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Conserved domains on  [gi|506340081|ref|WP_015859800|]
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S16 family serine protease [Solidesulfovibrio magneticus]

Protein Classification

response regulator( domain architecture ID 13370666)

response regulator receives the signal from a sensor partner in two-component systems through its receiver (REC) domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Lon super family cl33893
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
18-668 0e+00

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG0466:

Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 720.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  18 SDIGQLRARIDSQELPHHAREAANRELERLEKTDPSAAEYGVGLAYLDFLLGLPWAAVTPDRLDLAQAEAVLDARHHGLG 97
Cdd:COG0466  252 DEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLE 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  98 QIKDRVLEYLASRALRaapdfhvlvvddediaranlehvlrkegykvrgaanglealaevrrsefdlivtdlkmDKMdgl 177
Cdd:COG0466  332 KVKERILEYLAVRKLK----------------------------------------------------------KKL--- 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 178 qllaearrlspatrvmlvtgfatvdtaveamrqgavyylakpvnldelratvaalakektapasfRSPVLCFSGPPGTGK 257
Cdd:COG0466  351 -----------------------------------------------------------------KGPILCLVGPPGVGK 365
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 258 TSVGQAIAEALGRRFHRISLAGLRDEAELRGHRRTYVGALPGRVLQSYARLGVANPVFMLDEIDKIGKDFRGDPAAVFLE 337
Cdd:COG0466  366 TSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLE 445
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 338 MLDPEQNSQFVDNYLEAPFDLSRTLFIATANDLAELSGPLRDRLEVVPFRGYTTREKVRIAGEHLLPRQLREHGLTHPFP 417
Cdd:COG0466  446 VLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEEL 525
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 418 TVTEEALRQVVTGHTREAGVRNLDRELGRICRKLARLRLEqgEGAAPAEVDAALAAALLGPPPYRGETAGAAPRLGVATG 497
Cdd:COG0466  526 KISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAE--GKKKKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTG 603
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 498 LVYADYGGEIISVEAIRMEGTGELLLTGSLGEVLRESARTALSLVRSRAGELGVDPGLFATQDVHVHIPAGSIPKEGSSA 577
Cdd:COG0466  604 LAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSA 683
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 578 GLTVAVALASLFSGRPLRPDVAMTGEITLTGNVLPVGGIREKILAAARAGMREVLVPEANRPEVaamagEDSPE------ 651
Cdd:COG0466  684 GITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDL-----EEIPEevkkgl 758
                        650
                 ....*....|....*....
gi 506340081 652 --VLVRHVATVfaaLPLAL 668
Cdd:COG0466  759 efHPVEHIDEV---LKIAL 774
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
120-230 1.96e-33

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: 123.80  E-value: 1.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 506340081  200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVA 230
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
18-668 0e+00

