQVELEQQSVLLRSF 160
Cdd:PRK11091   81 EESRQRLSRLVAKLEEMRERDLELNVQLKDNIAQLNQEIAEREKAEEARQEAFEQLKNEIKEREETQIELEQQSSLLRSF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 161 LDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFRHNVSLTYEQWLVYPDGRKA 240
Cdd:PRK11091  161 LDASPDLVYYRNEDGEFSGCNRAMELLTGKSEKQLIGLTPKDVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 241 CFELRKVPFYDRVGKRHGLMGFGRDITERKRYQEALENASREKTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQSSY 320
Cdd:PRK11091  241 CFELRKVPFYDRVGKRHGLMGFGRDITERKRYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 321 LKTIHVSAVTLGNIFNDVIEMDKIERRKVQLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPKTVLTDGTRLR 400
Cdd:PRK11091  321 LKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLR 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 401 QVLWNLIGNAVKFTQQGEVKVSIWQEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGGKPATGTGIGLSVSRRLA 480
Cdd:PRK11091  401 QILWNLISNAVKFTQQGGVTVRVRYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKPATGTGIGLAVSKRLA 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 481 QNMGGDIQVESEIGQGSTFTLSITAPVVEEVAEHQDSDDDYPLPALHILLVEDIELNVVVACSVLENLGNTVDVAMNGKD 560
Cdd:PRK11091  481 QAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVEDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKE 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 561 ALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLPPLIALTANVLKDKKEYFDAGMDGVLSKPLSVPALTQVIE 640
Cdd:PRK11091  561 ALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 641 QFWGEHTSQnEEVENCDVTSQVDESILDCDMLEQYIELVGPKLIYDGLDVFEKMLPGYLAILDSNMVAKDQKGIVEEAHK 720
Cdd:PRK11091  641 KFWDTQDDE-ESTVTTEESSKANEALLDIPMLEQYVELVGPKLITDSLAVFEKMMPGYLSVLDSNLTARDQKGIVEEAHK 719
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 721 IKGAAGSVGLKNLQKIAQQIQSPDLPAWWDNVQEWVDELKQDWKADIETLRNWVDERTKK 780
Cdd:PRK11091  720 IKGAAGSVGLRHLQQLAQQIQSPDLPAWWDNVQDWVEELKNEWRHDVEVLKAWLAQAEKK 779
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
266-773 7.49e-112

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: 362.94  E-value: 7.49e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 266 ITERKRYQEAlENASREKTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQSSYLKTIHVSAVTLGNIFNDVIEMDKIE 345
Cdd:TIGR02956 448 KNHAKARAEA-EEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIE 526
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 346 RRKVQLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPKTVLTDGTRLRQVLWNLIGNAVKFTQQGEVKVSIWQ 425
Cdd:TIGR02956 527 AGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 426 EPENKIFFRVKDSGIGIPQDELDKIFAMYYQVTdsaGGKPATGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSITA 505
Cdd:TIGR02956 607 NDDSSLLFEVEDTGCGIAEEEQATLFDAFTQAD---GRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL 683
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 506 PVVEEVaehQDSDDDYP--LPALHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMT 583
Cdd:TIGR02956 684 TRGKPA---EDSATLTVidLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGD 760
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 584 GLDISRQLKQQYDKEDLPPLIALTANVLKDKKE-YFDAGMDGVLSKPLSVPALTQVI-------------------EQFW 643
Cdd:TIGR02956 761 GVTLLQQLRAIYGAKNEVKFIAFSAHVFNEDVAqYLAAGFDGFLAKPVVEEQLTAMIavilaggksnteapvlsasPSFD 840
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 644 GEHTSQNEEVENCDVTSQVDESILDCDMLEQYIELVGPKLIYDGLDVFEKMLPGYLAILDSNMVAKDQKGIVEEAHKIKG 723
Cdd:TIGR02956 841 SASVIENAQADDIPESNQASEFLLDEEQLQQDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQIKKLAHKLKG 920
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 2027583119 724 AAGSVGLKNLQKIAQQIQSPDLPAWWDNVQewVDELKQDWKADIETLRNW 773
Cdd:TIGR02956 921 SAGSLGLTQLTQLCQQLEKQGKTGALELSD--IDEIKQAWQASKTALDQW 968
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
274-503 1.43e-67

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 226.71  E-value: 1.43e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 274 EALENASREKTTFISTISHELRTPLNGIVGLSRILLDTnLTSEQSSYLKTIHVSAVTLGNIFNDVIEMDKIERRKVQLDN 353
Cdd:COG0642   101 LLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEP 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 354 QPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPkTVLTDGTRLRQVLWNLIGNAVKFTQQGE-VKVSIWQEpENKIF 432
Cdd:COG0642   180 EPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKYTPEGGtVTVSVRRE-GDRVR 257
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2027583119 433 FRVKDSGIGIPQDELDKIFAMYYQVTDSAGGKpatGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:COG0642   258 ISVEDTGPGIPPEDLERIFEPFFRTDPSRRGG---GTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTL 325
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
399-503 1.16e-44

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: 155.73  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVKFTQQGEVKVSIW----QEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVtDSAGGKPATGTGIGLS 474
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSleeeEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQA-DSSTTRKYGGTGLGLA 79
                          90       100
                  ....*....|....*....|....*....
gi 2027583119 475 VSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:cd16922    80 ISKKLVELMGGDISVESEPGQGSTFTFTL 108
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
394-503 1.62e-33

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 124.30  E-value: 1.62e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  394 TDGTRLRQVLWNLIGNAVKFT-QQGEVKVSIWQEPENkIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGGKPatGTGIG 472
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDH-VEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIG--GTGLG 77
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2027583119  473 LSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:smart00387  78 LSIVKKLVELHGGEISVESEPGGGTTFTITL 108
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
394-503 1.19e-31

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: 119.01  E-value: 1.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 394 TDGTRLRQVLWNLIGNAVKFT-QQGEVKVSIwqEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGGkpatGTGIG 472
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAaKAGEITVTL--SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGG----GTGLG 74
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2027583119 473 LSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:pfam02518  75 LSIVRKLVELLGGTITVESEPGGGTTVTLTL 105
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
265-503 9.74e-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: 119.09  E-value: 9.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 265 DITErkryQEALENASREkttFISTISHELRTPlngivglsrilldtnLTSEQsSYLKTIHVSAV---TLGNIF------ 335
Cdd:NF033092  361 DVTE----QEKIEQERRE---FVANVSHELRTP---------------LTTMR-SYLEALADGAWkdpELAPRFlgvtqn 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 336 ---------NDVIEMDKIERRKVQLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDvaptLPKTVLT---DGTRLRQVL 403
Cdd:NF033092  418 etermirlvNDLLQLSRMDSKDYKLNKEWVNFNEFFNYIIDRFEMILKNKNITFKRE----FPKRDLWveiDTDKITQVL 493
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 404 WNLIGNAVKFTQQ-GEVKVSIwQEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVtDSAGGKPATGTGIGLSVSRRLAQN 482
Cdd:NF033092  494 DNIISNAIKYSPEgGTITFRL-LETHNRIIISISDQGLGIPKKDLDKIFDRFYRV-DKARSRKMGGTGLGLAIAKEVVEA 571
                         250       260
                  ....*....|....*....|.
gi 2027583119 483 MGGDIQVESEIGQGSTFTLSI 503
Cdd:NF033092  572 HGGRIWAESEEGKGTTIYFTL 592
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
276-503 8.03e-22

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 99.71  E-value: 8.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 276 LENASREKTTFISTISHELRTPLNGI------VGLSRILLDTnlTSEQSSYLktIHVSAVTLGNIFNDVIEMDKIERRKV 349
Cdd:NF040691  264 LEELSRLQQRFVSDVSHELRTPLTTIrmaadvIHDSRDDFDP--ATARSAEL--LHTELDRFESLLSDLLEISRFDAGAA 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 350 QLDNQPVALPEFVND-LENLSGLLVQpKGLKFVMDvAPTLPKTVLTDGTRLRQVLWNLIGNAVKFTQQGEVKVSIWQEpE 428
Cdd:NF040691  340 ELDVEPVDLRPLVRRvVDALRQLAER-AGVELRVD-APGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVAQD-D 416
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2027583119 429 NKIFFRVKDSGIGIPQDELDKIFAMYYQvTDSAGGKPATGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:NF040691  417 TAVAVTVRDHGVGLKPGEVALVFDRFWR-ADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTL 490
 
Name Accession Description Interval E-value
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
1-780 0e+00

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 1469.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119   1 MKVLRGLAQYYVDLMMKLGLVRFSLLLASALVVLAMIMQMAVTIFLRGHVDSLDMVGSIFFGLIITPLAVYFLSVVVEQL 80
Cdd:PRK11091    1 MKQIRLLAQYYVDLMVKLGLVRFSLLLALALVVLAMVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  81 EESRQRLSRMVDKLEVMRKRDAELNIQLHGNIEQLNLEIQEREKAERAHLELLEQLKQEMKYREQTQVELEQQSVLLRSF 160
Cdd:PRK11091   81 EESRQRLSRLVAKLEEMRERDLELNVQLKDNIAQLNQEIAEREKAEEARQEAFEQLKNEIKEREETQIELEQQSSLLRSF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 161 LDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFRHNVSLTYEQWLVYPDGRKA 240
Cdd:PRK11091  161 LDASPDLVYYRNEDGEFSGCNRAMELLTGKSEKQLIGLTPKDVYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRKA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 241 CFELRKVPFYDRVGKRHGLMGFGRDITERKRYQEALENASREKTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQSSY 320
Cdd:PRK11091  241 CFELRKVPFYDRVGKRHGLMGFGRDITERKRYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 321 LKTIHVSAVTLGNIFNDVIEMDKIERRKVQLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPKTVLTDGTRLR 400
Cdd:PRK11091  321 LKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLR 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 401 QVLWNLIGNAVKFTQQGEVKVSIWQEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGGKPATGTGIGLSVSRRLA 480
Cdd:PRK11091  401 QILWNLISNAVKFTQQGGVTVRVRYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKPATGTGIGLAVSKRLA 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 481 QNMGGDIQVESEIGQGSTFTLSITAPVVEEVAEHQDSDDDYPLPALHILLVEDIELNVVVACSVLENLGNTVDVAMNGKD 560
Cdd:PRK11091  481 QAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVEDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKE 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 561 ALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLPPLIALTANVLKDKKEYFDAGMDGVLSKPLSVPALTQVIE 640
Cdd:PRK11091  561 ALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIK 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 641 QFWGEHTSQnEEVENCDVTSQVDESILDCDMLEQYIELVGPKLIYDGLDVFEKMLPGYLAILDSNMVAKDQKGIVEEAHK 720
Cdd:PRK11091  641 KFWDTQDDE-ESTVTTEESSKANEALLDIPMLEQYVELVGPKLITDSLAVFEKMMPGYLSVLDSNLTARDQKGIVEEAHK 719
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 721 IKGAAGSVGLKNLQKIAQQIQSPDLPAWWDNVQEWVDELKQDWKADIETLRNWVDERTKK 780
Cdd:PRK11091  720 IKGAAGSVGLRHLQQLAQQIQSPDLPAWWDNVQDWVEELKNEWRHDVEVLKAWLAQAEKK 779
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
266-773 7.49e-112

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: 362.94  E-value: 7.49e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 266 ITERKRYQEAlENASREKTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQSSYLKTIHVSAVTLGNIFNDVIEMDKIE 345
Cdd:TIGR02956 448 KNHAKARAEA-EEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIE 526
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 346 RRKVQLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPKTVLTDGTRLRQVLWNLIGNAVKFTQQGEVKVSIWQ 425
Cdd:TIGR02956 527 AGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 426 EPENKIFFRVKDSGIGIPQDELDKIFAMYYQVTdsaGGKPATGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSITA 505
Cdd:TIGR02956 607 NDDSSLLFEVEDTGCGIAEEEQATLFDAFTQAD---GRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL 683
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 506 PVVEEVaehQDSDDDYP--LPALHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMT 583
Cdd:TIGR02956 684 TRGKPA---EDSATLTVidLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGD 760
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 584 GLDISRQLKQQYDKEDLPPLIALTANVLKDKKE-YFDAGMDGVLSKPLSVPALTQVI-------------------EQFW 643
Cdd:TIGR02956 761 GVTLLQQLRAIYGAKNEVKFIAFSAHVFNEDVAqYLAAGFDGFLAKPVVEEQLTAMIavilaggksnteapvlsasPSFD 840
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 644 GEHTSQNEEVENCDVTSQVDESILDCDMLEQYIELVGPKLIYDGLDVFEKMLPGYLAILDSNMVAKDQKGIVEEAHKIKG 723
Cdd:TIGR02956 841 SASVIENAQADDIPESNQASEFLLDEEQLQQDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQIKKLAHKLKG 920
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 2027583119 724 AAGSVGLKNLQKIAQQIQSPDLPAWWDNVQewVDELKQDWKADIETLRNW 773
Cdd:TIGR02956 921 SAGSLGLTQLTQLCQQLEKQGKTGALELSD--IDEIKQAWQASKTALDQW 968
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
274-503 1.43e-67

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 226.71  E-value: 1.43e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 274 EALENASREKTTFISTISHELRTPLNGIVGLSRILLDTnLTSEQSSYLKTIHVSAVTLGNIFNDVIEMDKIERRKVQLDN 353
Cdd:COG0642   101 LLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEP 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 354 QPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPkTVLTDGTRLRQVLWNLIGNAVKFTQQGE-VKVSIWQEpENKIF 432
Cdd:COG0642   180 EPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKYTPEGGtVTVSVRRE-GDRVR 257
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2027583119 433 FRVKDSGIGIPQDELDKIFAMYYQVTDSAGGKpatGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:COG0642   258 ISVEDTGPGIPPEDLERIFEPFFRTDPSRRGG---GTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTL 325
PRK15347 PRK15347
two component system sensor kinase;
273-741 4.90e-67

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 239.16  E-value: 4.90e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 273 QEAlENASREKTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQSSYLKTIHVSAVTLGNIFNDVIEMDKIERRKVQLD 352
Cdd:PRK15347  389 QRA-EQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLS 467
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 353 NQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPKTVLTDGTRLRQVLWNLIGNAVKFTQQGEVKVSIWQEpENKIF 432
Cdd:PRK15347  468 LEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVKRH-EQQLC 546
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 433 FRVKDSGIGIPQDELDKIFAMYYQVTDSAGgkpatGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTL----------- 501
Cdd:PRK15347  547 FTVEDTGCGIDIQQQQQIFTPFYQADTHSQ-----GTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLvlplneyappe 621
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 502 ----SITAPV----------VEEVAEHQDSDDDYP----LPA---------------------------LHILLVEDIEL 536
Cdd:PRK15347  622 plkgELSAPLalhrqlsawgITCQPGHQNPALLDPelayLPGrlydllqqiiqgapnepvinlplqpwqLQILLVDDVET 701
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 537 NVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLP-PLIALTANVL-KDK 614
Cdd:PRK15347  702 NRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDPDcMIVALTANAApEEI 781
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 615 KEYFDAGMDGVLSKPLSVPALTQVIeqfwgEHTSQNEEVENCDVTSQVDEsildCDMLeqyIELVGPKL---IYDGLDVF 691
Cdd:PRK15347  782 HRCKKAGMNHYLTKPVTLAQLARAL-----ELAAEYQLLRGIELSPQDSS----CSPL---LDTDDMALnskLYQSLLLL 849
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 2027583119 692 EKMLPGYLAildsnmvakDQKGIVEEAHKIKGAAGSVGLKNLQKIAQQIQ 741
Cdd:PRK15347  850 LAQIEQAVE---------NQEVLSQLLHTLKGCAGQAGLTELQCAVIDLE 890
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
268-503 3.58e-66

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 219.39  E-value: 3.58e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 268 ERKRYQEALENASREKTTFISTISHELRTPLNGIVGLSRILLD--TNLTSEQSSYLKTIHVSAVTLGNIFNDVIEMDKIE 345
Cdd:COG2205     1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDeeDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 346 RRKVQLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPkTVLTDGTRLRQVLWNLIGNAVKFTQQG-EVKVSIW 424
Cdd:COG2205    81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELP-LVYADPELLEQVLANLLDNAIKYSPPGgTITISAR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2027583119 425 QEpENKIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGGKpatGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:COG2205   160 RE-GDGVRISVSDNGPGIPEEELERIFERFYRGDNSRGEG---GTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
270-742 2.75e-61

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 222.80  E-value: 2.75e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 270 KRYQEAlenaSREKTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQSSYLKTIHVSAVTLGNIFNDVIEMDKIERRKV 349
Cdd:PRK11107  284 KRAQEA----ARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKL 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 350 QLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPKTVLTDGTRLRQVLWNLIGNAVKFTQQGEVKVSIWQEPEN 429
Cdd:PRK11107  360 VLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALS 439
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 430 ----KIFFRVKDSGIGIPQDELDKIFAMYYQvTDSAGGKPATGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSITA 505
Cdd:PRK11107  440 ntkvQLEVQIRDTGIGISERQQSQLFQAFRQ-ADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPL 518
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 506 PVVEEVAEhqdsdDDYPLPAL---HILLVE----------------------------------DIEL------------ 536
Cdd:PRK11107  519 DLNPNPII-----DGLPTDCLagkRLLYVEpnsaaaqatldilsetplevtysptlsqlpeahyDILLlglpvtfreplt 593
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 537 --------------NVVVAC-------------------------------------------------------SV--- 544
Cdd:PRK11107  594 mlherlakaksmtdFLILALpcheqvlaeqlkqdgadaclskplshtrllpallepchhkqppllpptdesrlplTVmav 673
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 545 -------------LENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDlPPLIALTANVL 611
Cdd:PRK11107  674 ddnpanlkligalLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQN-TPIIAVTAHAM 752
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 612 KDKKEYF-DAGMDGVLSKPLSVPALTQVIEQFW-GEHTSQNEEVENCDVTSQVDESILDCDM-LEQyielVGPK--LIYD 686
Cdd:PRK11107  753 AGERERLlSAGMDDYLAKPIDEAMLKQVLLRYKpGPKFTSRVVAPEPPEPVHFPNATLDWQLaLRQ----AAGKpdLARD 828
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2027583119 687 GLDVFEKMLPGYLAILDSNMVAKDQKGIVEEAHKIKGAAGSVGLKNLQKIAQQIQS 742
Cdd:PRK11107  829 MLQMLLDFLPEVRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQ 884
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
247-510 3.36e-60

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 208.64  E-value: 3.36e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 247 VPFYDRVGKRHGLMGFGRDITERKRYQEAlenasreKTTFISTISHELRTPLNGIVGLSRILLD--TNLTSEQSSYLKTI 324
Cdd:COG5002   136 LRLSALLLGLLLLAAVERDITELERLEQM-------RREFVANVSHELRTPLTSIRGYLELLLDgaADDPEERREYLEII 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 325 HVSAVTLGNIFNDVIEMDKIERRKVQLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPkTVLTDGTRLRQVLW 404
Cdd:COG5002   209 LEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPL-LVLGDPDRLEQVLT 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 405 NLIGNAVKFTQQG-EVKVSIWQEpENKIFFRVKDSGIGIPQDELDKIFAMYYQVtDSAGGKPATGTGIGLSVSRRLAQNM 483
Cdd:COG5002   288 NLLDNAIKYTPEGgTITVSLREE-DDQVRISVRDTGIGIPEEDLPRIFERFYRV-DKSRSRETGGTGLGLAIVKHIVEAH 365
                         250       260
                  ....*....|....*....|....*..
gi 2027583119 484 GGDIQVESEIGQGSTFTLSItaPVVEE 510
Cdd:COG5002   366 GGRIWVESEPGKGTTFTITL--PLARE 390
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
266-747 3.05e-59

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 216.70  E-value: 3.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 266 ITERKRYQEAlENASREKTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQSSYLKTIHVSAVTLGNIFNDVIEMDKIE 345
Cdd:PRK11466  428 IEHRQARAEA-EKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIE 506
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 346 --RRKVQLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPKTVLTDGTRLRQVLWNLIGNAVKFTQQGEVKVSI 423
Cdd:PRK11466  507 agGKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRS 586
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 424 WQEpENKIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGgkpatGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:PRK11466  587 RTD-GEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGKRG-----GTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRL 660
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 504 -----TAPVVEEVAEHQDSDDdyplpaLHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGE-YDLVLLDI 577
Cdd:PRK11466  661 plrvaTAPVPKTVNQAVRLDG------LRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEpFAAALVDF 734
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 578 QLPDMTGLDISRQLKQQYdkedlPPL--IALTANVLKDKKEYFDAGM-DGVLSKPLSVPALTQVIeqfwgEHTSQneeve 654
Cdd:PRK11466  735 DLPDYDGITLARQLAQQY-----PSLvlIGFSAHVIDETLRQRTSSLfRGIIPKPVPREVLGQLL-----AHYLQ----- 799
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 655 ncdVTSQVDESiLDCDMLEQYIELVGPKLIYDGLDVFEKMLPGYLAILDSNMVAKDQKGIVEEAHKIKGAAGSVGLKNLQ 734
Cdd:PRK11466  800 ---LQVNNDQP-LDVSQLNEDAALMGTEKIHEWLALFKQHALPLLDEIDIARASQDSEKIKRAAHQLKSSCSSLGMRQAS 875
                         490
                  ....*....|...
gi 2027583119 735 KIAQQIQSPDLPA 747
Cdd:PRK11466  876 QACAQLEQQPLSA 888
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
136-762 1.18e-52

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 198.42  E-value: 1.18e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  136 LKQEMKYREQTQVELEQQSVLLRSFLDASPDLVYYRNENNEFSGCNRAME-LLTGKSEKHlvGLTPLDIYDVEIASKVME 214
Cdd:PRK09959   557 LLRSVRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFEhYFTADYYKN--AMLPLENSDSPFKDVFSN 634
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  215 TDEKVFRHNVSLT-YEQWLVYPDG-RKACFE----LRKVPfydrvGKRHGLMGFG-RDITERKRYQEALE-------NAS 280
Cdd:PRK09959   635 AHEVTAETKENRTiYTQVFEIDNGiEKRCINhwhtLCNLP-----ASDHAVYICGwQDITETRDLIHALEvernkaiNAT 709
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  281 REKTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQS-SYLKTIHVSAVTLGNIFNDVIEMDKIERRKVQLDNQPVALP 359
Cdd:PRK09959   710 VAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIP 789
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  360 EFVNDLENLSGLLVQPKGLkfVMDVAPTLPKTVLT--DGTRLRQVLWNLIGNAVKFTQQGEVKV--SIWQEPENKIFFR- 434
Cdd:PRK09959   790 TLVQNTCHSFGAIAASKSI--ALSCSSTFPDHYLVkiDPQAFKQVLSNLLSNALKFTTEGAVKIttSLGHIDDNHAVIKm 867
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  435 -VKDSGIGIPQDELDKIFAMYYQvtdSAGGKPATGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSITAPVVEEVAE 513
Cdd:PRK09959   868 tIMDSGSGLSQEEQQQLFKRYSQ---TSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQVAT 944
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  514 -HQDSDDDYPLP-ALHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQL 591
Cdd:PRK09959   945 vEAKAEQPITLPeKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKL 1024
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  592 KQQYDKedlPPLIALTANVLKDKKEY-FDAGMDGVLSKPLSVPALTQVIEQFwgeHTSQN--EEVENCDVTSQVDESILD 668
Cdd:PRK09959  1025 REQNSS---LPIWGLTANAQANEREKgLSCGMNLCLFKPLTLDVLKTHLSQL---HQVAHiaPQYRHLDIEALKNNTAND 1098
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  669 CDMLEQYIELVGPKLiydgldvfEKMLPGYLAILDsnmvAKDQKGIVEEAHKIKGAAGSVGLKNLQKIAQQIQ------- 741
Cdd:PRK09959  1099 LQLMQEILMTFQHET--------HKDLPAAFHALE----AGDNRTFHQCIHRIHGAANILNLQKLINISHQLEitpvsdd 1166
                          650       660
                   ....*....|....*....|..
gi 2027583119  742 -SPDLPAWWDNVQEWVDELKQD 762
Cdd:PRK09959  1167 sKPEILQLLNSVKEHIAELDQE 1188
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
149-514 1.89e-51

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 183.51  E-value: 1.89e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 149 ELEQQSVLLRSFLDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIydVEIASKVMETDEKVFRHNVSLT- 227
Cdd:COG3852     1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAEL--FPEDSPLRELLERALAEGQPVTe 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 228 YEQWLVYPDGRKACFELRKVPFYDRVGKRhGLMGFGRDITERKRYQEALENASREKT--TFISTISHELRTPLNGIVGLS 305
Cdd:COG3852    79 REVTLRRKDGEERPVDVSVSPLRDAEGEG-GVLLVLRDITERKRLERELRRAEKLAAvgELAAGLAHEIRNPLTGIRGAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 306 RILLDTNLTSEQSSYLKTIHVSAVTLGNIfndvieMDKIER--RKVQLDNQPVALPEFVNDLENLSGLLVqPKGLKFVMD 383
Cdd:COG3852   158 QLLERELPDDELREYTQLIIEEADRLNNL------VDRLLSfsRPRPPEREPVNLHEVLERVLELLRAEA-PKNIRIVRD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 384 VAPTLPkTVLTDGTRLRQVLWNLIGNAVK-FTQQGEVKVSIWQE---------PENKIFFRVKDSGIGIPQDELDKIFam 453
Cdd:COG3852   231 YDPSLP-EVLGDPDQLIQVLLNLVRNAAEaMPEGGTITIRTRVErqvtlgglrPRLYVRIEVIDNGPGIPEEILDRIF-- 307
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2027583119 454 YYQVTdsagGKPaTGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSItaPVVEEVAEH 514
Cdd:COG3852   308 EPFFT----TKE-KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYL--PLEQAEEEP 361
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
4-503 2.16e-49

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 181.91  E-value: 2.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119   4 LRGLAQYYVDLMMKLGLVRFSLLLASALVVLAMIMQMAVTIFLRGHVDSLDMVGSIFFGLIITPLAVYFLSVVVEQLEES 83
Cdd:COG4251     3 LLALLLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  84 RQRLSRMVDKLEVMRKRDAELNIQLHGNIEQLNLEIQEREKAERAHLELLEQLKQEMKYREQTQVELEQQSVLLRSFLDA 163
Cdd:COG4251    83 LLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 164 SPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFRHNVSLTYEQWLVYPDGRKACFE 243
Cdd:COG4251   163 LLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 244 LRKVPFYDRVGKRHGLMGFGRDITERKRYQEALENASREKTTFISTISHELRTPLNGIVGLSRILLD---TNLTSEQSSY 320
Cdd:COG4251   243 LLLLLLILVLELLELRLELEELEEELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEdygDKLDEEGREY 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 321 LKTIHVSAVTLGNIFNDVIEMDKIERRkvQLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTlpktVLTDGTRLR 400
Cdd:COG4251   323 LERIRDAAERMQALIDDLLAYSRVGRQ--ELEFEPVDLNELLEEVLEDLEPRIEERGAEIEVGPLPT----VRGDPTLLR 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 401 QVLWNLIGNAVKFTQQGEV-KVSI-WQEPENKIFFRVKDSGIGIPQDELDKIFAMYyQVTDSAGGKPatGTGIGLSVSRR 478
Cdd:COG4251   397 QVFQNLISNAIKYSRPGEPpRIEIgAEREGGEWVFSVRDNGIGIDPEYAEKIFEIF-QRLHSRDEYE--GTGIGLAIVKK 473
                         490       500
                  ....*....|....*....|....*
gi 2027583119 479 LAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:COG4251   474 IVERHGGRIWVESEPGEGATFYFTL 498
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
139-503 1.26e-45

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: 170.54  E-value: 1.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 139 EMKYREQtqvELEQQSVLLRSFLDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEK 218
Cdd:COG5809   128 ERKRMEE---ALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQ 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 219 VFRHNVSLTYEQWLVYPDGRKACFELRKVPFyDRVGKRHGLMGFGRDITERKRYQEALENAsrEKTTFIS----TISHEL 294
Cdd:COG5809   205 LLKDGGIAQGEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVIIFRDITERKKLEELLRKS--EKLSVVGelaaGIAHEI 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 295 RTPLNGIVGLSRILLDTNlTSEQSSYLKTIHVSAVTLGNIFNDVIEMDKIERRKVQldnqPVALPEFVNDLEnlsgLLVQ 374
Cdd:COG5809   282 RNPLTSLKGFIQLLKDTI-DEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYE----PKDLNTLIEEVI----PLLQ 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 375 P----KGLKFVMDVAPTLPkTVLTDGTRLRQVLWNLIGNAVKFT-QQGEVKVSIWQEPENKIFFRVKDSGIGIPQDELDK 449
Cdd:COG5809   353 PqallKNVQIELELEDDIP-DILGDENQLKQVFINLLKNAIEAMpEGGNITIETKAEDDDKVVISVTDEGCGIPEERLKK 431
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2027583119 450 IFAMYYQVTDsaggkpaTGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:COG5809   432 LGEPFYTTKE-------KGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITL 478
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
399-503 1.16e-44

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: 155.73  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVKFTQQGEVKVSIW----QEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVtDSAGGKPATGTGIGLS 474
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSleeeEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQA-DSSTTRKYGGTGLGLA 79
                          90       100
                  ....*....|....*....|....*....
gi 2027583119 475 VSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:cd16922    80 ISKKLVELMGGDISVESEPGQGSTFTFTL 108
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
59-512 5.63e-40

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: 152.81  E-value: 5.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  59 IFFGLIITPLAVYFLSVVVEQLEESRQRLSRMVDKLevmrkRDAELNIQLHgniEQLNLEIQErekAERAHLELLEQLKQ 138
Cdd:COG5000    12 LLIALLLLLLALWLALLLARRLTRPLRRLAEATRAV-----AAGDLSVRLP---VTGDDEIGE---LARAFNRMTDQLKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 139 EmkyreqtQVELEQQSVLLRSFLDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDveiASKVMETDEK 218
Cdd:COG5000    81 Q-------REELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLP---ELDLAELLRE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 219 VFRHNVSLTYEqwlVYPDGRKaCFELRKVPFYDRvgkrhGLMGFGRDITERKRyqeALENASREKttFISTISHELRTPL 298
Cdd:COG5000   151 ALERGWQEEIE---LTRDGRR-TLLVRASPLRDD-----GYVIVFDDITELLR---AERLAAWGE--LARRIAHEIKNPL 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 299 NGIVGLSRILldtnltseQSSYLKTIHVSAVTLGNIFNDVI-EMDKIER---------RKVQLDNQPVALPEFVNDLENL 368
Cdd:COG5000   217 TPIQLSAERL--------RRKLADKLEEDREDLERALDTIIrQVDRLKRivdefldfaRLPEPQLEPVDLNELLREVLAL 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 369 SGLLVQPKGLKFVMDVAPTLPkTVLTDGTRLRQVLWNLIGNAVKFT-QQGEVKVSIWQEpENKIFFRVKDSGIGIPQDEL 447
Cdd:COG5000   289 YEPALKEKDIRLELDLDPDLP-EVLADRDQLEQVLINLLKNAIEAIeEGGEIEVSTRRE-DGRVRIEVSDNGPGIPEEVL 366
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2027583119 448 DKIFAMYYqvTDsaggKPaTGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSItaPVVEEVA 512
Cdd:COG5000   367 ERIFEPFF--TT----KP-KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRL--PLAEEAE 422
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
265-639 9.48e-40

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 158.21  E-value: 9.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 265 DITERKRYQEAL-------ENASREKTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQSSYLKTIHVSAVTLGNIFND 337
Cdd:PRK10841  422 DVSARVKMEESLqemaqaaEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISD 501
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 338 VIEMDKIERRKVQLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPKTVLTDGTRLRQVLWNLIGNAVKFTQQG 417
Cdd:PRK10841  502 ILDFSKIESEQLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTG 581
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 418 EVKVSIwQEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVtdSAGG-KPATGTGIGLSVSRRLAQNMGGDIQVESEIGQG 496
Cdd:PRK10841  582 CIVLHV-RVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQV--GTGVqRNFQGTGLGLAICEKLINMMDGDISVDSEPGMG 658
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 497 STFTLSI--------TAPVVE-----------------------------EVAEHQ----DSDD----DYP--------- 522
Cdd:PRK10841  659 SQFTIRIplygaqypQKKGVEglqgkrcwlavrnasleqfletllqrsgiQVQRYEgqepTPEDvlitDDPvqkkwqgra 738
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 523 -----------------------------LPAL-------------------------------HILLVEDIELNVVVAC 542
Cdd:PRK10841  739 vitfcrrhigipleiapgewvhstatpheLPALlariyrielesddsanalpstdkavsdnddmMILVVDDHPINRRLLA 818
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 543 SVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEdlpPLIALTANVLKDKKEY-FDAG 621
Cdd:PRK10841  819 DQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTL---PVIGVTANALAEEKQRcLEAG 895
                         490
                  ....*....|....*...
gi 2027583119 622 MDGVLSKPLSVPALTQVI 639
Cdd:PRK10841  896 MDSCLSKPVTLDVLKQTL 913
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
150-500 7.25e-39

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: 147.35  E-value: 7.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 150 LEQQSVLLRSFLDASPDLVYYRNENNEFSGCNRAMELLTG-----KSEKHLVGLT-PLDIYDV---EIASKVMEtdekvf 220
Cdd:TIGR02966   1 LSALLSRFRAAAQALPDAVVVLDEEGQIEWCNPAAERLLGlrwpdDLGQRITNLIrHPEFVEYlaaGRFSEPLE------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 221 rhnvsltyeqwLVYPDGRKACFELRKVPFydrvGKRHGLMGFgRDITERKRyqeaLENASREkttFISTISHELRTPLNG 300
Cdd:TIGR02966  75 -----------LPSPINSERVLEIRIAPY----GEEQKLLVA-RDVTRLRR----LEQMRRD---FVANVSHELRTPLTV 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 301 IVGLSRILLDTNLT--SEQSSYLKTIHVSAVTLGNIFNDVIEMDKIERRKVQLDNQPVALPEFVNDLENLSGLLVQPKGL 378
Cdd:TIGR02966 132 LRGYLETLADGPDEdpEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEALSQGKNH 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 379 KFVMDVAPTLPktVLTDGTRLRQVLWNLIGNAVKFTQ-QGEVKVSiWQEPENKIFFRVKDSGIGIPQDELDKIFAMYYQV 457
Cdd:TIGR02966 212 QITFEIDGGVD--VLGDEDELRSAFSNLVSNAIKYTPeGGTITVR-WRRDGGGAEFSVTDTGIGIAPEHLPRLTERFYRV 288
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2027583119 458 tDSAGGKPATGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFT 500
Cdd:TIGR02966 289 -DKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFS 330
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
528-639 1.66e-37

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: 135.67  E-value: 1.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLPPLIALT 607
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRRTPIIALT 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2027583119 608 ANVLK-DKKEYFDAGMDGVLSKPLSVPALTQVI 639
Cdd:cd17546    81 ANALEeDREKCLEAGMDDYLSKPVKLDQLKEVL 113
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
264-503 1.35e-36