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 720.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  18 SDIGQLRARIDSQELPHHAREAANRELERLEKTDPSAAEYGVGLAYLDFLLGLPWAAVTPDRLDLAQAEAVLDARHHGLG 97
Cdd:COG0466  252 DEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLE 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  98 QIKDRVLEYLASRALRaapdfhvlvvddediaranlehvlrkegykvrgaanglealaevrrsefdlivtdlkmDKMdgl 177
Cdd:COG0466  332 KVKERILEYLAVRKLK----------------------------------------------------------KKL--- 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 178 qllaearrlspatrvmlvtgfatvdtaveamrqgavyylakpvnldelratvaalakektapasfRSPVLCFSGPPGTGK 257
Cdd:COG0466  351 -----------------------------------------------------------------KGPILCLVGPPGVGK 365
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 258 TSVGQAIAEALGRRFHRISLAGLRDEAELRGHRRTYVGALPGRVLQSYARLGVANPVFMLDEIDKIGKDFRGDPAAVFLE 337
Cdd:COG0466  366 TSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLE 445
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 338 MLDPEQNSQFVDNYLEAPFDLSRTLFIATANDLAELSGPLRDRLEVVPFRGYTTREKVRIAGEHLLPRQLREHGLTHPFP 417
Cdd:COG0466  446 VLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEEL 525
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 418 TVTEEALRQVVTGHTREAGVRNLDRELGRICRKLARLRLEqgEGAAPAEVDAALAAALLGPPPYRGETAGAAPRLGVATG 497
Cdd:COG0466  526 KISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAE--GKKKKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTG 603
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 498 LVYADYGGEIISVEAIRMEGTGELLLTGSLGEVLRESARTALSLVRSRAGELGVDPGLFATQDVHVHIPAGSIPKEGSSA 577
Cdd:COG0466  604 LAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSA 683
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 578 GLTVAVALASLFSGRPLRPDVAMTGEITLTGNVLPVGGIREKILAAARAGMREVLVPEANRPEVaamagEDSPE------ 651
Cdd:COG0466  684 GITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDL-----EEIPEevkkgl 758
                        650
                 ....*....|....*....
gi 506340081 652 --VLVRHVATVfaaLPLAL 668
Cdd:COG0466  759 efHPVEHIDEV---LKIAL 774
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
18-661 0e+00

endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat shock and other stresses in E. coli, B. subtilis, and other species. The yeast member, designated PIM1, is located in the mitochondrial matrix, required for mitochondrial function, and also induced by heat shock. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273258 [Multi-domain]  Cd Length: 775  Bit Score: 603.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081   18 SDIGQLRARIDSQELPHHAREAANRELERLEKTDPSAAEYGVGLAYLDFLLGLPWAAVTPDRLDLAQAEAVLDARHHGLG 97
Cdd:TIGR00763 247 DELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLK 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081   98 QIKDRVLEYLASRALRaapdfhvlvvddediaranlehvlrkegykvrgaanglealaevrrsefdlivtdlkmDKMDGl 177
Cdd:TIGR00763 327 KVKERILEYLAVQKLR----------------------------------------------------------GKMKG- 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  178 qllaearrlspatrvmlvtgfatvdtaveamrqgavyylakpvnldelratvaalakektapasfrsPVLCFSGPPGTGK 257
Cdd:TIGR00763 348 -------------------------------------------------------------------PILCLVGPPGVGK 360
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  258 TSVGQAIAEALGRRFHRISLAGLRDEAELRGHRRTYVGALPGRVLQSYARLGVANPVFMLDEIDKIGKDFRGDPAAVFLE 337
Cdd:TIGR00763 361 TSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLE 440
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  338 MLDPEQNSQFVDNYLEAPFDLSRTLFIATANDLAELSGPLRDRLEVVPFRGYTTREKVRIAGEHLLPRQLREHGLTHPFP 417
Cdd:TIGR00763 441 VLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDEL 520
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  418 TVTEEALRQVVTGHTREAGVRNLDRELGRICRKLARLRLEQGEGAAPA----EVDAALAAALLGPPPYRGETAGAAPRLG 493
Cdd:TIGR00763 521 KITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVEQGEKKKSEaesvVITPDNLKKYLGKPVFTYERAYEVTPPG 600
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  494 VATGLVYADYGGEIISVEAIRMEGTGELLLTGSLGEVLRESARTALSLVRSRAGELGVDPGLFATQDVHVHIPAGSIPKE 573
Cdd:TIGR00763 601 VVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKD 680
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  574 GSSAGLTVAVALASLFSGRPLRPDVAMTGEITLTGNVLPVGGIREKILAAARAGMREVLVPEANR---PEVAAMAGEDSP 650
Cdd:TIGR00763 681 GPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRrdlEELPENVKEGLE 760
                         650
                  ....*....|.
gi 506340081  651 EVLVRHVATVF 661
Cdd:TIGR00763 761 IHFVKHYDEVL 771
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
23-668 5.43e-146