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 141.47  E-value: 1.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 264 RDITERKRYQEALENASREKT--TFISTISHELRTPLNGIVG---LSRILLDTNLTSEQ-SSYLKTIHVSAVTLGNIfnd 337
Cdd:COG4191   121 RAEEELRELQEQLVQSEKLAAlgELAAGIAHEINNPLAAILGnaeLLRRRLEDEPDPEElREALERILEGAERAAEI--- 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 338 viemdkIER-----RKVQLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPKtVLTDGTRLRQVLWNLIGN--- 409
Cdd:COG4191   198 ------VRSlrafsRRDEEEREPVDLNELIDEALELLRPRLKARGIEVELDLPPDLPP-VLGDPGQLEQVLLNLLINaid 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 410 AVKFTQQGEVKVSIWQEpENKIFFRVKDSGIGIPQDELDKIFAMYYqvTDSAGGKpatGTGIGLSVSRRLAQNMGGDIQV 489
Cdd:COG4191   271 AMEEGEGGRITISTRRE-GDYVVISVRDNGPGIPPEVLERIFEPFF--TTKPVGK---GTGLGLSISYGIVEKHGGRIEV 344
                         250
                  ....*....|....
gi 2027583119 490 ESEIGQGSTFTLSI 503
Cdd:COG4191   345 ESEPGGGTTFTITL 358
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
394-503 1.62e-33

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 124.30  E-value: 1.62e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  394 TDGTRLRQVLWNLIGNAVKFT-QQGEVKVSIWQEPENkIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGGKPatGTGIG 472
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDH-VEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIG--GTGLG 77
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2027583119  473 LSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:smart00387  78 LSIVKKLVELHGGEISVESEPGGGTTFTITL 108
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
522-648 1.37e-32

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: 122.27  E-value: 1.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 522 PLPALHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLp 601
Cdd:COG0784     2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDI- 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2027583119 602 PLIALTANVLK-DKKEYFDAGMDGVLSKPLSVPALTQVIEQFWGEHTS 648
Cdd:COG0784    81 PIIALTAYADEeDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
264-501 2.02e-32

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 133.55  E-value: 2.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 264 RDITERKRYQEALENASREKT--TFISTISHELRTPLNGIVGLSRILLDTNLTSEQSSYLKTIHVSAVTLGNIFNDVIEM 341
Cdd:PRK11360  369 SDLTERKRLQRRVARQERLAAlgELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEF 448
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 342 DKieRRKVQldNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPkTVLTDGTRLRQVLWNLIGNAVK-FTQQGEVK 420
Cdd:PRK11360  449 SR--PRESQ--WQPVSLNALVEEVLQLFQTAGVQARVDFETELDNELP-PIWADPELLKQVLLNILINAVQaISARGKIR 523
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 421 VSIWQEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVTdsaggkpATGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFT 500
Cdd:PRK11360  524 IRTWQYSDGQVAVSIEDNGCGIDPELLKKIFDPFFTTK-------AKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFT 596

                  .
gi 2027583119 501 L 501
Cdd:PRK11360  597 L 597
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
143-508 2.66e-32

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


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 131.78  E-value: 2.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 143 REQTQVELEQQSVLLRSFLDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFRH 222
Cdd:COG5805   145 KKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIESITEV 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 223 NVSLTYEQWLVYPDGRKACFELRKVPFYDRVGKRHGLMGFGRDITERKRYQEALenASREKTTFI----STISHELRTPL 298
Cdd:COG5805   225 WQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEELM--ARSEKLSIAgqlaAGIAHEIRNPL 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 299 NGIVGLSRILLDTNLTSEQssylktihvsavtlgniFNDVI--EMDKIER---------RKVQLDNQPVALPEFVNDLEN 367
Cdd:COG5805   303 TSIKGFLQLLQPGIEDKEE-----------------YFDIMlsELDRIESiiseflalaKPQAVNKEKENINELIQDVVT 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 368 LSGLLVQPKGLKFVMDVAPTLPKtVLTDGTRLRQVLWNLIGNAVK-FTQQGEVKVSIWQEpENKIFFRVKDSGIGIPQDE 446
Cdd:COG5805   366 LLETEAILHNIQIRLELLDEDPF-IYCDENQIKQVFINLIKNAIEaMPNGGTITIHTEEE-DNSVIIRVIDEGIGIPEER 443
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2027583119 447 LDKIFAMYYQVTDSaggkpatGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTlsITAPVV 508
Cdd:COG5805   444 LKKLGEPFFTTKEK-------GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFT--ITLPLS 496
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
394-503 1.19e-31

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: 119.01  E-value: 1.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 394 TDGTRLRQVLWNLIGNAVKFT-QQGEVKVSIwqEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGGkpatGTGIG 472
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAaKAGEITVTL--SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGG----GTGLG 74
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2027583119 473 LSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:pfam02518  75 LSIVRKLVELLGGTITVESEPGGGTTVTLTL 105
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
399-503 3.85e-31

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: 117.32  E-value: 3.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVKFT-QQGEVKVSIWQEPENkIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGGKpatGTGIGLSVSR 477
Cdd:cd00075     1 LEQVLSNLLDNALKYSpPGGTIEISLRQEGDG-VVLEVEDNGPGIPEEDLERIFERFYRGDKSREGG---GTGLGLAIVR 76
                          90       100
                  ....*....|....*....|....*.
gi 2027583119 478 RLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:cd00075    77 RIVEAHGGRITVESEPGGGTTFTVTL 102
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
265-503 9.74e-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: 119.09  E-value: 9.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 265 DITErkryQEALENASREkttFISTISHELRTPlngivglsrilldtnLTSEQsSYLKTIHVSAV---TLGNIF------ 335
Cdd:NF033092  361 DVTE----QEKIEQERRE---FVANVSHELRTP---------------LTTMR-SYLEALADGAWkdpELAPRFlgvtqn 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 336 ---------NDVIEMDKIERRKVQLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDvaptLPKTVLT---DGTRLRQVL 403
Cdd:NF033092  418 etermirlvNDLLQLSRMDSKDYKLNKEWVNFNEFFNYIIDRFEMILKNKNITFKRE----FPKRDLWveiDTDKITQVL 493
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 404 WNLIGNAVKFTQQ-GEVKVSIwQEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVtDSAGGKPATGTGIGLSVSRRLAQN 482
Cdd:NF033092  494 DNIISNAIKYSPEgGTITFRL-LETHNRIIISISDQGLGIPKKDLDKIFDRFYRV-DKARSRKMGGTGLGLAIAKEVVEA 571
                         250       260
                  ....*....|....*....|.
gi 2027583119 483 MGGDIQVESEIGQGSTFTLSI 503
Cdd:NF033092  572 HGGRIWAESEEGKGTTIYFTL 592
PRK09303 PRK09303
histidine kinase;
287-507 7.75e-26

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 110.43  E-value: 7.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 287 ISTISHELRTPLNGIVglsrILLDTnltsEQSSYLKTIHVSAVTLGNIFNDVI--EMDKIER-------------RKVQL 351
Cdd:PRK09303  155 LAMLAHDLRTPLTAAS----LALET----LELGQIDEDTELKPALIEQLQDQArrQLEEIERlitdllevgrtrwEALRF 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 352 DNQPVALP----EFVNDLENlsglLVQPKGLKFVMDVAPTLPkTVLTDGTRLRQVLWNLIGNAVKFTQ-QGEVKVSIWQE 426
Cdd:PRK09303  227 NPQKLDLGslcqEVILELEK----RWLAKSLEIQTDIPSDLP-SVYADQERIRQVLLNLLDNAIKYTPeGGTITLSMLHR 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 427 PENKIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGgkpATGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLsiTAP 506
Cdd:PRK09303  302 TTQKVQVSICDTGPGIPEEEQERIFEDRVRLPRDEG---TEGYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHF--TLP 376

                  .
gi 2027583119 507 V 507
Cdd:PRK09303  377 V 377
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
525-640 1.35e-25

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: 104.22  E-value: 1.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 525 ALHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLpPLI 604
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADI-PII 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2027583119 605 ALTANVLK-DKKEYFDAGMDGVLSKPLSVPALTQVIE 640
Cdd:COG3706    80 FLTALDDEeDRARALEAGADDYLTKPFDPEELLARVD 116
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
528-641 7.76e-25

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: 99.92  E-value: 7.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLpPLIALT 607
Cdd:cd17548     2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDI-PVIALT 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2027583119 608 ANVLK-DKKEYFDAGMDGVLSKPLSVPALTQVIEQ 641
Cdd:cd17548    81 AYAMKgDREKILEAGCDGYISKPIDTREFLETVAK 115
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
1-777 4.83e-24

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


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 108.21  E-value: 4.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119   1 MKVLRGLAQYYVDLMMKLGLVRFSLLLASALVVLAMIMQMAVTIFLRGHVDSLDMVGSIFFGLIITPLAVYFLSVVVEQL 80
Cdd:COG2198   104 LLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLLLLALLLALLLLVLLVLLLLLLL 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  81 EESRQRLSRMVDKLEVMRKRDAELNIQLHGNIEQLNLEIQEREKAERAHLELLEQLKQEMKYREQTQVELEQQSVLLRSF 160
Cdd:COG2198   184 LLLLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAELAALLLLLLLLLLLLILLLLLLL 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 161 LDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFRHNVSLTYEQWLVYPDGRKA 240
Cdd:COG2198   264 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 241 CFELRKVPFYDRVGKRHGLMGFGRDITERKRYQEALENASREKTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQSSY 320
Cdd:COG2198   344 LLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSLLLLLLLLLLLLLL 423
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 321 LKTIHVSAVTLGNIFNDVIEMDKIERRKVQLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPKTVLTDGTRLR 400
Cdd:COG2198   424 LLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 503
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 401 QVLWNLIGNAVKFTQQGEVKVSIWQEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGGKPATGTGIGLSVSRRLA 480
Cdd:COG2198   504 LLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALLLGLGLLLGLLLGGLLLLLLLLL 583
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 481 QNMGGDIQVESEIGQGSTFTLSITAPVVEEVAEHQDSDDDYPLPALHILLVEDIELNVVVACSVLENLGNTVDVAMNGKD 560
Cdd:COG2198   584 LLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAVLLAAAAAAA 663
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 561 ALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLPPLIALTANVLKDKKEYFDAGMDGVLSKPLSVPALTQVIE 640
Cdd:COG2198   664 ALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLAALLLLLLLLLLLLLLLLLL 743
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 641 QFWGEHTSQNEEVEncdvtsqVDESILDCDMLEQYIElvGPKLIYDGLDVFEKMLPGYLAILDSNMVAKDQKGIVEEAHK 720
Cdd:COG2198   744 LLAAAAAAAASPAA-------PALPVLDLEALRRLGG--DPELLRELLELFLEELPELLAELRQALAAGDLEALARLAHK 814
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2027583119 721 IKGAAGSVGLKNLQKIAQQIQSPDLPAWWDNVQEWVDELKQDWKADIETLRNWVDER 777
Cdd:COG2198   815 LKGSAGNLGAPRLAELAAELEQAARAGDLEEAEELLAELEAELERVLAALEALLAEE 871
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
524-652 8.83e-24

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: 100.62  E-value: 8.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 524 PALHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLpPL 603
Cdd:COG3437     5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDI-PV 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2027583119 604 IALTANV-LKDKKEYFDAGMDGVLSKPLSVPALTQVIEQFWGEHTSQNEE 652
Cdd:COG3437    84 IFLTALAdPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQREL 133
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
526-640 1.02e-23

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


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 99.65  E-value: 1.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 526 LHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlPPLIA 605
Cdd:COG0745     2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSD---IPIIM 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2027583119 606 LTA-NVLKDKKEYFDAGMDGVLSKPLSVPALTQVIE 640
Cdd:COG0745    79 LTArDDEEDRVRGLEAGADDYLTKPFDPEELLARIR 114
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
528-640 1.42e-23

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: 96.07  E-value: 1.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlPPLIALT 607
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPT---TPVIILT 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2027583119 608 ANV-LKDKKEYFDAGMDGVLSKPLSVPALTQVIE 640
Cdd:pfam00072  78 AHGdEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
269-501 2.18e-22

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 101.02  E-value: 2.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 269 RKRYQEA---LENASREKT------TFISTISHELRTPLNGIVGLSRILLDTNLTSEQSSYLKTIHVSAVT-LGNIFNDV 338
Cdd:PRK10364  214 YRRYLRSrqlLQDEMKRKEklvalgHLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADrLNRVVSEL 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 339 IEMdkieRRKVQLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPkTVLTDGTRLRQVLWNLIGNAVK-FTQQG 417
Cdd:PRK10364  294 LEL----VKPTHLALQAVDLNDLINHSLQLVSQDANSREIQLRFTANDTLP-EIQADPDRLTQVLLNLYLNAIQaIGQHG 368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 418 EVKVSIwQEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVTdsaggkpATGTGIGLSVSRRLAQNMGGDIQVESEIGQGS 497
Cdd:PRK10364  369 VISVTA-SESGAGVKISVTDSGKGIAADQLEAIFTPYFTTK-------AEGTGLGLAVVHNIVEQHGGTIQVASQEGKGA 440

                  ....
gi 2027583119 498 TFTL 501
Cdd:PRK10364  441 TFTL 444
HKR_ArcB_TM pfam18415
Histidine kinase receptor ArcB trans-membrane domain; Histidine kinase receptors (HKRs) are ...
15-89 2.63e-22

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: 91.06  E-value: 2.63e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2027583119  15 MMKLGLVRFSLLLASALVVLAMIMQMAVTIFLRGHVDSLDMVGSIFFGLIITPLAVYFLSVVVEQLEESRQRLSR 89
Cdd:pfam18415   1 VIRLGTVRFSLLLAILLILFALLIQILLSLLLTGEVHWEDLLRSIFFGLLSAPWVLYFFSVVVEQLERSRQRLSK 75
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
276-503 8.03e-22

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 99.71  E-value: 8.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 276 LENASREKTTFISTISHELRTPLNGI------VGLSRILLDTnlTSEQSSYLktIHVSAVTLGNIFNDVIEMDKIERRKV 349
Cdd:NF040691  264 LEELSRLQQRFVSDVSHELRTPLTTIrmaadvIHDSRDDFDP--ATARSAEL--LHTELDRFESLLSDLLEISRFDAGAA 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 350 QLDNQPVALPEFVND-LENLSGLLVQpKGLKFVMDvAPTLPKTVLTDGTRLRQVLWNLIGNAVKFTQQGEVKVSIWQEpE 428
Cdd:NF040691  340 ELDVEPVDLRPLVRRvVDALRQLAER-AGVELRVD-APGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVAQD-D 416
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2027583119 429 NKIFFRVKDSGIGIPQDELDKIFAMYYQvTDSAGGKPATGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:NF040691  417 TAVAVTVRDHGVGLKPGEVALVFDRFWR-ADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTL 490
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-503 1.00e-21

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: 90.46  E-value: 1.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVKFTQQGEVK-VSIWQEPE-NKIFFRVKDSGIGIPQDELDKIFAMYYQV-TDSAGGkpatGTGIGLSV 475
Cdd:cd16921     1 LGQVLTNLLGNAIKFRRPRRPPrIEVGAEDVgEEWTFYVRDNGIGIDPEYAEKVFGIFQRLhSREEYE----GTGVGLAI 76
                          90       100
                  ....*....|....*....|....*...
gi 2027583119 476 SRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:cd16921    77 VRKIIERHGGRIWLESEPGEGTTFYFTL 104
PRK13557 PRK13557
histidine kinase; Provisional
347-597 5.04e-20

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 94.35  E-value: 5.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 347 RKVQLDNQPVALPEFVNDLENLSGLLVQPkGLKFVMDVAPTLPKTVLtDGTRLRQVLWNLIGNAVKFTQQGEvKVSIWQE 426
Cdd:PRK13557  228 RKQRLEGRVLNLNGLVSGMGELAERTLGD-AVTIETDLAPDLWNCRI-DPTQAEVALLNVLINARDAMPEGG-RVTIRTR 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 427 ------PENKIF----------FRVKDSGIGIPQDELDKIFAMYYQVTDSagGKpatGTGIGLSVSRRLAQNMGGDIQVE 490
Cdd:PRK13557  305 nveiedEDLAMYhglppgryvsIAVTDTGSGMPPEILARVMDPFFTTKEE--GK---GTGLGLSMVYGFAKQSGGAVRIY 379
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 491 SEIGQGSTFTLSItaPVVEEVAEHQDSdddYPLPAL------HILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAM 564
Cdd:PRK13557  380 SEVGEGTTVRLYF--PASDQAENPEQE---PKARAIdrggteTILIVDDRPDVAELARMILEDFGYRTLVASNGREALEI 454
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2027583119 565 FAPG-EYDLVLLDIQLP-DMTGLDISRQLKQQYDK 597
Cdd:PRK13557  455 LDSHpEVDLLFTDLIMPgGMNGVMLAREARRRQPK 489
PAS COG2202
PAS domain [Signal transduction mechanisms];
145-283 1.09e-19

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 89.31  E-value: 1.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 145 QTQVELEQQSVLLRSFLDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFRHNV 224
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2027583119 225 SLTYEQWLVYPDGRKACFELRKVPFYDRVGKRHGLMGFGRDITERKRYQEALEnASREK 283
Cdd:COG2202    81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALR-ESEER 138
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-503 2.42e-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: 2.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVK-FTQQGEVKVSIWQEpENKIFFRVKDSGIGIPQDELDKIFAMYYQVtdsaggKP-ATGTGIGLSVS 476
Cdd:cd16943     4 LNQVLLNLLVNAAQaMEGRGRITIRTWAH-VDQVLIEVEDTGSGIDPEILGRIFDPFFTT------KPvGEGTGLGLSLS 76
                          90       100
                  ....*....|....*....|....*..
gi 2027583119 477 RRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:cd16943    77 YRIIQKHGGTIRVASVPGGGTRFTIIL 103
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
254-503 5.14e-19

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 89.91  E-value: 5.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 254 GKRHGLMGFGRDITERKRYQEALENAsREKTTFISTISHELRTPLNGIVGLsrilLDTNLTSEQSSYLKTIhvsavtlgn 333
Cdd:COG3290   161 GRVVGAVATFRDRTELERLEEELEGV-KELAEALRAQRHDFRNHLHTISGL----LQLGEYDEALEYIDEI--------- 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 334 ifndVIEMDKIERRKVQLDNQPValpefvndlenLSGLL------VQPKGLKFVMDVAPTLPKTVLTDGTrLRQVLWNLI 407
Cdd:COG3290   227 ----SEELQELIDSLLSRIGNPV-----------LAALLlgkaarARERGIDLTIDIDSDLPDLPLSDTD-LVTILGNLL 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 408 GNAV-----KFTQQGEVKVSIWQEpENKIFFRVKDSGIGIPQDELDKIFAMYYQvTdsaggKPATGTGIGLSVSRRLAQN 482
Cdd:COG3290   291 DNAIeavekLPEEERRVELSIRDD-GDELVIEVEDSGPGIPEELLEKIFERGFS-T-----KLGEGRGLGLALVKQIVEK 363
                         250       260
                  ....*....|....*....|.
gi 2027583119 483 MGGDIQVESEIGQGSTFTLSI 503
Cdd:COG3290   364 YGGTIEVESEEGEGTVFTVRL 384
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
264-640 5.21e-19

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 92.05  E-value: 5.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 264 RDITERKRYQEALENASREKT--TFISTISHELRTPLNGIVGLSRILLDT-NLTSEQSSYLKTIhVSAvtlGNIFNDVIE 340
Cdd:PRK13837  429 RLETERDALERRLEHARRLEAvgTLASGIAHNFNNILGAILGYAEMALNKlARHSRAARYIDEI-ISA---GARARLIID 504
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 341 MDKIERRKVQLDNQPVALPEFVNdlENLSGLLVQ-PKGLKFVMDVAPTlPKTVLTDGTRLRQVLWNLIGNAVK-FTQQGE 418
Cdd:PRK13837  505 QILAFGRKGERNTKPFDLSELVT--EIAPLLRVSlPPGVELDFDQDQE-PAVVEGNPAELQQVLMNLCSNAAQaMDGAGR 581
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 419 VKVSIWQE--------------PENKIFFRVKDSGIGIPQDELDKIFAMYYqvTDSAGGkpatgTGIGLSVSRRLAQNMG 484
Cdd:PRK13837  582 VDISLSRAklrapkvlshgvlpPGRYVLLRVSDTGAGIDEAVLPHIFEPFF--TTRAGG-----TGLGLATVHGIVSAHA 654
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 485 GDIQVESEIGQGSTFT--LSITAPVveEVAEhQDSDDDYPLPALH---ILLVEDIELNVVVACSVLENLGNTvDVAMNG- 558
Cdd:PRK13837  655 GYIDVQSTVGRGTRFDvyLPPSSKV--PVAP-QAFFGPGPLPRGRgetVLLVEPDDATLERYEEKLAALGYE-PVGFSTl 730
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 559 KDALAMFA--PGEYDLVLLDIQLPDMTGL--DISRQLKqqydkeDLPPLIA---LTANVLKDKKeyfdAGMDGVLSKPLS 631
Cdd:PRK13837  731 AAAIAWISkgPERFDLVLVDDRLLDEEQAaaALHAAAP------TLPIILGgnsKTMALSPDLL----ASVAEILAKPIS 800

                  ....*....
gi 2027583119 632 VPALTQVIE 640
Cdd:PRK13837  801 SRTLAYALR 809
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
243-508 5.98e-19

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 90.07  E-value: 5.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 243 ELRKVPFYDRvgkrHGLMgFGRDITERKRyqeaLENASREkttFISTISHELRTPLNGIVGLSRILLDTNLtsEQSSYLK 322
Cdd:PRK11006  176 EIRVMPYTEG----QLLM-VARDVTQMHQ----LEGARRN---FFANVSHELRTPLTVLQGYLEMMQDQPL--EGALREK 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 323 TIHV---SAVTLGNIFNDVIEMDKIERRKVQLDNQPVALPEFVNDLENLSGLLVQPKGlKFVMDVAPTLpkTVLTDGTRL 399
Cdd:PRK11006  242 ALHTmreQTQRMEGLVKQLLTLSKIEAAPTIDLNEKVDVPMMLRVLEREAQTLSQGKH-TITFEVDNSL--KVFGNEDQL 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 400 RQVLWNLIGNAVKFTQQG-EVKVSiWQEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVtDSAGGKPATGTGIGLSVSRR 478
Cdd:PRK11006  319 RSAISNLVYNAVNHTPEGtHITVR-WQRVPQGAEFSVEDNGPGIAPEHIPRLTERFYRV-DKARSRQTGGSGLGLAIVKH 396
                         250       260       270
                  ....*....|....*....|....*....|
gi 2027583119 479 LAQNMGGDIQVESEIGQGSTFTLSITAPVV 508
Cdd:PRK11006  397 ALSHHDSRLEIESEVGKGTRFSFVLPERLI 426
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
289-503 9.49e-19

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 89.90  E-value: 9.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 289 TISHELRTPLNGIVGLSRiLLDTNLTSEQ-SSYLKTIHVSAVTLGNIFNDVIEMDKIERRKVQLDNQPVALPEFVNDLEN 367
Cdd:PRK11100  262 TLTHELKSPLAAIRGAAE-LLQEDPPPEDrARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVE 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 368 LSGLLVQPKGLKFVMDVAPTlpkTVLTDGTRLRQVLWNLIGNAVKFT-QQGEVKVSIWQEpENKIFFRVKDSGIGIPQDE 446
Cdd:PRK11100  341 AREAQAAAKGITLRLRPDDA---RVLGDPFLLRQALGNLLDNAIDFSpEGGTITLSAEVD-GEQVALSVEDQGPGIPDYA 416
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2027583119 447 LDKIFAMYYQVTDSAGGKpaTGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:PRK11100  417 LPRIFERFYSLPRPANGR--KSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTL 471
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
290-503 1.08e-18

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: 89.16  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 290 ISHELRTPLNGIVGLSRILLDTNLTSE-QSSYLKTIhvsavtlgnifndVIEMDKIER--------RKVQLDN-QPVALP 359
Cdd:COG5806   208 IAHEVRNPLTVVRGFIQLLQEPELSDEkRKQYIRIA-------------LEELDRAEAiitdyltfAKPQPEKlEKIDVS 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 360 EFVNDLENLSGLLVQPKGLKFVMDVAPTLpkTVLTDGTRLRQVLWNLIGNAVKFTQQ-GEVKVSIwQEPENKIFFRVKDS 438
Cdd:COG5806   275 EELEHVIDVLSPYANMNNVEIQTELEPGL--YIEGDRQKLQQCLINIIKNGIEAMPNgGTLTIDV-SIDKNKVIISIKDT 351
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2027583119 439 GIGIPQDELDKIFAMYYQVTDsaggkpaTGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:COG5806   352 GVGMTKEQLERLGEPYFSTKE-------KGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITL 409
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
529-629 7.37e-18

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: 79.19  E-value: 7.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 529 LLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlPPLIALTA 608
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPD---IPVIVLTA 77
                          90       100
                  ....*....|....*....|..
gi 2027583119 609 NV-LKDKKEYFDAGMDGVLSKP 629
Cdd:cd00156    78 KAdEEDAVRALELGADDYLVKP 99
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
528-635 1.10e-17

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: 79.45  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIEL---NVVVAcsvLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEdlpPLI 604
Cdd:cd17624     1 ILLVEDDALlgdGLKTG---LRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSL---PVL 74
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2027583119 605 ALTAN-VLKDKKEYFDAGMDGVLSKPLSVPAL 635
Cdd:cd17624    75 ILTARdGVDDRVAGLDAGADDYLVKPFALEEL 106
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
526-639 3.24e-17

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: 78.21  E-value: 3.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 526 LHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGE--YDLVLLDIQLPDMTGLDISRQLKQQYDKEDLPPL 603
Cdd:cd19933     1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEhsFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPLI 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2027583119 604 IALTANVLKDKKEY-FDAGMDGVLSKPLSVPALTQVI 639
Cdd:cd19933    81 VALTANTDDSTREKcLSLGMNGVITKPVSLHALGDEL 117
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
276-502 3.40e-17

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: 85.13  E-value: 3.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 276 LENASREKTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQssYLKTIHVSAVT---LGNIFNDVIEMDKIERRKVQLD 352
Cdd:TIGR01386 234 LEDAFQRLSQFSADLAHELRTPLTNLLGQTQVALSQPRTGEE--YREVLESNLEElerLSRMVSDMLFLARADNGQLALE 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 353 NQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLPktvlTDGTRLRQVLWNLIGNAVKFTQQG-EVKVSIwQEPENKI 431
Cdd:TIGR01386 312 RVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEGLVR----GDPQMFRRAISNLLSNALRHTPDGgTITVRI-ERRSDEV 386
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2027583119 432 FFRVKDSGIGIPQDELDKIFAMYYQVtDSAGGKPATGTGIGLSVSRRLAQNMGGDIQVESEIGQgSTFTLS 502
Cdd:TIGR01386 387 RVSVSNPGPGIPPEHLSRLFDRFYRV-DPARSNSGEGTGLGLAIVRSIMEAHGGRASAESPDGK-TRFILR 455
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
526-642 4.35e-17

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 78.47  E-value: 4.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 526 LHILLVEDIELNVVVACSVLENLGN--TVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlPPL 603
Cdd:COG4565     4 IRVLIVEDDPMVAELLRRYLERLPGfeVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPD---VDV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2027583119 604 IALTANV-LKDKKEYFDAGMDGVLSKPLSVPALTQVIEQF 642
Cdd:COG4565    81 IVITAARdPETVREALRAGVVDYLIKPFTFERLREALERY 120
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
528-639 8.09e-17

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: 76.73  E-value: 8.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLpPLIALT 607
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANT-PAIALT 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2027583119 608 A-NVLKDKKEYFDAGMDGVLSKPLSVPALTQVI 639
Cdd:cd17580    80 GyGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
529-629 8.12e-17

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


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 76.29  E-value: 8.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 529 LLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlPPLIALTA 608
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSD---IPIIMLTA 77
                          90       100
                  ....*....|....*....|..
gi 2027583119 609 -NVLKDKKEYFDAGMDGVLSKP 629
Cdd:cd17574    78 kDEEEDKVLGLELGADDYITKP 99
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
527-657 1.44e-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: 82.70  E-value: 1.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlPPLIAL 606
Cdd:COG2204     4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPD---LPVILL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2027583119 607 TANV-LKDKKEYFDAGMDGVLSKPLSVPALTQVIEQFWGEHTSQNEEVENCD 657
Cdd:COG2204    81 TGYGdVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSG 132
envZ PRK09467
osmolarity sensor protein; Provisional
290-489 3.43e-16

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 81.88  E-value: 3.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 290 ISHELRTPLngivglSRILLDTNLTSEQSSYLKTihvsavtlgNIFNDVIEMDKIERR---KVQLDNQPVALPEFVNDLE 366
Cdd:PRK09467  236 VSHDLRTPL------TRIRLATEMMSEEDGYLAE---------SINKDIEECNAIIEQfidYLRTGQEMPMEMADLNALL 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 367 NLSGLLVQPKGLKFVMDVAPTlPKTVLTDGTRLRQVLWNLIGNAVKFTQqGEVKVSIWQEpENKIFFRVKDSGIGIPQDE 446
Cdd:PRK09467  301 GEVIAAESGYEREIETALQPG-PIEVPMNPIAIKRALANLVVNAARYGN-GWIKVSSGTE-GKRAWFQVEDDGPGIPPEQ 377
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2027583119 447 LDKIFAMYYQvTDSAGGkpATGTGIGLSVSRRLAQNMGGDIQV 489
Cdd:PRK09467  378 LKHLFQPFTR-GDSARG--SSGTGLGLAIVKRIVDQHNGKVEL 417
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
529-640 4.21e-16

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: 74.95  E-value: 4.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 529 LLVED-IELNVVVaCSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQydKEDLPPLIaLT 607
Cdd:cd17625     1 LVVEDeKDLSEAI-TKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREE--GIETPVLL-LT 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2027583119 608 A-NVLKDKKEYFDAGMDGVLSKPLSVPALTQVIE 640
Cdd:cd17625    77 AlDAVEDRVKGLDLGADDYLPKPFSLAELLARIR 110
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
282-345 1.46e-15

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 71.47  E-value: 1.46e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2027583119 282 EKTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQSSYLKTIHVSAVTLGNIFNDVIEMDKIE 345
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIE 64
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-500 1.46e-15

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


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 73.01  E-value: 1.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVKFT-QQGEVKVSIWQEPENKiFFRVKDSGIGIPQDELDKIFAMYYQVtDSAGGKPATGTGIGLSVSR 477
Cdd:cd16952     1 LRSAFSNLVSNAVKYTpPSDTITVRWSQEESGA-RLSVEDTGPGIPPEHIPRLTERFYRV-DIERCRNTGGTGLGLAIVK 78
                          90       100
                  ....*....|....*....|...
gi 2027583119 478 RLAQNMGGDIQVESEIGQGSTFT 500
Cdd:cd16952    79 HVMSRHDARLLIASELGKGSRFT 101
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
156-266 1.82e-15

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: 72.84  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 156 LLRSFLDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFRH-NVSLTYEQWLVY 234
Cdd:pfam00989   2 DLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQgEESRGFEVSFRV 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2027583119 235 PDGRKACFELRKVPFYDRVGKRHGLMGFGRDI 266
Cdd:pfam00989  82 PDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
394-502 1.82e-15

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


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 72.70  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 394 TDGTRLRQVLWNLIGNAVKFTQQGEvKVSIW-QEPENKIFFRVKDSGIGIPQDELDKIFAMYYqvTDSAGGKPATGTGIG 472
Cdd:cd16948     1 TDAKWLSFIIGQIVSNALKYSKQGG-KIEIYsETNEQGVVLSIKDFGIGIPEEDLPRVFDKGF--TGENGRNFQESTGMG 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 2027583119 473 LSVSRRLAQNMGGDIQVESEIGQGSTFTLS 502
Cdd:cd16948    78 LYLVKKLCDKLGHKIDVESEVGEGTTFTIT 107
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
389-496 2.12e-15

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


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 72.82  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 389 PKTVLTDGTRLRQVLWNLIGNAVKFTQQGEVkVSIWQEPENKIFFRVKDSGIGIPQDELDKIFAMYYQvtdsAGGKPATG 468
Cdd:cd16940     4 DIQVQGDALLLFLLLRNLVDNAVRYSPQGSR-VEIKLSADDGAVIRVEDNGPGIDEEELEALFERFYR----SDGQNYGG 78
                          90       100
                  ....*....|....*....|....*...
gi 2027583119 469 TGIGLSVSRRLAQNMGGDIQVESEIGQG 496
Cdd:cd16940    79 SGLGLSIVKRIVELHGGQIFLGNAQGGG 106
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
527-629 2.66e-15

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: 72.15  E-value: 2.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLpPLIAL 606
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHI-PVIMI 79
                          90       100
                  ....*....|....*....|....
gi 2027583119 607 TA-NVLKDKKEYFDAGMDGVLSKP 629
Cdd:cd17538    80 TAlDDREDRIRGLEAGADDFLSKP 103
PRK10490 PRK10490
sensor protein KdpD; Provisional
267-513 2.84e-15

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 80.08  E-value: 2.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 267 TERkryqEALENAsrekttFISTISHELRTPLNGIVGLSRILLdTNLTSEQSSYlkTIHVSAV---TLGNI--FNDVIEM 341
Cdd:PRK10490  658 SER----EQLRNA------LLAALSHDLRTPLTVLFGQAEILT-LDLASEGSPH--ARQASEIrqqVLNTTrlVNNLLDM 724
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 342 DKIERRKVQLDNQPVALPEFVND-LENLS-GLLVQPkglkfvmdVAPTLPKTVL---TDGTRLRQVLWNLIGNAVKFT-Q 415
Cdd:PRK10490  725 ARIQSGGFNLRKEWLTLEEVVGSaLQMLEpGLSGHP--------INLSLPEPLTlihVDGPLFERVLINLLENAVKYAgA 796
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 416 QGEVKVSIWQEPENkIFFRVKDSGIGIPQDELDKIFAMYyqvtdSAGGKPAT--GTGIGLSVSRRLAQNMGGDIQVESEI 493
Cdd:PRK10490  797 QAEIGIDAHVEGER-LQLDVWDNGPGIPPGQEQLIFDKF-----ARGNKESAipGVGLGLAICRAIVEVHGGTIWAENRP 870
                         250       260
                  ....*....|....*....|...
gi 2027583119 494 GQGSTFTLSI---TAPVVEEVAE 513
Cdd:PRK10490  871 EGGACFRVTLpleTPPELEEFHE 893
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
395-494 3.75e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli 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: 72.11  E-value: 3.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 395 DGTRLRQVLWNLIGNAVKFTQQ-GEVKVSIWQEPEnKIFFRVKDSGIGIPQDELDKIFAMYYQVtDSAGGKPATGTGIGL 473
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTgGKLRIRAAQTPQ-EVRLDVEDSAPGVSDDQLARLFERFYRV-ESSRNRASGGSGLGL 78
                          90       100
                  ....*....|....*....|..
gi 2027583119 474 SVSRRLAQNMGGDIQVE-SEIG 494
Cdd:cd16946    79 AICHNIALAHGGTISAEhSPLG 100
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
282-345 4.36e-15