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 443.61  E-value: 5.43e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  23 LRARIDSQELPHHAREAANRELERLEKTDPSAAEYGVGLAYLDFLLGLPWAAVTPDRLDLAQAEAVLDARHHGLGQIKDR 102
Cdd:PRK10787 254 LKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDR 333
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 103 VLEYLASRAlraapdfhvlvvddediaRANlehvlrkegyKVRGaanglealaevrrsefdlivtdlkmdkmdglqllae 182
Cdd:PRK10787 334 ILEYLAVQS------------------RVN----------KIKG------------------------------------ 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 183 arrlspatrvmlvtgfatvdtaveamrqgavyylakpvnldelratvaalakektapasfrsPVLCFSGPPGTGKTSVGQ 262
Cdd:PRK10787 350 --------------------------------------------------------------PILCLVGPPGVGKTSLGQ 367
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 263 AIAEALGRRFHRISLAGLRDEAELRGHRRTYVGALPGRVLQSYARLGVANPVFMLDEIDKIGKDFRGDPAAVFLEMLDPE 342
Cdd:PRK10787 368 SIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPE 447
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 343 QNSQFVDNYLEAPFDLSRTLFIATANDLaELSGPLRDRLEVVPFRGYTTREKVRIAGEHLLPRQLREHGLTHPFPTVTEE 422
Cdd:PRK10787 448 QNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDS 526
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 423 ALRQVVTGHTREAGVRNLDRELGRICRKLARlRLEQGEGAAPAEVDAALAAALLGPPPYRGETAGAAPRLGVATGLVYAD 502
Cdd:PRK10787 527 AIIGIIRYYTREAGVRSLEREISKLCRKAVK-QLLLDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTE 605
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 503 YGGEIISVEAIRMEGTGELLLTGSLGEVLRESARTALSLVRSRAGELGVDPGLFATQDVHVHIPAGSIPKEGSSAGLTVA 582
Cdd:PRK10787 606 VGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMC 685
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 583 VALASLFSGRPLRPDVAMTGEITLTGNVLPVGGIREKILAAARAGMREVLVPEANRPEVAAMAGEDSPEVLVRHVATVFA 662
Cdd:PRK10787 686 TALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEE 765

                 ....*.
gi 506340081 663 ALPLAL 668
Cdd:PRK10787 766 VLTLAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
241-389 1.15e-87

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 271.74  E-value: 1.15e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 241 SFRSPVLCFSGPPGTGKTSVGQAIAEALGRRFHRISLAGLRDEAELRGHRRTYVGALPGRVLQSYARLGVANPVFMLDEI 320
Cdd:cd19500   34 SMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEI 113
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506340081 321 DKIGKDFRGDPAAVFLEMLDPEQNSQFVDNYLEAPFDLSRTLFIATANDLAELSGPLRDRLEVVPFRGY 389
Cdd:cd19500  114 DKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATANSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
477-664 2.41e-73

Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.


Pssm-ID: 428442 [Multi-domain]  Cd Length: 205  Bit Score: 235.21  E-value: 2.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  477 GPPPYRGETAGAAPRLGVATGLVYADYGGEIISVEAIRMEGTGELLLTGSLGEVLRESARTALSLVRSRAGELGVDPGLF 556
Cdd:pfam05362  12 GVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDPDFF 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  557 ATQDVHVHIPAGSIPKEGSSAGLTVAVALASLFSGRPLRPDVAMTGEITLTGNVLPVGGIREKILAAARAGMREVLVPEA 636
Cdd:pfam05362  92 EKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVIIPKE 171
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 506340081  637 NRPEVaamagEDSPE--------VLVRHVATVFAAL 664
Cdd:pfam05362 172 NEKDL-----EDIPEnvregleiIPVEHVDEVLKHA 202
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
120-230 1.96e-33

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: 123.80  E-value: 1.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 506340081  200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVA 230
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
119-238 1.33e-31