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 70.29  E-value: 4.36e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2027583119  282 EKTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQSSYLKTIHVSAVTLGNIFNDVIEMDKIE 345
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIE 64
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-503 6.62e-15

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: 71.78  E-value: 6.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVKFTQQGEVKVSIWQEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAgGKPATGTGIGLSVSRR 478
Cdd:cd16947    21 LQRILKNLISNAIKYGSDGKFLGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSR-NSAKQGNGLGLTITKR 99
                          90       100
                  ....*....|....*....|....*
gi 2027583119 479 LAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:cd16947   100 LAESMGGSIYVNSKPYEKTVFTVTL 124
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
528-629 9.98e-15

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 70.55  E-value: 9.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlPPLIALT 607
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQ---TPVLMLT 77
                          90       100
                  ....*....|....*....|...
gi 2027583119 608 A-NVLKDKKEYFDAGMDGVLSKP 629
Cdd:cd19935    78 ArDSVEDRVKGLDLGADDYLVKP 100
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
528-629 3.68e-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: 69.23  E-value: 3.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVED-IELNVVVACSvLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQydKEDLPPLIaL 606
Cdd:cd19934     1 LLLVEDdALLAAQLKEQ-LSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSE--GRATPVLI-L 76
                          90       100
                  ....*....|....*....|....
gi 2027583119 607 TANV-LKDKKEYFDAGMDGVLSKP 629
Cdd:cd19934    77 TARDsWQDKVEGLDAGADDYLTKP 100
PAS COG2202
PAS domain [Signal transduction mechanisms];
143-276 5.41e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 72.75  E-value: 5.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 143 REQTQVELEQQSVLLRSFLDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFRH 222
Cdd:COG2202   125 RKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEG 204
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2027583119 223 NVSlTYEQWLVYPDGRKACFELR-KVPFYDRVGKRHGLMGFGRDITERKRYQEAL 276
Cdd:COG2202   205 GRE-SYELELRLKDGDGRWVWVEaSAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
PRK10604 PRK10604
sensor protein RstB; Provisional
283-517 7.64e-14

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 74.25  E-value: 7.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 283 KTTFISTISHELRTPLngiVGLS-RILLDTNLTSEQSSYLKTihvsavTLGNIfNDVIE----MDKIERRKVQLDNQPVA 357
Cdd:PRK10604  212 KKQLIDGIAHELRTPL---VRLRyRLEMSDNLSAAESQALNR------DIGQL-EALIEelltYARLDRPQNELHLSEPD 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 358 LPEFVND-LENLSgLLVQPKGLKFVMdvaPTLPKTVLTDGTRLRQVLWNLIGNAVKFTQQgEVKVSIWQEpENKIFFRVK 436
Cdd:PRK10604  282 LPAWLSThLADIQ-AVTPEKTVRLDT---PHQGDYGALDMRLMERVLDNLLNNALRYAHS-RVRVSLLLD-GNQACLIVE 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 437 DSGIGIPQDELDKIFAMYYQVtDSAGGKPATGTGIGLSVSRRLAQNMGGDIQVE-SEIGqGSTFTLSItaPVVEEVAEHQ 515
Cdd:PRK10604  356 DDGPGIPPEERERVFEPFVRL-DPSRDRATGGCGLGLAIVHSIALAMGGSVNCDeSELG-GARFSFSW--PVWHNLPQFT 431

                  ..
gi 2027583119 516 DS 517
Cdd:PRK10604  432 SA 433
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
527-630 2.21e-13

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: 67.08  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVEDIELNVVVACSVLENLGNT-VDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLpPLIA 605
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAGYLeVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDV-PIVM 80
                          90       100
                  ....*....|....*....|....*.
gi 2027583119 606 LTANVLKD-KKEYFDAGMDGVLSKPL 630
Cdd:cd17551    81 ITADTDREvRLRALEAGATDFLTKPF 106
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-496 3.00e-13

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: 66.32  E-value: 3.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVKFTQqGEVKVSIWQEPeNKIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGGKpatGTGIGLSVSRR 478
Cdd:cd16950     1 LKRVLSNLVDNALRYGG-GWVEVSSDGEG-NRTRIQVLDNGPGIAPEEVDELFQPFYRGDNARGTS---GTGLGLAIVQR 75
                          90
                  ....*....|....*...
gi 2027583119 479 LAQNMGGDIQVESEIGQG 496
Cdd:cd16950    76 ISDAHGGSLTLANRAGGG 93
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-505 4.52e-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: 4.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVKFTQQgEVKVSIWQEpENKIFFRVKDSGIGIPQDELDKIFAMYYQVtDSAGGKPATGTGIGLSVSRR 478
Cdd:cd16949     1 LARALENVLRNALRYSPS-KILLDISQD-GDQWTITITDDGPGVPEDQLEQIFLPFYRV-DSARDRESGGTGLGLAIAER 77
                          90       100
                  ....*....|....*....|....*..
gi 2027583119 479 LAQNMGGDIQVESEIGQGSTFTLSITA 505
Cdd:cd16949    78 AIEQHGGKIKASNRKPGGLRVRIWLPA 104
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
395-503 4.77e-13

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: 65.98  E-value: 4.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 395 DGTRLRQVLWNLIGNAVKFTQQG-EVKVSIWQEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGGKPAtGTGIGL 473
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGgRIRCILEKFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHG-GTGLGL 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 2027583119 474 SVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:cd16925    80 SIVKEFVELHGGTVTVSDAPGGGALFQVEL 109
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
545-632 6.38e-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: 65.76  E-value: 6.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 545 LENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLpPLIALTAnvlkdKKEYFDA---- 620
Cdd:cd19937    17 LEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSI-PIIMLTA-----KGEEFDKvlgl 90
                          90
                  ....*....|....
gi 2027583119 621 --GMDGVLSKPLSV 632
Cdd:cd19937    91 elGADDYITKPFSP 104
PRK10643 PRK10643
two-component system response regulator PmrA;
528-635 1.97e-12

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 67.37  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQydKEDLPPLIaLT 607
Cdd:PRK10643    3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQK--KYTLPVLI-LT 79
                          90       100
                  ....*....|....*....|....*....
gi 2027583119 608 A-NVLKDKKEYFDAGMDGVLSKPLSVPAL 635
Cdd:PRK10643   80 ArDTLEDRVAGLDVGADDYLVKPFALEEL 108
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
527-643 3.21e-12

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: 64.36  E-value: 3.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVEDIELNVVVACSVLENLG--NTVDVAMNGKDALAM-FAPGEY------DLVLLDIQLPDMTGLDISRQLKQQydk 597
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDFlRGEGEYadaprpDLILLDLNMPRMDGFEVLREIKAD--- 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2027583119 598 EDLP--PLIALTA-NVLKDKKEYFDAGMDGVLSKPLSVPALTQVIEQ---FW 643
Cdd:cd17557    78 PDLRriPVVVLTTsDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSlgeYW 129
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
161-271 3.35e-12

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: 63.59  E-value: 3.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 161 LDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFRHNVSLTYEQWLVyPDGRKA 240
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELL-LNGEER 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2027583119 241 CFELRKVPFYDRVGKRHGLMGFGRDITERKR 271
Cdd:pfam08448  80 HYELRLTPLRDPDGEVIGVLVISRDITERRR 110
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
402-504 6.55e-12

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: 62.69  E-value: 6.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 402 VLWNLIGNAVKF---TQQGEVKVSIWQEPENKIF-FRVKDSGIGIPQDELDKIFAMYYQVtdsaggKPATGTGIGLSVSR 477
Cdd:cd16915     4 IVGNLIDNALDAlaaTGAPNKQVEVFLRDEGDDLvIEVRDTGPGIAPELRDKVFERGVST------KGQGERGIGLALVR 77
                          90       100
                  ....*....|....*....|....*..
gi 2027583119 478 RLAQNMGGDIQVESEIGQGSTFTLSIT 504
Cdd:cd16915    78 QSVERLGGSITVESEPGGGTTFSIRIP 104
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-503 6.63e-12

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: 62.41  E-value: 6.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVKFTQQGEVK---VSIWQEPENKIFFR--VKDSGIGIPQDELDKIFAMYYQVTdsaggkpATGTGIGL 473
Cdd:cd16920     1 IQQVLINLVRNGIEAMSEGGCErreLTIRTSPADDRAVTisVKDTGPGIAEEVAGQLFDPFYTTK-------SEGLGMGL 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 2027583119 474 SVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:cd16920    74 SICRSIIEAHGGRLSVESPAGGGATFQFTL 103
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
262-503 8.11e-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: 68.62  E-value: 8.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 262 FGRDITERKRYQEALENASrekttfiSTISHELRTPLnGIVGLSRILLDT-NLTSEQSSYLKTIHVSAVTLGNIFNDVIE 340
Cdd:TIGR03785 471 FAQMVARLRQYTHYLENMS-------SRLSHELRTPV-AVVRSSLENLELqALEQEKQKYLERAREGTERLSMILNNMSE 542
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 341 MDKIERRKVQLDNQPVALPEFVNDLenLSGLLVQPKGLKFVMDVaPTLPKTVLTDGTRLRQVLWNLIGNAVKFTQQG--- 417
Cdd:TIGR03785 543 ATRLEQAIQSAEVEDFDLSEVLSGC--MQGYQMTYPPQRFELNI-PETPLVMRGSPELIAQMLDKLVDNAREFSPEDgli 619
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 418 EVKVSiwqEPENKIFFRVKDSGIGIPQDELDKIFAMYYQVTDSaGGKPATGTGIGLSVSRRLAQNMGGDIQVESEI-GQG 496
Cdd:TIGR03785 620 EVGLS---QNKSHALLTVSNEGPPLPEDMGEQLFDSMVSVRDQ-GAQDQPHLGLGLYIVRLIADFHQGRIQAENRQqNDG 695

                  ....*..
gi 2027583119 497 STFTLSI 503
Cdd:TIGR03785 696 VVFRISL 702
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
527-631 9.96e-12

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: 62.65  E-value: 9.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLpPLIAL 606
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDI-PIIML 80
                          90       100
                  ....*....|....*....|....*.
gi 2027583119 607 TANVLK-DKKEYFDAGMDGVLSKPLS 631
Cdd:cd17618    81 TARGEEeDKVRGLEAGADDYITKPFS 106
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
528-629 1.18e-11

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: 61.76  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLpPLIALT 607
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHI-PVIFLT 79
                          90       100
                  ....*....|....*....|....*
gi 2027583119 608 A-NVLKDKKEYFDAGmdGV--LSKP 629
Cdd:cd19920    80 AlTDTEDKVKGFELG--AVdyITKP 102
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
680-771 1.45e-11

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: 61.11  E-value: 1.45e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  680 GPKLIYDGLDVFEKMLPGYLAILDSNMVAKDQKGIVEEAHKIKGAAGSVGLKNLQKIAQQIQSPDLPAWWDNVqEWVDEL 759
Cdd:smart00073   2 GLELFREELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEV-ELTPDL 80
                           90
                   ....*....|..
gi 2027583119  760 KQDWKADIETLR 771
Cdd:smart00073  81 LDLLLELVDVLK 92
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
528-609 1.55e-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: 62.04  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDielNVVVA---CSVLENLG-NTVDVAMNGKDALAMFAPGEYDLVLLDIQLP-DMTGLDISRQLKQQYDKedlpP 602
Cdd:cd17534     3 ILIVED---EAIIAldlKEILESLGyEVVGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKFDI----P 75

                  ....*..
gi 2027583119 603 LIALTAN 609
Cdd:cd17534    76 VIFLTAY 82
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
528-608 1.57e-11

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


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 61.83  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlPPLIALT 607
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLP---TSVIVIT 77

                  .
gi 2027583119 608 A 608
Cdd:cd17572    78 A 78
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
266-491 1.68e-11

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 67.79  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 266 ITERKRYQEALENASRE-KTTF--------ISTISHELRTPLNGIvglSRILLDTNLTSEQSSYLKTIHvsavTLGNIFN 336
Cdd:COG4192   407 IEERKRIEKNLRQTQDElIQAAkmavvgqtMTSLAHELNQPLNAM---SMYLFSAKKALEQENYAQLPT----SLDKIEG 479
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 337 DVIEMDKIER------RKVQLDNQPVALPEFVNDLENLsgLLVQPKGLKFVMDVAPTLPktVLTDGTRLRQVLWNLIGNA 410
Cdd:COG4192   480 LIERMDKIIKslrqfsRKSDTPLQPVDLRQVIEQAWEL--VESRAKPQQITLHIPDDLM--VQGDQVLLEQVLVNLLVNA 555
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 411 VK-FTQQGEVKVsIWQEPENKIFFRVKDSGIGIPqdELDKIFAMYYQVTDsaggkpaTGTGIGLSVSRRLAQNMGGDIQV 489
Cdd:COG4192   556 LDaVATQPQISV-DLLSNAENLRVAISDNGNGWP--LVDKLFTPFTTTKE-------VGLGLGLSICRSIMQQFGGDLYL 625

                  ..
gi 2027583119 490 ES 491
Cdd:COG4192   626 AS 627
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
402-503 2.22e-11

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 67.25  E-value: 2.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 402 VLWNLIGN---AVKFTQQGEVKVSIWQEpENKIFFRVKDSGIGIPQDELDKIFAMYYqvtdSAGGKpatGTGIGLSVSRR 478
Cdd:PRK11086  437 ILGNLIENaleAVGGEEGGEISVSLHYR-NGWLHCEVSDDGPGIAPDEIDAIFDKGY----STKGS---NRGVGLYLVKQ 508
                          90       100
                  ....*....|....*....|....*
gi 2027583119 479 LAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:PRK11086  509 SVENLGGSIAVESEPGVGTQFFVQI 533
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-503 2.41e-11

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: 61.05  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVKFTQQGEVKVSIWQEPE-NKIFFRVKDSGIGIPQDELDKIFAMYYqvTDS-AGGKPATGTGIGLSVS 476
Cdd:cd16953     1 LGQVLRNLIGNAISFSPPDTGRITVSAMPTgKMVTISVEDEGPGIPQEKLESIFDRFY--TERpANEAFGQHSGLGLSIS 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2027583119 477 RRLAQNMGGDIQVES----EIGQGSTFTLSI 503
Cdd:cd16953    79 RQIIEAHGGISVAENhnqpGQVIGARFTVQL 109
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
287-475 3.41e-11

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 66.11  E-value: 3.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 287 ISTISHELRTPLngivglSRILLDTNLTSE---QSSYLKTIHVSAVTLGNIFNDVIEMDKIERrKVQLDNQPVALPEFVN 363
Cdd:PRK09470  247 LSDISHELRTPL------TRLQLATALLRRrqgESKELERIETEAQRLDSMINDLLVLSRNQQ-KNHLERETFKANSLWS 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 364 DLENLSGLLVQPKGLKFVMDVAPTlPKTVLTDGTRLRQVLWNLIGNAVKFTQQgEVKVSIwQEPENKIFFRVKDSGIGIP 443
Cdd:PRK09470  320 EVLEDAKFEAEQMGKSLTVSAPPG-PWPINGNPNALASALENIVRNALRYSHT-KIEVAF-SVDKDGLTITVDDDGPGVP 396
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2027583119 444 QDELDKIFAMYYQVtDSAGGKPATGTGIGLSV 475
Cdd:PRK09470  397 EEEREQIFRPFYRV-DEARDRESGGTGLGLAI 427
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
688-761 3.59e-11

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: 59.67  E-value: 3.59e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2027583119 688 LDVFEKMLPGYLAILDSNMVAKDQKGIVEEAHKIKGAAGSVGLKNLQKIAQQIQS----PDLPAWWDNVQEWVDELKQ 761
Cdd:pfam01627   3 LELFLEEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDllreGELPLDPELLEALRDLLEA 80
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
526-654 4.04e-11

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 63.68  E-value: 4.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 526 LHILLVEDIELNVVVACSVLENLGNT--VDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlPPL 603
Cdd:COG3279     2 MKILIVDDEPLARERLERLLEKYPDLevVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPP---PPI 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2027583119 604 IALTANvlkdkKEY----FDAG-MDGVLsKPLSVPALTQVIEQFWGEHTSQNEEVE 654
Cdd:COG3279    79 IFTTAY-----DEYaleaFEVNaVDYLL-KPIDEERLAKALEKAKERLEAKAAAEA 128
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
274-503 5.17e-11

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 65.56  E-value: 5.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 274 EALENASREKTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQssyLKTIHVSAVT----LGNIFNDVIEMDKIERRKV 349
Cdd:PRK09835  253 ERIEDVFTRQSNFSADIAHEIRTPITNLITQTEIALSQSRSQKE---LEDVLYSNLEeltrMAKMVSDMLFLAQADNNQL 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 350 QLDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTLpktVLTDGTRLRQVLWNLIGNAVKFTQQGE-VKVSIwQEPE 428
Cdd:PRK09835  330 IPEKKMLDLADEVGKVFDFFEAWAEERGVELRFVGDPCQ---VAGDPLMLRRAISNLLSNALRYTPAGEaITVRC-QEVD 405
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2027583119 429 NKIFFRVKDSGIGIPQDELDKIFAMYYQVtDSAGGKPATGTGIGLSVSRRLAQNMGGDIQVESEIgQGSTFTLSI 503
Cdd:PRK09835  406 HQVQLVVENPGTPIAPEHLPRLFDRFYRV-DPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVISL 478
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-501 5.99e-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: 59.78  E-value: 5.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVKFTQQGEV-KVSIWQEPEN-KIFFRVKDSGIGIPQDELDKIFAMYYqvTDSAGGKpatGTGIGLSVS 476
Cdd:cd16976     1 IQQVLMNLLQNALDAMGKVENpRIRIAARRLGgRLVLVVRDNGPGIAEEHLSRVFDPFF--TTKPVGK---GTGLGLSIS 75
                          90       100
                  ....*....|....*....|....*
gi 2027583119 477 RRLAQNMGGDIQVESEIGQGSTFTL 501
Cdd:cd16976    76 YGIVEEHGGRLSVANEEGAGARFTF 100
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
527-644 6.47e-11