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 119.18  E-value: 1.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLS--PATRVMLVT 196
Cdd:COG0784    7 RILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPrlPDIPIIALT 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 506340081 197 GFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEKTA 238
Cdd:COG0784   87 AYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
120-235 4.82e-31

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: 117.44  E-value: 4.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGY---KVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVT 196
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDWEELgfeVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 506340081 197 GFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKE 235
Cdd:cd17536   81 GYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKEE 119
PRK15115 PRK15115
response regulator GlrR; Provisional
119-320 2.10e-23

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 103.76  E-value: 2.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:PRK15115   7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKPVNLDELRATVAAlAKEKTAPAS---------FRSPVL-----------------CFSGP 252
Cdd:PRK15115  87 GSIPDAVAATQQGVFSFLTKPVDRDALYKAIDD-ALEQSAPATderwreaivTRSPLMlrlleqarmvaqsdvsvLINGQ 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506340081 253 PGTGKTSVGQAIAEALGRR---FHRISLAGLRD---EAELRGHRRtyvGALPGRVLQSYARLGVAN-PVFMLDEI 320
Cdd:PRK15115 166 SGTGKEILAQAIHNASPRAskpFIAINCGALPEqllESELFGHAR---GAFTGAVSNREGLFQAAEgGTLFLDEI 237
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
119-171 8.77e-13

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: 63.36  E-value: 8.77e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 506340081   119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKM 171
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMM 54
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
243-384 4.85e-05

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.90  E-value: 4.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081   243 RSPVLCFSGPPGTGKTSVGQAIAEALGR---RFHRISLAGLRDEAELRGHRRTYVGALPGRVLQSYARLGVA------NP 313
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPpggGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAlarklkPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506340081   314 VFMLDEIDKIGKDfrgdpaavflEMLDPEQNSQFVDNYLEAPFDLSRTLFIATANDLAELSGPLRDRLEVV 384
Cdd:smart00382  81 VLILDEITSLLDA----------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRR 141
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
18-668 0e+00

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 720.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  18 SDIGQLRARIDSQELPHHAREAANRELERLEKTDPSAAEYGVGLAYLDFLLGLPWAAVTPDRLDLAQAEAVLDARHHGLG 97
Cdd:COG0466  252 DEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLE 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  98 QIKDRVLEYLASRALRaapdfhvlvvddediaranlehvlrkegykvrgaanglealaevrrsefdlivtdlkmDKMdgl 177
Cdd:COG0466  332 KVKERILEYLAVRKLK----------------------------------------------------------KKL--- 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 178 qllaearrlspatrvmlvtgfatvdtaveamrqgavyylakpvnldelratvaalakektapasfRSPVLCFSGPPGTGK 257
Cdd:COG0466  351 -----------------------------------------------------------------KGPILCLVGPPGVGK 365
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 258 TSVGQAIAEALGRRFHRISLAGLRDEAELRGHRRTYVGALPGRVLQSYARLGVANPVFMLDEIDKIGKDFRGDPAAVFLE 337
Cdd:COG0466  366 TSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLE 445
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 338 MLDPEQNSQFVDNYLEAPFDLSRTLFIATANDLAELSGPLRDRLEVVPFRGYTTREKVRIAGEHLLPRQLREHGLTHPFP 417
Cdd:COG0466  446 VLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEEL 525
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 418 TVTEEALRQVVTGHTREAGVRNLDRELGRICRKLARLRLEqgEGAAPAEVDAALAAALLGPPPYRGETAGAAPRLGVATG 497
Cdd:COG0466  526 KISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAE--GKKKKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTG 603
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 498 LVYADYGGEIISVEAIRMEGTGELLLTGSLGEVLRESARTALSLVRSRAGELGVDPGLFATQDVHVHIPAGSIPKEGSSA 577
Cdd:COG0466  604 LAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSA 683
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 578 GLTVAVALASLFSGRPLRPDVAMTGEITLTGNVLPVGGIREKILAAARAGMREVLVPEANRPEVaamagEDSPE------ 651
Cdd:COG0466  684 GITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDL-----EEIPEevkkgl 758
                        650
                 ....*....|....*....
gi 506340081 652 --VLVRHVATVfaaLPLAL 668
Cdd:COG0466  759 efHPVEHIDEV---LKIAL 774
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
18-661 0e+00

endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat shock and other stresses in E. coli, B. subtilis, and other species. The yeast member, designated PIM1, is located in the mitochondrial matrix, required for mitochondrial function, and also induced by heat shock. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273258 [Multi-domain]  Cd Length: 775  Bit Score: 603.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081   18 SDIGQLRARIDSQELPHHAREAANRELERLEKTDPSAAEYGVGLAYLDFLLGLPWAAVTPDRLDLAQAEAVLDARHHGLG 97
Cdd:TIGR00763 247 DELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLK 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081   98 QIKDRVLEYLASRALRaapdfhvlvvddediaranlehvlrkegykvrgaanglealaevrrsefdlivtdlkmDKMDGl 177
Cdd:TIGR00763 327 KVKERILEYLAVQKLR----------------------------------------------------------GKMKG- 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  178 qllaearrlspatrvmlvtgfatvdtaveamrqgavyylakpvnldelratvaalakektapasfrsPVLCFSGPPGTGK 257
Cdd:TIGR00763 348 -------------------------------------------------------------------PILCLVGPPGVGK 360
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  258 TSVGQAIAEALGRRFHRISLAGLRDEAELRGHRRTYVGALPGRVLQSYARLGVANPVFMLDEIDKIGKDFRGDPAAVFLE 337
Cdd:TIGR00763 361 TSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLE 440
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  338 MLDPEQNSQFVDNYLEAPFDLSRTLFIATANDLAELSGPLRDRLEVVPFRGYTTREKVRIAGEHLLPRQLREHGLTHPFP 417
Cdd:TIGR00763 441 VLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDEL 520
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  418 TVTEEALRQVVTGHTREAGVRNLDRELGRICRKLARLRLEQGEGAAPA----EVDAALAAALLGPPPYRGETAGAAPRLG 493
Cdd:TIGR00763 521 KITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVEQGEKKKSEaesvVITPDNLKKYLGKPVFTYERAYEVTPPG 600
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  494 VATGLVYADYGGEIISVEAIRMEGTGELLLTGSLGEVLRESARTALSLVRSRAGELGVDPGLFATQDVHVHIPAGSIPKE 573
Cdd:TIGR00763 601 VVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKD 680
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  574 GSSAGLTVAVALASLFSGRPLRPDVAMTGEITLTGNVLPVGGIREKILAAARAGMREVLVPEANR---PEVAAMAGEDSP 650
Cdd:TIGR00763 681 GPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRrdlEELPENVKEGLE 760
                         650
                  ....*....|.
gi 506340081  651 EVLVRHVATVF 661
Cdd:TIGR00763 761 IHFVKHYDEVL 771
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
23-668 5.43e-146