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: 60.26  E-value: 6.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVEDIELNVVVACSVLENLGN-TVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLpPLIA 605
Cdd:cd17552     3 RILVIDDEEDIREVVQACLEKLAGwEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSI-PVIL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2027583119 606 LTANV-LKDKKEYFDAGMDGVLSKPLSVPALTQVIEQFWG 644
Cdd:cd17552    82 LTAKAqPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLLG 121
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
686-764 7.62e-11

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


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 59.32  E-value: 7.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 686 DGLDVFEKMLPGYLAILDSNMV----AKDQKGIVEEAHKIKGAAGSVGLKNLQKIAQQIQS---------PDLPAWWDNV 752
Cdd:cd00088     3 ELLELFLEEAEELLEELERALLeledAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDlldalrdglEVTPELIDLL 82
                          90
                  ....*....|..
gi 2027583119 753 QEWVDELKQDWK 764
Cdd:cd00088    83 LDALDALKAELE 94
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
524-655 8.07e-11

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: 61.90  E-value: 8.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 524 PALHILLVEDIELNVVVACSVLENLG-NTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQqydkEDLPP 602
Cdd:COG3707     2 RGLRVLVVDDEPLRRADLREGLREAGyEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISE----ERPAP 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2027583119 603 LIALTANVLKDKKEY-FDAGMDGVLSKPLS----VPALTQVIEQFWgEHTSQNEEVEN 655
Cdd:COG3707    78 VILLTAYSDPELIERaLEAGVSAYLVKPLDpedlLPALELALARFR-ELRALRRELAK 134
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
528-629 8.65e-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: 59.10  E-value: 8.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVED---IeLNVVVAcsVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDkedlPPLI 604
Cdd:cd17620     1 ILVIEDepqI-RRFLRT--ALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSA----VPVI 73
                          90       100
                  ....*....|....*....|....*.
gi 2027583119 605 ALTA-NVLKDKKEYFDAGMDGVLSKP 629
Cdd:cd17620    74 VLSArDEESDKIAALDAGADDYLTKP 99
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-489 1.19e-10

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: 59.01  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVKFTQQ-GEVKVSIWQEPENkIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGGKPAtgTGIGLSVSR 477
Cdd:cd16945     5 LRQAINNLLDNAIDFSPEgGLIALQLEADTEG-IELLVFDEGSGIPDYALNRVFERFYSLPRPHSGQKS--TGLGLAFVQ 81
                          90
                  ....*....|..
gi 2027583119 478 RLAQNMGGDIQV 489
Cdd:cd16945    82 EVAQLHGGRITL 93
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
528-629 1.29e-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: 58.63  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGN--TVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlPPLIA 605
Cdd:COG4753     2 VLIVDDEPLIREGLKRILEWEAGfeVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPD---TKIII 78
                          90       100
                  ....*....|....*....|....*...
gi 2027583119 606 LTANvlkDKKEY----FDAGMDGVLSKP 629
Cdd:COG4753    79 LSGY---SDFEYaqeaIKLGADDYLLKP 103
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
528-595 1.75e-10

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: 58.66  E-value: 1.75e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2027583119 528 ILLVEDiELNVVVACS-VLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQY 595
Cdd:cd17550     1 ILIVDD-EEDIRESLSgILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKY 68
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
280-341 2.06e-10

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: 56.84  E-value: 2.06e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2027583119 280 SREKTTFISTISHELRTPLNGIVGLSRILLDTNLTSE-QSSYLKTIHVSAVTLGNIFNDVIEM 341
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEeQREYLERIREEAERLLRLINDLLDL 63
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
528-608 2.90e-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: 58.09  E-value: 2.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVED-IELNVVVAcSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlpPLIAL 606
Cdd:cd17623     1 ILLIDDdRELTELLT-EYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQV----PVLML 75

                  ..
gi 2027583119 607 TA 608
Cdd:cd17623    76 TA 77
PRK13560 PRK13560
hypothetical protein; Provisional
134-276 2.99e-10

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 63.92  E-value: 2.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 134 EQLKQEMKYREQTQVELEQQSVLLRSFLDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVM 213
Cdd:PRK13560  183 DGFAEDITERKRAEERIDEALHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQPADDYQ 262
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2027583119 214 ETDEKVFRHNVSLTYEQWLVYPDGRKACFELR--KVPFYDRVGKRHGLMGFGRDITERKRYQEAL 276
Cdd:PRK13560  263 EADAAKFDADGSQIIEAEFQNKDGRTRPVDVIfnHAEFDDKENHCAGLVGAITDISGRRAAEREL 327
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
526-580 4.06e-10

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 55.65  E-value: 4.06e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2027583119  526 LHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLP 580
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
519-641 8.10e-10

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: 57.14  E-value: 8.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 519 DDYPL--PALHILLVEDIELNVVVACSvlenlgntvdvamNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYD 596
Cdd:cd17535     5 DDHPLvrEGLRRLLESEPDIEVVGEAA-------------DGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYP 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2027583119 597 KedlPPLIALTANVLKDK-KEYFDAGMDGVLSKPLSVPALTQVIEQ 641
Cdd:cd17535    72 D---LKVIVLTAHDDPEYvLRALKAGAAGYLLKDSSPEELIEAIRA 114
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
395-503 1.03e-09

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: 56.39  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 395 DGTRLRQVLWNLIGNAVKFTQ-----QGEVKVSIWQEPENKIFFRVKDSGIGIPQDELDKIFAMYyqVTDSaggkpATGT 469
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEgrpsdVGEVRIRVEADQDGRIVLIVCDNGKGFPREMRHRATEPY--VTTR-----PKGT 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2027583119 470 GIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:cd16944    74 GLGLAIVKKIMEEHGGRISLSNREAGGACIRIIL 107
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
22-510 1.21e-09

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 61.46  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  22 RFSLLLASALVVLAMIMQMAVTIFLRGHVDSLDMVGSIFFGLIITPLAVYFLSVVVEQLEESRQRLSRMVDKLEVMRKRD 101
Cdd:COG3920    35 ALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAALLALLVLLLLLLLAAAALALALLLAALAGLLLLA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 102 AELNIQLHGNIEQLNLEIQEREKAERAHLELLEQLKQEMKYREQTQVELEQQSVLLRSFLDASPDLVYYRNENNEFSGCN 181
Cdd:COG3920   115 ALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAALLLLAEELAALRLAAAALLLLLAALLDLGLALAAL 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 182 RAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFRHNVSLTYEQwLVYPDGRKACFELRKVPFYDRVGKRHGLMG 261
Cdd:COG3920   195 AAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELER-RRRARGLGRLLLLLLLLLLLLRALLLLAAG 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 262 FGRDITERKRYQEALENASREKTTFISTISHELRTPLNGIVGLSRIlldtnltseQSSYLKTIHVSAVtlgnifndvieM 341
Cdd:COG3920   274 IRLVITERKRAEEELEASLEEKELLLRELHHRVKNNLQVVSSLLRL---------QARRADDPEAREA-----------L 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 342 DKIERR-----KVQ------LDNQPVALPEFVNDLENLSGLLVQPKGLKFVMDVAPTL--PKT------VLTDgtrlrqv 402
Cdd:COG3920   334 EESQNRiqalaLVHellyqsEDWEGVDLRDYLRELLEPLRDSYGGRGIRIELDGPDVElpADAavplglILNE------- 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 403 lwnLIGNAVKF----TQQGEVKVSiWQEPENKIFFRVKDSGIGIPqdeldkifamyyqvtdsAGGKPATGTGIGLSVSRR 478
Cdd:COG3920   407 ---LVTNALKHaflsGEGGRIRVS-WRREDGRLRLTVSDNGVGLP-----------------EDVDPPARKGLGLRLIRA 465
                         490       500       510
                  ....*....|....*....|....*....|..
gi 2027583119 479 LAQNMGGDIQVESEigQGSTFTLSITAPVVEE 510
Cdd:COG3920   466 LVRQLGGTLELDRP--EGTRVRITFPLAELAA 495
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
427-501 1.46e-09

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: 56.23  E-value: 1.46e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2027583119 427 PENKIFFRVKDSGIGIPQDELDKIFAMYYqvTDSAGGKpatGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTL 501
Cdd:cd16919    44 PGNYVCLEVSDTGSGMPAEVLRRAFEPFF--TTKEVGK---GTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRI 113
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
156-276 1.48e-09

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: 56.53  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 156 LLRSFLDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFRHNVSLTYEQWLVYP 235
Cdd:TIGR00229   4 RYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRR 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2027583119 236 -DGRKACFELRKVPfYDRVGKRHGLMGFGRDITERKRYQEAL 276
Cdd:TIGR00229  84 kDGSEIWVEVSVSP-IRTNGGELGVVGIVRDITERKEAEEAL 124
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
269-576 1.55e-09

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 61.49  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 269 RKRYQEALEN-----ASRE-------KTTFISTISHELRTPLNGIVGLSRILLDTNLTSEQSSYLKTIHVSAVTLGNIFN 336
Cdd:PRK10618  424 RDQDREVLVNkklqqAQREyeknqqaRKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVD 503
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 337 DVIEMDKIERRKVQLDNQPVALPEFVND--LENLSglLVQPKGLKFVMDVAPTLPKTVLTDGTRLRQVLWNLIGNAVKFT 414
Cdd:PRK10618  504 NIQLLNMLETQDWKPEQELFSLQDLIDEvlPEVLP--AIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTT 581
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 415 QQGEVKVSIWQEPENK--IFFRVKDSGIGIPQDELDKIfaMYYQVTDSAGGKPATGTGIGLSVSRRLAQNMGGDIQVESE 492
Cdd:PRK10618  582 AYGKITLEVDQDESSPdrLTIRILDTGAGVSIKELDNL--HFPFLNQTQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSR 659
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 493 IGQGSTFTLSITAPVVEevaEHQDSDDDYPLPALHILL---VEDIElNVVvaCSVLENLGNTVDVamngKDALAMFApgE 569
Cdd:PRK10618  660 EGLGTRYSIHLKMLAAD---PEVEEEEEKLLDGVTVLLditSEEVR-KIV--TRQLENWGATCIT----PDERLISQ--E 727

                  ....*..
gi 2027583119 570 YDLVLLD 576
Cdd:PRK10618  728 YDIFLTD 734
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
406-510 2.01e-09

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 60.42  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 406 LIGNAVKF-----TQQGEVKVSIWQEpENKIFFRVKDSGIGIPQDELDKIFAMYyqvtdsagGKPATGTGIGLS-VSRRL 479
Cdd:COG2972   344 LVENAIEHgiepkEGGGTIRISIRKE-GDRLVITVEDNGVGMPEEKLEKLLEEL--------SSKGEGRGIGLRnVRERL 414
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2027583119 480 AQNMGGD--IQVESEIGQGSTFTLSItaPVVEE 510
Cdd:COG2972   415 KLYYGEEygLEIESEPGEGTTVTIRI--PLEEE 445
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-502 2.04e-09

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: 55.51  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVKFTQQgEVKVSIWQEpENKIFFRVKDSGIGIPQDELDKIFAMYYQVtDSAGGKPATGTGIGLSVSRR 478
Cdd:cd16939     1 MARALDNLLRNALRYAHR-TVRIALLVS-GGRLTLIVEDDGPGIPAAARERVFEPFVRL-DPSRDRATGGFGLGLAIVHR 77
                          90       100
                  ....*....|....*....|....*
gi 2027583119 479 LAQNMGGDIQV-ESEIGqGSTFTLS 502
Cdd:cd16939    78 VALWHGGHVECdDSELG-GACFRLT 101
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
528-629 2.07e-09

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: 55.46  E-value: 2.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDielNVVVACSV---LENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLPpLI 604
Cdd:cd19927     1 ILLVDD---DPGIRLAVkdyLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIP-VI 76
                          90       100
                  ....*....|....*....|....*.
gi 2027583119 605 ALTANVL-KDKKEYFDAGMDGVLSKP 629
Cdd:cd19927    77 FLTAKGMtSDRIKGYNAGCDGYLSKP 102
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
526-641 2.12e-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: 55.81  E-value: 2.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 526 LHILLVEDIELNVVVACSVLENLG-NTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLPPLI 604
Cdd:cd19923     1 MKVLVVDDFSTMRRIIKNLLKELGfNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLM 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2027583119 605 ----ALTANVLKDKKeyfdAGMDGVLSKPLSVPALTQVIEQ 641
Cdd:cd19923    81 vtaeAKKENVIAAAQ----AGVNNYIVKPFTAATLKEKLEK 117
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
528-635 3.10e-09

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: 55.47  E-value: 3.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQqyDKEDLPPLIaLT 607
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRA--AGNDLPILV-LT 77
                          90       100
                  ....*....|....*....|....*....
gi 2027583119 608 A-NVLKDKKEYFDAGMDGVLSKPLSVPAL 635
Cdd:cd17627    78 ArDSVSDRVAGLDAGADDYLVKPFALEEL 106
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
528-629 4.11e-09

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: 55.02  E-value: 4.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLpPLIALT 607
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDI-PVILLT 79
                          90       100
                  ....*....|....*....|....*
gi 2027583119 608 AnvLKDKKEY---FDAGMDGVLSKP 629
Cdd:cd17598    80 T--LSDPRDVirgLECGADNFITKP 102
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
528-629 4.83e-09

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: 54.27  E-value: 4.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPG-EYDLVLLDIQLPD-MTGLDISRQLKQQYdkEDLPPLIA 605
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPGgMNGSQLAEEARRRR--PDLKVLLT 78
                          90       100
                  ....*....|....*....|....
gi 2027583119 606 LTANVLKDKKEYFDAGMDgVLSKP 629
Cdd:cd18161    79 SGYAENAIEGGDLAPGVD-VLSKP 101
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
529-632 5.09e-09

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: 54.67  E-value: 5.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 529 LLVEDIELNVVVACSV-LENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQqyDKEDLPPLIaLT 607
Cdd:cd17615     2 VLVVDDEPNITELLSMaLRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRA--DGPDVPVLF-LT 78
                          90       100
                  ....*....|....*....|....*.
gi 2027583119 608 A-NVLKDKKEYFDAGMDGVLSKPLSV 632
Cdd:cd17615    79 AkDSVEDRIAGLTAGGDDYVTKPFSL 104
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
388-503 5.23e-09

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: 55.16  E-value: 5.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 388 LPKTVLTDGTRLRQVLWNLIGNAVK------------FTQQGEVKVSIWQEPENK---------IFFRVKDSGIGIPQDE 446
Cdd:cd16938     1 LPDVVVGDERRVFQVLLHMLGNLLKmrngggnitfrvFLEGGSEDRSDRDWGPWRpsmsdesveIRFEVEINDSGSPSIE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2027583119 447 LDKIFamyyQVTDSAGGKPATGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:cd16938    81 SASMR----NSLNRRYNLSELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
527-608 5.39e-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: 5.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVEDiELNV-VVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQydKEDLpPLIA 605
Cdd:cd17554     2 KILVVDD-EENIrELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREK--KPDL-PVII 77

                  ...
gi 2027583119 606 LTA 608
Cdd:cd17554    78 CTA 80
pleD PRK09581
response regulator PleD; Reviewed
528-631 5.63e-09

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 59.14  E-value: 5.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLpPLIALT 607
Cdd:PRK09581    5 ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHI-PVVMVT 83
                          90       100
                  ....*....|....*....|....*
gi 2027583119 608 A-NVLKDKKEYFDAGMDGVLSKPLS 631
Cdd:PRK09581   84 AlDDPEDRVRGLEAGADDFLTKPIN 108
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
528-629 8.20e-09

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: 53.74  E-value: 8.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlpPLIALT 607
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSNV----PVIMVT 76
                          90       100
                  ....*....|....*....|...
gi 2027583119 608 ANVLK-DKKEYFDAGMDGVLSKP 629
Cdd:cd17621    77 AKDSEiDKVVGLELGADDYVTKP 99
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
527-639 8.57e-09

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: 54.23  E-value: 8.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVEDielNVVVACSV---LENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLpPL 603
Cdd:cd17562     2 KILAVDD---SASIRQMVsftLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFT-PI 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2027583119 604 IALTANVLKDKK-EYFDAGMDGVLSKPLSVPALTQVI 639
Cdd:cd17562    78 LMLTTESSDEKKqEGKAAGATGWLVKPFDPEQLLEVV 114
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
145-311 1.30e-08

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: 57.86  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 145 QTQVELEQQSVLLRSFLDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFRHnv 224
Cdd:COG3829     1 AEELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSPLLEVLKTGKPVTGV-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 225 sltyeqwLVYPDGRKACFELRKVPFYDRvGKRHGLMGFGRDITERKRYQEALENASREKttfistiSHELRTPLNGIVGL 304
Cdd:COG3829    79 -------IQKTGGKGKTVIVTAIPIFED-GEVIGAVETFRDITELKRLERKLREEELER-------GLSAKYTFDDIIGK 143

                  ....*..
gi 2027583119 305 SRILLDT 311
Cdd:COG3829   144 SPAMKEL 150
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
395-503 1.36e-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: 53.23  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 395 DGTRLRQVLWNLIGNAVKFT-QQGEVKVSIWQEpENKIFFRVKDSGIGIPQDELDKIFAMYYqvTDSAGGKPATGTGIGL 473
Cdd:cd16975     1 DTLLLSRALINIISNACQYApEGGTVSISIYDE-EEYLYFEIWDNGHGFSEQDLKKALELFY--RDDTSRRSGGHYGMGL 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 2027583119 474 SVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:cd16975    78 YIAKNLVEKHGGSLIIENSQKGGAEVTVKI 107
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
527-594 1.52e-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: 53.16  E-value: 1.52e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2027583119 527 HILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQ 594
Cdd:cd17619     2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQ 69
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
527-608 2.50e-08

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 55.35  E-value: 2.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVED---IELNVVVAcsvLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYdkEDLpPL 603
Cdd:PRK11083    5 TILLVEDeqaIADTLVYA---LQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFH--PAL-PV 78

                  ....*
gi 2027583119 604 IALTA 608
Cdd:PRK11083   79 IFLTA 83
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
528-629 2.50e-08

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: 52.80  E-value: 2.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVED-------IELnvvvacsVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQydKEDL 600
Cdd:cd17616     1 VLLIEDdsataqsIEL-------MLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLA--KVKT 71
                          90       100
                  ....*....|....*....|....*....
gi 2027583119 601 PPLIALTANVLKDKKEYFDAGMDGVLSKP 629
Cdd:cd17616    72 PILILSGLADIEDKVKGLGFGADDYMTKP 100
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
526-635 3.61e-08

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 54.93  E-value: 3.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 526 LHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQydKEDLPPLIA 605
Cdd:PRK09836    1 MKLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSA--NKGMPILLL 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 2027583119 606 LTANVLKDKKEYFDAGMDGVLSKPLSVPAL 635
Cdd:PRK09836   79 TALGTIEHRVKGLELGADDYLVKPFAFAEL 108
glnL PRK11073
nitrogen regulation protein NR(II);
273-501 4.53e-08

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 55.86  E-value: 4.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 273 QEALENASREkttFISTISHELRTPLNGIVG----LSRILLDTNLTSeqssYLKTIHVSAVTLGNIFNDVIEMDKIERRK 348
Cdd:PRK11073  123 QHAQQVAARD---LVRGLAHEIKNPLGGLRGaaqlLSKALPDPALTE----YTKVIIEQADRLRNLVDRLLGPQRPGTHV 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 349 VQLDNQPValpEFVNDLENLSgllvQPKGLKFVMDVAPTLPKtVLTDGTRLRQVLWNLIGNAVKFTQQGEVKVSIWQEPE 428
Cdd:PRK11073  196 TESIHKVA---ERVVQLVSLE----LPDNVRLIRDYDPSLPE-LAHDPDQIEQVLLNIVRNALQALGPEGGTITLRTRTA 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 429 NKIFF-----------RVKDSGIGIPQDELDKIFamYYQVTDSAGGkpatgTGIGLSVSRRLAQNMGGDIQVESEIGQgS 497
Cdd:PRK11073  268 FQLTLhgeryrlaariDIEDNGPGIPPHLQDTLF--YPMVSGREGG-----TGLGLSIARNLIDQHSGKIEFTSWPGH-T 339

                  ....
gi 2027583119 498 TFTL 501
Cdd:PRK11073  340 EFSV 343
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
164-266 9.42e-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: 50.71  E-value: 9.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 164 SPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFRHNVSLTYEQWLVYPDGRKACFE 243
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                          90       100
                  ....*....|....*....|...
gi 2027583119 244 LRKVPFYDRVGKRHGLMGFGRDI 266
Cdd:cd00130    81 VSLTPIRDEGGEVIGLLGVVRDI 103
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
528-635 9.89e-08

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 50.89  E-value: 9.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDielNVVVACSVLENL---GNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEdlpPLI 604
Cdd:cd17573     1 ILLIED---DSTLGKEISKGLnekGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSI---VVI 74
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2027583119 605 ALTANVLKDKK-EYFDAGMDGVLSKPLSVPAL 635
Cdd:cd17573    75 VLSDNPKTEQEiEAFKEGADDYIAKPFDFKVL 106
PRK11517 PRK11517
DNA-binding response regulator HprR;
526-654 1.05e-07

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 53.36  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 526 LHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlpPLIA 605
Cdd:PRK11517    1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT----PVIC 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2027583119 606 LTA-NVLKDKKEYFDAGMDGVLSKPLSVPALTQVIEQFWGEHTSQNEEVE 654
Cdd:PRK11517   77 LTArDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQHHALNSTLE 126
PRK10336 PRK10336
two-component system response regulator QseB;
526-632 1.43e-07

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 52.98  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 526 LHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEdlpPLIA 605
Cdd:PRK10336    1 MRILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQRE---PVLI 77
                          90       100
                  ....*....|....*....|....*...
gi 2027583119 606 LTA-NVLKDKKEYFDAGMDGVLSKPLSV 632
Cdd:PRK10336   78 LTArDALAERVEGLRLGADDYLCKPFAL 105
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
528-631 1.93e-07

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: 50.11  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVED-------IELNvvvacsvLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedl 600
Cdd:cd17614     1 ILVVDDekpisdiLKFN-------LTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSNV--- 70
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2027583119 601 pPLIALTANVLK-DKKEYFDAGMDGVLSKPLS 631
Cdd:cd17614    71 -PIIMLTAKDSEvDKVLGLELGADDYVTKPFS 101
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
395-503 2.76e-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: 49.58  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 395 DGTRLRQVLWNLIGNAVKFTQQGEVKVSIWQEPENKIF----------FRVKDSGIGIPQDELDKIFAmyyqvtdsaGGK 464
Cdd:cd16932     3 DQIRLQQVLADFLLNAVRFTPSPGGWVEIKVSPTKKQIgdgvhvihleFRITHPGQGLPEELVQEMFE---------ENQ 73
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2027583119 465 PATGTGIGLSVSRRLAQNMGGDIQVESEIGQgSTFTLSI 503
Cdd:cd16932    74 WTTQEGLGLSISRKLVKLMNGDVRYLREAGR-SYFLITL 111
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
528-595 4.39e-07

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: 49.26  E-value: 4.39e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2027583119 528 ILLVEDIELnvvvacsVLENLGNTVD----------VAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQY 595
Cdd:cd17536     1 VLIVDDEPL-------IREGLKKLIDweelgfevvgEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELY 71
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
528-631 6.13e-07

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: 48.74  E-value: 6.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIElnvVVACSV---LENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDkeDLPPLI 604
Cdd:cd17555     3 ILVIDDDE---VVRESIaayLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESP--DTPVIV 77
                          90       100
                  ....*....|....*....|....*..
gi 2027583119 605 ALTANVLKDKKEYFDAGMDGVLSKPLS 631
Cdd:cd17555    78 VSGAGVMSDAVEALRLGAWDYLTKPIE 104
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
527-631 7.35e-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: 48.52  E-value: 7.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVED-IELNVVVAcSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlpPLIA 605
Cdd:cd19939     1 RILIVEDeLELARLTR-DYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHSHV----PILM 75
                          90       100
                  ....*....|....*....|....*..
gi 2027583119 606 LTANVLK-DKKEYFDAGMDGVLSKPLS 631
Cdd:cd19939    76 LTARTEEmDRVLGLEMGADDYLCKPFS 102
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
527-593 8.67e-07

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: 48.21  E-value: 8.67e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027583119 527 HILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQ 593
Cdd:cd17563     2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRA 68
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
527-652 1.36e-06

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: 49.14  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEdlpPLIAL 606
Cdd:COG4567     6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDA---RIVVL 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2027583119 607 T-----ANVLkdkkEYFDAGMDGVLSKPLSVPALTQVIEQFWGEHTSQNEE 652
Cdd:COG4567    83 TgyasiATAV----EAIKLGADDYLAKPADADDLLAALERAEGDAPAPPEN 129
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
528-629 1.61e-06

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: 47.46  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlpPLIALT 607
Cdd:cd17626     3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAESGV----PIVMLT 78
                          90       100
                  ....*....|....*....|...
gi 2027583119 608 ANV-LKDKKEYFDAGMDGVLSKP 629
Cdd:cd17626    79 AKSdTVDVVLGLESGADDYVAKP 101
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
518-642 2.01e-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: 47.24  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 518 DDDYPLPALHILLVEDIELNVVVAcsvlenlgntvdVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDK 597
Cdd:cd19925     7 EDDPMVAEIHRAYVEQVPGFTVIG------------TAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHD 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2027583119 598 EDlppLIALT-ANVLKDKKEYFDAGMDGVLSKPLSVPALTQVIEQF 642
Cdd:cd19925    75 VD---VIVVTaANDVETVREALRLGVVDYLIKPFTFERLRQRLERY 117
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
528-663 2.57e-06

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 49.42  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFaPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlpPLIALT 607
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLL-DDSIDLLLLDVMMPKKNGIDTLKELRQTHQT----PVIMLT 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2027583119 608 ANVLK-DKKEYFDAGMDGVLSKPLSVPALTQVIE-----QFWGEhtsQNEEVENCDVTSQVD 663
Cdd:PRK10955   79 ARGSElDRVLGLELGADDYLPKPFNDRELVARIRailrrSHWSE---QQQNNDNGSPTLEVD 137
PRK10610 PRK10610
chemotaxis protein CheY;
526-637 2.88e-06

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 47.28  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 526 LHILLVEDIELNVVVACSVLENLG-NTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLPPLI 604
Cdd:PRK10610    6 LKFLVVDDFSTMRRIVRNLLKELGfNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLM 85
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2027583119 605 aLTANVlkdKKEYF----DAGMDGVLSKPLSVPALTQ 637
Cdd:PRK10610   86 -VTAEA---KKENIiaaaQAGASGYVVKPFTAATLEE 118
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
555-604 3.35e-06

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: 46.76  E-value: 3.35e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2027583119 555 AMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLkqqyDKEDLPPLI 604
Cdd:cd17532    30 AENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKL----SKLAKPPLI 75
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
528-609 3.55e-06

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: 46.60  E-value: 3.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVED-IELNVVVAcSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlpPLIAL 606
Cdd:cd17622     3 ILLVEDdPKLARLIA-DFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG----PILLL 77

                  ...
gi 2027583119 607 TAN 609
Cdd:cd17622    78 TAL 80
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
401-503 5.20e-06

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: 45.88  E-value: 5.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 401 QVLW-NLIGNAVKFTQQG-EVKVSIWQEpENKIFFRVKDSGIGIPQDELDKIFAMyyQVTDSAGgkpaTGTGIgLSVSRR 478
Cdd:cd16957     7 QVLVeNAIRHAFPKRKENnEVRVVVKKD-QHKVHVSVSDNGQGIPEERLDLLGKT--TVTSEKG----TGTAL-ENLNRR 78
                          90       100
                  ....*....|....*....|....*..
gi 2027583119 479 LAQNMG--GDIQVESEIGQGSTFTLSI 503
Cdd:cd16957    79 LIGLFGseACLHIESEVHGGTEVWFVI 105
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
364-491 5.34e-06

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: 46.47  E-value: 5.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 364 DLENL-SGL--LVQPKGLKFVMDVAPTLpkTVLTDGTRLRQVLWNLIGNAVKFTQqGEVKVSIWQEPEnKIFFRVKDSGI 440
Cdd:cd16954     2 LLDSLcSALnkVYQRKGVSISLDISPEL--RFPGERNDLMELLGNLLDNACKWCL-EFVEVTARQTDG-GLHLIVDDDGP 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2027583119 441 GIPQDELDKIFAMYYQVTDSAGGKpatgtGIGLSVSRRLAQNMGGDIQVES 491
Cdd:cd16954    78 GVPESQRSKIFQRGQRLDEQRPGQ-----GLGLAIAKEIVEQYGGELSLSD 123
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
527-631 6.97e-06

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: 45.83  E-value: 6.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlpPLIAL 606
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFSDV----PIIMV 76
                          90       100
                  ....*....|....*....|....*.
gi 2027583119 607 TANVLK-DKKEYFDAGMDGVLSKPLS 631
Cdd:cd19938    77 TARVEEiDRLLGLELGADDYICKPYS 102
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
526-641 7.13e-06

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 49.26  E-value: 7.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 526 LHILLVEDIelnvVVACSVLENL----GNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQydKEDLP 601
Cdd:PRK10365    6 IDILVVDDD----ISHCTILQALlrgwGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAL--NPAIP 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2027583119 602 PLIALTANVLKDKKEYFDAGMDGVLSKPLSVPALTQVIEQ 641
Cdd:PRK10365   80 VLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
524-608 8.15e-06

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 49.08  E-value: 8.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 524 PALHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDisrQLKQQYDKEDLPPL 603
Cdd:PRK11361    3 AINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIK---ALKEMRSHETRTPV 79

                  ....*
gi 2027583119 604 IALTA 608
Cdd:PRK11361   80 ILMTA 84
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-503 9.12e-06

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: 45.08  E-value: 9.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVKFT--QQGEVKVSIWQE-------PENKIFFRVK--DSGIGIPQDELDKIFamYYQVTDSAGGkpat 467
Cdd:cd16918     1 LIQVFLNLVRNAAQALagSGGEIILRTRTQrqvtlghPRHRLALRVSviDNGPGIPPDLQDTIF--YPMVSGRENG---- 74
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2027583119 468 gTGIGLSVSRRLAQNMGGDIQVESEIGQgSTFTLSI 503
Cdd:cd16918    75 -TGLGLAIAQNIVSQHGGVIECDSQPGH-TVFSVSL 108
orf27 CHL00148
Ycf27; Reviewed
527-631 1.38e-05

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 47.40  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVEDiELNVVvacSVLEN----LGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlpP 602
Cdd:CHL00148    8 KILVVDD-EAYIR---KILETrlsiIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKESDV----P 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 2027583119 603 LIALTA-NVLKDKKEYFDAGMDGVLSKPLS 631
Cdd:CHL00148   80 IIMLTAlGDVSDRITGLELGADDYVVKPFS 109
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
451-503 1.62e-05

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


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 46.04  E-value: 1.62e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2027583119 451 FAMYYQVTDSAGgkpatgTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:cd16916   131 FSTAEQVTDVSG------RGVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRL 177
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
526-591 2.02e-05

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 44.88  E-value: 2.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2027583119 526 LHILLVEDIELNVVVACSVLENLGN--TVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQL 591
Cdd:COG2197     2 IRVLIVDDHPLVREGLRALLEAEPDieVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
528-640 2.16e-05

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: 44.19  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLG-NTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKqQYDKEdlPPLIAL 606
Cdd:cd17542     3 VLIVDDAAFMRMMLKDILTKAGyEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIK-KIDPN--AKVIMC 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2027583119 607 TANVLKDK-KEYFDAGMDGVLSKPLSVPALTQVIE 640
Cdd:cd17542    80 SAMGQEEMvKEAIKAGAKDFIVKPFQPERVLEAVE 114
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
528-629 2.19e-05

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: 43.97  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDiELNVVVACS-VLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlpPLIAL 606
Cdd:cd19936     1 IALVDD-DRNILTSVSmALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKSTL----PVIFL 75
                          90       100
                  ....*....|....*....|....*....
gi 2027583119 607 TAnvlkdKKEYFDA------GMDGVLSKP 629
Cdd:cd19936    76 TS-----KDDEIDEvfglrmGADDYITKP 99
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
180-268 2.30e-05

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


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 43.60  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 180 CNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFRHNVSLTYEqwLVYPDGRKACFELRKVPFYDRVGKRHGL 259
Cdd:pfam13426   7 VNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVREFEVV--LYRKDGEPFPVLVSLAPIRDDGGELVGI 84

                  ....*....
gi 2027583119 260 MGFGRDITE 268
Cdd:pfam13426  85 IAILRDITE 93
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
527-629 2.37e-05

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 44.43  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFA--PgEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLpPLI 604
Cdd:cd17544     2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEqhP-DIKLVITDYNMPEMDGFELVREIRKKYSRDQL-AII 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2027583119 605 --------ALTANVLKdkkeyfdAGMDGVLSKP 629
Cdd:cd17544    80 gisasgdnALSARFIK-------AGANDFLTKP 105
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-504 2.49e-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: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 399 LRQVLWNLIGNAVKFT-QQGEVKVSIWQEpENKIFFRVKDSGIGIPQDELDKIFAMYYQVTDSaggKPATGTGIGLSVSR 477
Cdd:cd16923     1 LQRVFSNLLSNAIKYSpENTRIYITSFLT-DDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS---RNTEGAGLGLSIAK 76
                          90       100
                  ....*....|....*....|....*..
gi 2027583119 478 RLAQNMGGDIQVESEiGQGSTFTLSIT 504
Cdd:cd16923    77 AIIELHGGSASAEYD-DNHDLFKVRLP 102
PRK10337 PRK10337
sensor protein QseC; Provisional
405-481 2.55e-05

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 47.34  E-value: 2.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027583119 405 NLIGNAVKFTQQGEVkVSIWQEPENkifFRVKDSGIGIPQDELDKIFAMYYQvtdsAGGKPATGTGIGLSVSRRLAQ 481
Cdd:PRK10337  359 NLLDNAIRYSPQGSV-VDVTLNARN---FTVRDNGPGVTPEALARIGERFYR----PPGQEATGSGLGLSIVRRIAK 427
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
526-640 2.77e-05

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 43.94  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 526 LHILLVEDIELNVVVACSVLENLGNTV-DVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQqydkEDLPPLI 604
Cdd:cd19932     1 VRVLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITS----ENIAPIV 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2027583119 605 ALTANVLKDKKEYF-DAGMDGVLSKPLSVPALTQVIE 640
Cdd:cd19932    77 LLTAYSQQDLVERAkEAGAMAYLVKPFSESDLIPAIE 113
PRK13435 PRK13435
response regulator; Provisional
523-631 3.11e-05