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 443.61  E-value: 5.43e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  23 LRARIDSQELPHHAREAANRELERLEKTDPSAAEYGVGLAYLDFLLGLPWAAVTPDRLDLAQAEAVLDARHHGLGQIKDR 102
Cdd:PRK10787 254 LKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDR 333
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 103 VLEYLASRAlraapdfhvlvvddediaRANlehvlrkegyKVRGaanglealaevrrsefdlivtdlkmdkmdglqllae 182
Cdd:PRK10787 334 ILEYLAVQS------------------RVN----------KIKG------------------------------------ 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 183 arrlspatrvmlvtgfatvdtaveamrqgavyylakpvnldelratvaalakektapasfrsPVLCFSGPPGTGKTSVGQ 262
Cdd:PRK10787 350 --------------------------------------------------------------PILCLVGPPGVGKTSLGQ 367
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 263 AIAEALGRRFHRISLAGLRDEAELRGHRRTYVGALPGRVLQSYARLGVANPVFMLDEIDKIGKDFRGDPAAVFLEMLDPE 342
Cdd:PRK10787 368 SIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPE 447
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 343 QNSQFVDNYLEAPFDLSRTLFIATANDLaELSGPLRDRLEVVPFRGYTTREKVRIAGEHLLPRQLREHGLTHPFPTVTEE 422
Cdd:PRK10787 448 QNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDS 526
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 423 ALRQVVTGHTREAGVRNLDRELGRICRKLARlRLEQGEGAAPAEVDAALAAALLGPPPYRGETAGAAPRLGVATGLVYAD 502
Cdd:PRK10787 527 AIIGIIRYYTREAGVRSLEREISKLCRKAVK-QLLLDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTE 605
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 503 YGGEIISVEAIRMEGTGELLLTGSLGEVLRESARTALSLVRSRAGELGVDPGLFATQDVHVHIPAGSIPKEGSSAGLTVA 582
Cdd:PRK10787 606 VGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMC 685
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 583 VALASLFSGRPLRPDVAMTGEITLTGNVLPVGGIREKILAAARAGMREVLVPEANRPEVAAMAGEDSPEVLVRHVATVFA 662
Cdd:PRK10787 686 TALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEE 765

                 ....*.
gi 506340081 663 ALPLAL 668
Cdd:PRK10787 766 VLTLAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
241-389 1.15e-87

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 271.74  E-value: 1.15e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 241 SFRSPVLCFSGPPGTGKTSVGQAIAEALGRRFHRISLAGLRDEAELRGHRRTYVGALPGRVLQSYARLGVANPVFMLDEI 320
Cdd:cd19500   34 SMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEI 113
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506340081 321 DKIGKDFRGDPAAVFLEMLDPEQNSQFVDNYLEAPFDLSRTLFIATANDLAELSGPLRDRLEVVPFRGY 389
Cdd:cd19500  114 DKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATANSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
477-664 2.41e-73

Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.


Pssm-ID: 428442 [Multi-domain]  Cd Length: 205  Bit Score: 235.21  E-value: 2.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  477 GPPPYRGETAGAAPRLGVATGLVYADYGGEIISVEAIRMEGTGELLLTGSLGEVLRESARTALSLVRSRAGELGVDPGLF 556
Cdd:pfam05362  12 GVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDPDFF 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  557 ATQDVHVHIPAGSIPKEGSSAGLTVAVALASLFSGRPLRPDVAMTGEITLTGNVLPVGGIREKILAAARAGMREVLVPEA 636
Cdd:pfam05362  92 EKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVIIPKE 171
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 506340081  637 NRPEVaamagEDSPE--------VLVRHVATVFAAL 664
Cdd:pfam05362 172 NEKDL-----EDIPEnvregleiIPVEHVDEVLKHA 202
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
119-426 1.34e-42

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: 159.36  E-value: 1.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:COG2204    4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKPVNLDELRATV------AALAKEKTAP--------------------ASFRSPVLcFSGP 252
Cdd:COG2204   84 GDVETAVEAIKAGAFDYLTKPFDLEELLAAVeralerRRLRRENAEDsgligrspamqevrrliekvAPSDATVL-ITGE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 253 PGTGKTSVGQAIAEALGRR---FHRISLAGLRD---EAELRGHRRtyvGALPGRVLQSYARLGVANP-VFMLDEIDKIgk 325
Cdd:COG2204  163 SGTGKELVARAIHRLSPRAdgpFVAVNCAAIPEellESELFGHEK---GAFTGAVARRIGKFELADGgTLFLDEIGEM-- 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 326 dfrgdPAAVFLEMLDPEQNSQFVDNYLEAPFDLSRTLFIATANDLAEL--SGPLRD----RLEVVPFRGYTTREK----V 395
Cdd:COG2204  238 -----PLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELveEGRFREdlyyRLNVFPIELPPLRERrediP 312
                        330       340       350
                 ....*....|....*....|....*....|.
gi 506340081 396 RIAgEHLLPRQLREHGLTHPFPTVTEEALRQ 426
Cdd:COG2204  313 LLA-RHFLARFAAELGKPVKLSPEALEALLA 342
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
120-230 1.96e-33