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 44.66  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 523 LPALHILLVED---IELNVvvACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPD-MTGLDISRQLKQQYDKE 598
Cdd:PRK13435    3 LRQLKVLIVEDealIALEL--EKLVEEAGHEVVGIAMSSEQAIALGRRRQPDVALVDVHLADgPTGVEVARRLSADGGVE 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2027583119 599 dlppLIALTANVlKDKKEYFdAGMDGVLSKPLS 631
Cdd:PRK13435   81 ----VVFMTGNP-ERVPHDF-AGALGVIAKPYS 107
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
545-608 4.27e-05

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 43.42  E-value: 4.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2027583119 545 LENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYdkEDLpPLIALTA 608
Cdd:cd19919    20 LAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRH--PDL-PVIIMTA 80
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
528-635 4.65e-05

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 45.57  E-value: 4.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQydkeDLPPLIALT 607
Cdd:PRK10529    4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQW----SAIPVIVLS 79
                          90       100
                  ....*....|....*....|....*....
gi 2027583119 608 A-NVLKDKKEYFDAGMDGVLSKPLSVPAL 635
Cdd:PRK10529   80 ArSEESDKIAALDAGADDYLSKPFGIGEL 108
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
526-591 5.55e-05

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: 43.20  E-value: 5.55e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027583119 526 LHILLVEDIELNVVVACSVLENLGN-TVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQL 591
Cdd:cd17530     1 LRVLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHL 67
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
545-629 6.64e-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: 42.53  E-value: 6.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 545 LENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYdkEDLPPLIALTANVLKDKKEYFDAGMDG 624
Cdd:cd19926    18 LGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRL--PQTPVAVITAYGSLDTAIEALKAGAFD 95

                  ....*
gi 2027583119 625 VLSKP 629
Cdd:cd19926    96 FLTKP 100
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
528-591 9.27e-05

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: 42.46  E-value: 9.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2027583119 528 ILLVEDiELNVVVACSV-LENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQL 591
Cdd:cd19922     1 ILLLEK-ERNLAHFLSLeLQKEGYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAEKL 64
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
268-494 9.78e-05

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 45.78  E-value: 9.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 268 ERKRYqealenaSREKTTfISTISHELRTPLNgivglsriLLDTNLTSEQSSylKTIHVSAVtlgnifnDVIEMDKIERR 347
Cdd:PRK10815  259 ERERY-------TKYRTT-LTDLTHSLKTPLA--------VLQSTLRSLRSG--KQMSVEQA-------EPIMLEQISRI 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 348 KVQLD----------NQPVALPEfvndLENLSGLL----------VQPKGLKFVMDVAPTLpkTVLTDGTRLRQVLWNLI 407
Cdd:PRK10815  314 SQQIGyylhrasmrsEHNLLSRE----LHSVAPLLdnltsalnkvYQRKGVNITLDISPEI--TFVGEKNDFMEVMGNVL 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 408 GNAVKFTQQGeVKVSIwQEPENKIFFRVKDSGIGIPQDELDKIFAMYyQVTDSAggKPatGTGIGLSVSRRLAQNMGGDI 487
Cdd:PRK10815  388 DNACKYCLEF-VEISA-RQTDEHLHIVVEDDGPGIPESKRELIFDRG-QRADTL--RP--GQGLGLSVAREITEQYEGKI 460

                  ....*...
gi 2027583119 488 QV-ESEIG 494
Cdd:PRK10815  461 SAgDSPLG 468
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
552-629 1.03e-04

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: 42.38  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 552 VDVAMNGKDALAMFA---PgeyDLVLLDIQLPDMTGLDISRQLKQQYDkedlPPLIALTANVLKDKKEYFDA---GMDGV 625
Cdd:cd17541    29 VGTARDGEEALEKIKelkP---DVITLDIEMPVMDGLEALRRIMAERP----TPVVMVSSLTEEGAEITLEAlelGAVDF 101

                  ....
gi 2027583119 626 LSKP 629
Cdd:cd17541   102 IAKP 105
PRK10766 PRK10766
two-component system response regulator TorR;
527-596 1.06e-04

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 44.26  E-value: 1.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYD 596
Cdd:PRK10766    4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRST 73
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
357-510 1.55e-04

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 44.22  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 357 ALPEFVNDLENLSGLLVQpkglkFVMDVAP-TLPKTVLTDGTR-LRQvlwnLIGNAVKFTQQGEVKVSIWQEPeNKIFFR 434
Cdd:COG4585   128 ALEELAERLLRAAGIRVE-----LDVDGDPdRLPPEVELALYRiVQE----ALTNALKHAGATRVTVTLEVDD-GELTLT 197
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2027583119 435 VKDSGIGIPQDEldkifamyyqvtdsaggkpATGTGIGLSVSRRLAQNMGGDIQVESEIGQGstFTLSITAPVVEE 510
Cdd:COG4585   198 VRDDGVGFDPEA-------------------APGGGLGLRGMRERAEALGGTLTIGSAPGGG--TRVRATLPLAAA 252
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
431-498 1.66e-04

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: 43.10  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 431 IFFRVKDSGIGIPQDELDKIFAMYY----------QVTDSAGGKPAT--GTGIGLSVSRRLAQNMGGDIQVESEIGQGST 498
Cdd:cd16929    84 LTIKISDRGGGIPREDLARLFSYMYstapqpslddFSDLISGTQPSPlaGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTD 163
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
456-503 2.28e-04

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 44.40  E-value: 2.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2027583119 456 QVTD-SaggkpatGTGIGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:COG0643   375 EVTDlS-------GRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRL 416
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
528-595 2.65e-04

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: 41.23  E-value: 2.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2027583119 528 ILLVEDiELNVVVA-CSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQY 595
Cdd:cd17569     3 ILLVDD-EPNILKAlKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERY 70
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
525-640 3.25e-04

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 42.78  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 525 ALHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEDLPPLI 604
Cdd:PRK10161    2 ARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVM 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2027583119 605 ALTANVLKDKKEYFDAGMDGVLSKPLSVPALTQVIE 640
Cdd:PRK10161   82 LTARGEEEDRVRGLETGADDYITKPFSPKELVARIK 117
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
542-608 4.75e-04

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: 42.01  E-value: 4.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027583119 542 CSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQydkEDLPPLIALTA 608
Cdd:COG4566    16 AFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAAR---GSPLPVIFLTG 79
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
528-641 4.82e-04

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD 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. 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: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 40.94  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDiELNVVVACS-VLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQydKEDLpPLIAL 606
Cdd:cd17549     1 VLLVDD-DADVREALQqTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIREL--DPDL-PVILI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2027583119 607 TAnvlkdkkeYFDAGM------DGV---LSKPLSVPALTQVIEQ 641
Cdd:cd17549    77 TG--------HGDVPMaveamrAGAydfLEKPFDPERLLDVVRR 112
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
156-221 5.08e-04

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: 38.92  E-value: 5.08e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2027583119  156 LLRSFLDASPDLVYYRNENNEFSGCNRAMELLTGKSEKHLVGLTPLDIYDVEIASKVMETDEKVFR 221
Cdd:smart00091   2 RLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
528-644 5.60e-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: 40.23  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQydKEDLPPLIALT 607
Cdd:cd17553     3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVI--DENIRVIIMTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2027583119 608 ANVLKDKKEYFDAGMDGVLSKPLSVPALTQVIEQFWG 644
Cdd:cd17553    81 YGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYLP 117
PRK15369 PRK15369
two component system response regulator;
528-628 6.36e-04

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 41.99  E-value: 6.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIEL------NVVVACSVLENLGNTvdvamngKDALAMFAPG---EYDLVLLDIQLPDMTGLDISRQLKQQYdke 598
Cdd:PRK15369    6 ILLVDDHELiingikNMLAPYPRYKIVGQV-------DNGLEVYNACrqlEPDIVILDLGLPGMNGLDVIPQLHQRW--- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2027583119 599 dlPPL--IALTANVL-KDKKEYFDAGMDG-VLSK 628
Cdd:PRK15369   76 --PAMniLVLTARQEeHMASRTLAAGALGyVLKK 107
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
528-594 6.36e-04

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: 39.95  E-value: 6.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2027583119 528 ILLVEDIEL--NVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQ 594
Cdd:cd19930     1 VLIAEDQEMvrGALAALLELEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREE 69
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
555-643 6.58e-04

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate/nitrite response regulator protein NarL contains an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. Escherichia coli NarL activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons, and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal. Phosphorylation of the NarL REC domain releases the C-terminal HTH output domain that subsequently binds specific DNA promoter sites to repress or activate gene expression. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 40.02  E-value: 6.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 555 AMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQqyDKEDLPPLIALTANVLKDKKEYFDAGMDGVLSKPLSVPA 634
Cdd:cd19931    30 ASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALRE--EGVSARIVILTVSDAEDDVVTALRAGADGYLLKDMEPED 107

                  ....*....
gi 2027583119 635 LTQVIEQFW 643
Cdd:cd19931   108 LLEALKQAA 116
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
555-642 6.72e-04

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 40.21  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 555 AMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQydkeDLPPL-IALTANVLKDKKE-YFDAGMDGVLSKPLSV 632
Cdd:cd17593    31 AENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVE----QLETKvIVVSGDVQPEAKErVLELGALAFLKKPFDP 106
                          90
                  ....*....|
gi 2027583119 633 PALTQVIEQF 642
Cdd:cd17593   107 EKLAQLLEEL 116
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
528-629 7.34e-04

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: 39.67  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPG---------EYDLVLLDIQLPDMTGLDISRQLKQQYDKE 598
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLakegndlskELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2027583119 599 DLPPLIALTANVLKDKKEYFDAGMDGVLSKP 629
Cdd:cd19924    81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
PRK11173 PRK11173
two-component response regulator; Provisional
527-636 9.60e-04

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 41.54  E-value: 9.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVED--IELNVVVacSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlpPLI 604
Cdd:PRK11173    5 HILIVEDelVTRNTLK--SIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQANV----ALM 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2027583119 605 ALTA---NVlkDKKEYFDAGMDGVLSKPLSVPALT 636
Cdd:PRK11173   79 FLTGrdnEV--DKILGLEIGADDYITKPFNPRELT 111
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
552-608 1.01e-03

phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the phosphorelay system in the early stage of spore formation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress and may act in the with sigma factor spo0H to control the expression of some genes that are critical to the sporulation process. Spo0A contains a regulatory N-terminal REC domain and a C-terminal DNA-binding transcription activation domain as its effector/output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 39.51  E-value: 1.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2027583119 552 VDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLkQQYDKEDLPPLIALTA 608
Cdd:cd17561    30 VGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKL-RRMRLEKRPKIIMLTA 85
PRK10816 PRK10816
two-component system response regulator PhoP;
526-629 1.13e-03

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 41.26  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 526 LHILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQqyDKEDLPPLIA 605
Cdd:PRK10816    1 MRVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRS--NDVSLPILVL 78
                          90       100
                  ....*....|....*....|....
gi 2027583119 606 LTANVLKDKKEYFDAGMDGVLSKP 629
Cdd:PRK10816   79 TARESWQDKVEVLSAGADDYVTKP 102
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
78-153 1.18e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 42.25  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119  78 EQLEESRQRL----SRMvDKLEVMRKRdaelniQLHGNIEQLNLEIQEREKAERAHLELLEQ-LKQEMKYREQTQVELEQ 152
Cdd:pfam15709 329 EQEKASRDRLraerAEM-RRLEVERKR------REQEEQRRLQQEQLERAEKMREELELEQQrRFEEIRLRKQRLEEERQ 401

                  .
gi 2027583119 153 Q 153
Cdd:pfam15709 402 R 402
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
552-641 1.20e-03

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 41.17  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 552 VDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKqqyDKEDLPPLIALT-ANVLKDKKEYFDAGMDGVLSKPL 630
Cdd:PRK10651   35 VGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLR---EKSLSGRIVVFSvSNHEEDVVTALKRGADGYLLKDM 111
                          90
                  ....*....|.
gi 2027583119 631 SVPALTQVIEQ 641
Cdd:PRK10651  112 EPEDLLKALQQ 122
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
528-609 1.95e-03

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: 38.76  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMF--APGEYDLVLLDIQLPDMTGLDIsrqLKQQYDKEDLpPLIA 605
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLreNKDEFDLVITDVHMPDMDGFEF---LELIRLEMDL-PVIM 76

                  ....
gi 2027583119 606 LTAN 609
Cdd:cd17584    77 MSAD 80
ompR PRK09468
osmolarity response regulator; Provisional
545-629 2.06e-03

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 40.73  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 545 LENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQydkEDLPPLIALTANVLK-DKKEYFDAGMD 623
Cdd:PRK09468   25 LTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQ---NNPTPIIMLTAKGEEvDRIVGLEIGAD 101

                  ....*.
gi 2027583119 624 GVLSKP 629
Cdd:PRK09468  102 DYLPKP 107
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
527-639 2.24e-03

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: 38.58  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 527 HILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlpPLIAL 606
Cdd:cd17594     1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSDV----PIIII 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2027583119 607 TANVLK--DKKEYFDAGMDGVLSKPLSVPALTQVI 639
Cdd:cd17594    77 SGDRRDeiDRVVGLELGADDYLAKPFGLRELLARV 111
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
451-503 2.68e-03

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 41.25  E-value: 2.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2027583119 451 FAMYYQVTDsaggkpATGTGIGLSVSRRLAQNMGGDIQVESEIGQGST------FTLSI 503
Cdd:PRK10547  475 FSTAEQVTD------VSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTirillpLTLAI 527
PRK15479 PRK15479
transcriptional regulator TctD;
545-635 3.17e-03

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 39.70  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 545 LENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQydKEDLPPLIaLTANV-LKDKKEYFDAGMD 623
Cdd:PRK15479   20 LVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKR--GQTLPVLL-LTARSaVADRVKGLNVGAD 96
                          90
                  ....*....|..
gi 2027583119 624 GVLSKPLSVPAL 635
Cdd:PRK15479   97 DYLPKPFELEEL 108
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
545-641 3.34e-03

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: 37.96  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 545 LENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlPPLIALTAN------VLKDKKEYF 618
Cdd:cd17537    20 LRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSN---IPIIFITGHgdvpmaVEAMKAGAV 96
                          90       100
                  ....*....|....*....|...
gi 2027583119 619 DagmdgVLSKPLSVPALTQVIEQ 641
Cdd:cd17537    97 D-----FLEKPFRDQVLLDAIEQ 114
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
77-154 3.72e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 40.81  E-value: 3.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119   77 VEQLE------ESRQRLSRMvdKLEVMRKRDAELNIQLHGNIEQLNleIQEREKAERA--HLELL-EQ-------LKQEM 140
Cdd:PRK10929   189 VDELElaqlsaNNRQELARL--RSELAKKRSQQLDAYLQALRNQLN--SQRQREAERAleSTELLaEQsgdlpksIVAQF 264
                           90
                   ....*....|....
gi 2027583119  141 KYREQTQVELEQQS 154
Cdd:PRK10929   265 KINRELSQALNQQA 278
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
552-627 4.72e-03

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 39.62  E-value: 4.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2027583119 552 VDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKedlpPLIALTAnvlkdkkeyFDAGMDGVLS 627
Cdd:PRK10701   28 VTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQG----PIVLLTS---------LDSDMNHILA 90
PRK09191 PRK09191
two-component response regulator; Provisional
528-608 5.23e-03

two-component response regulator; Provisional


Pssm-ID: 236402 [Multi-domain]  Cd Length: 261  Bit Score: 39.45  E-value: 5.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 528 ILLVED-------IElnvvvacSVLENLGNTV-DVAMNGKDALAMFAPGEYDLVLLDIQLPD-MTGLDISRQLKQQYDKe 598
Cdd:PRK09191  140 VLIIEDepiiamdLE-------QLVESLGHRVtGIARTRAEAVALAKKTRPGLILADIQLADgSSGIDAVNDILKTFDV- 211
                          90
                  ....*....|
gi 2027583119 599 dlpPLIALTA 608
Cdd:PRK09191  212 ---PVIFITA 218
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
77-153 5.71e-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: 5.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027583119  77 VEQLEESRQRLSRMVDKLEVMRKRDAELNIQLHGNIEQLNLEIQEREKAERAHLELLEQLKQEMKYREQTQVELEQQ 153
Cdd:COG1196   283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
395-503 6.40e-03

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 39.82  E-value: 6.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027583119 395 DGTRLRQVLWNLIGNAVKF---TQQGEVKVSIWQEPE-NKIFFRVKDSGIGIPQDELDKIFAMYYQVTDSAGGKpatgTG 470
Cdd:PRK15053  429 DSTEFAAIVGNLLDNAFEAslrSDEGNKIVELFLSDEgDDVVIEVADQGCGVPESLRDKIFEQGVSTRADEPGE----HG 504
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2027583119 471 IGLSVSRRLAQNMGGDIQVESEIGQGSTFTLSI 503
Cdd:PRK15053  505 IGLYLIASYVTRCGGVITLEDNDPCGTLFSIFI 537
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
78-153 6.88e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 6.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2027583119  78 EQLEESRQRLSRMVDKLEVMRKRDAELNIQLHGNIEQLNLEIQEREKAERAHLELLEQLKQEMKYREQTQVELEQQ 153
Cdd:COG1196   267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
PRK10693 PRK10693
two-component system response regulator RssB;
554-631 8.32e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 39.20  E-value: 8.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2027583119 554 VAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQYDKEdlpPLIALTA-NVLKDKKEYFDAGMDGVLSKPLS 631
Cdd:PRK10693    2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQT---PVLVISAtENMADIAKALRLGVQDVLLKPVK 77
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
528-594 8.42e-03

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: 36.88  E-value: 8.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027583119 528 ILLVEDIELNVVVACSVLENLGNTVDVAMNGKDALAMFAPGEYDLVLLDIQLPDMTGLDISRQLKQQ 594
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQI 67
 
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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