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: 123.80  E-value: 1.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 506340081  200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVA 230
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
119-238 1.33e-31

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 119.18  E-value: 1.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLS--PATRVMLVT 196
Cdd:COG0784    7 RILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPrlPDIPIIALT 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 506340081 197 GFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEKTA 238
Cdd:COG0784   87 AYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
120-235 4.82e-31

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: 117.44  E-value: 4.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGY---KVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVT 196
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDWEELgfeVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 506340081 197 GFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKE 235
Cdd:cd17536   81 GYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKEE 119
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
121-219 7.11e-31

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: 116.17  E-value: 7.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 121 LVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFAT 200
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                         90
                 ....*....|....*....
gi 506340081 201 VDTAVEAMRQGAVYYLAKP 219
Cdd:cd00156   81 EEDAVRALELGADDYLVKP 99
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
120-219 1.35e-30

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: 115.64  E-value: 1.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKE-GYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTG 197
Cdd:COG4753    2 VLIVDDEPLIREGLKRILEWEaGFEVVGeAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILSG 81
                         90       100
                 ....*....|....*....|..
gi 506340081 198 FATVDTAVEAMRQGAVYYLAKP 219
Cdd:COG4753   82 YSDFEYAQEAIKLGADDYLLKP 103
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
119-234 1.58e-30

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: 118.91  E-value: 1.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:COG0745    3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTAR 82
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAK 234
Cdd:COG0745   83 DDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLR 118
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
120-229 3.50e-30

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: 114.90  E-value: 3.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDE-DIaRANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:cd17550    1 ILIVDDEeDI-RESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGH 79
                         90       100       110
                 ....*....|....*....|....*....|.
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKPVNLDELRATV 229
Cdd:cd17550   80 GTIETAVKATKLGAYDFIEKPLSLDRLLLTI 110
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
119-232 4.69e-30

Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 114.51  E-value: 4.69e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:COG5803    4 KILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMMTAY 83
                         90       100       110
                 ....*....|....*....|....*....|....
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:COG5803   84 GELDMVEEAKELGAKGYFTKPFDIDELREAVNKL 117
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
120-229 8.01e-30

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: 113.65  E-value: 8.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17569    3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTGYA 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 506340081 200 TVDTAVEAMRQGAVY-YLAKPVNLDELRATV 229
Cdd:cd17569   83 DLDAAIEAINEGEIYrFLTKPWDDEELKETI 113
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
119-232 2.13e-29

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: 112.54  E-value: 2.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:cd17563    2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGY 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKPVNLDELratVAAL 232
Cdd:cd17563   82 ASIATAVEAIKLGADDYLAKPADADEI---LAAL 112
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
119-240 2.85e-29

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: 114.24  E-value: 2.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:COG4567    6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLTGY 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEKTAPA 240
Cdd:COG4567   86 ASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAPP 127
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
120-234 2.05e-28

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: 110.27  E-value: 2.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVA-ALAK 234
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRrALEK 116
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
119-233 1.91e-27

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: 109.23  E-value: 1.91e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLsPATR---VMLV 195
Cdd:COG3706    3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRAD-PRTAdipIIFL 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 506340081 196 TGFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALA 233
Cdd:COG3706   82 TALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVA 119
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
112-238 2.14e-27

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: 110.64  E-value: 2.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 112 LRAAPDFHVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPA-- 189
Cdd:COG3437    1 MRTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTrd 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 506340081 190 TRVMLVTGFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEKTA 238
Cdd:COG3437   81 IPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRL 129
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
120-230 7.42e-27

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: 105.36  E-value: 7.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVA 230
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVR 111
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
115-405 1.14e-25

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 110.71  E-value: 1.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 115 APDFHVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVML 194
Cdd:PRK11361   2 TAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 195 VTGFATVDTAVEAMRQGAVYYLAKPVNLDEL-------------RATVAALAKE----------------------KTAP 239
Cdd:PRK11361  82 MTAYAEVETAVEALRCGAFDYVIKPFDLDELnlivqralqlqsmKKEIRHLHQAlstswqwghiltnspammdickDTAK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 240 ASFRSPVLCFSGPPGTGKTSVGQAIAEALGRR---FHRISLAGLRD---EAELRGHRRtyvGALPGRVLQSYARLGVANP 313
Cdd:PRK11361 162 IALSQASVLISGESGTGKELIARAIHYNSRRAkgpFIKVNCAALPEsllESELFGHEK---GAFTGAQTLRQGLFERANE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 314 -VFMLDEIDKIgkdfrgdPAAVFLEMLDPEQNSQFVDNYLEAPFDLSRTLFIATANDLAEL--SGPLRD----RLEVVPF 386
Cdd:PRK11361 239 gTLLLDEIGEM-------PLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMvkEGTFREdlfyRLNVIHL 311
                        330       340
                 ....*....|....*....|..
gi 506340081 387 RGYTTREK---VRIAGEHLLPR 405
Cdd:PRK11361 312 ILPPLRDRredISLLANHFLQK 333
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
120-405 5.31e-25

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 108.58  E-value: 5.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDeDIARAN-LEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:PRK10365   8 ILVVDD-DISHCTiLQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKPVNLDELRAT-VAALAKEKTAPASF------------RSPVL-----------------C 248
Cdd:PRK10365  87 SSVETAVEALKTGALDYLIKPLDFDNLQATlEKALAHTHSIDAETpavtasqfgmvgKSPAMqhllseialvapseatvL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 249 FSGPPGTGKTSVGQAIAEALGRR---FHRISLAGLRD---EAELRGHRRtyvGALPGRVLQSYARLGVAN-PVFMLDEID 321
Cdd:PRK10365 167 IHGDSGTGKELVARAIHASSARSekpLVTLNCAALNEsllESELFGHEK---GAFTGADKRREGRFVEADgGTLFLDEIG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 322 KIGKDFRgdpaaVFLEMLDPEQNSQFVDNYLEAPFDLSrtLFIATANDLAE--LSGPLRD----RLEVV-----PFRgyT 390
Cdd:PRK10365 244 DISPMMQ-----VRLLRAIQEREVQRVGSNQTISVDVR--LIAATHRDLAAevNAGRFRQdlyyRLNVVaievpSLR--Q 314
                        330
                 ....*....|....*
gi 506340081 391 TREKVRIAGEHLLPR 405
Cdd:PRK10365 315 RREDIPLLAGHFLQR 329
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
119-247 1.23e-24

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 99.66  E-value: 1.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDE-DIARANLEHVLRKEGYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVT 196
Cdd:COG4565    5 RVLIVEDDpMVAELLRRYLERLPGFEVVGvASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVIVIT 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 506340081 197 GFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEKTAPASFRSPVL 247
Cdd:COG4565   85 AARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQEEDL 135
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
120-220 1.26e-23

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: 96.12  E-value: 1.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17555    3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGAG 82
                         90       100
                 ....*....|....*....|.
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPV 220
Cdd:cd17555   83 VMSDAVEALRLGAWDYLTKPI 103
PRK15115 PRK15115
response regulator GlrR; Provisional
119-320 2.10e-23

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 103.76  E-value: 2.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:PRK15115   7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKPVNLDELRATVAAlAKEKTAPAS---------FRSPVL-----------------CFSGP 252
Cdd:PRK15115  87 GSIPDAVAATQQGVFSFLTKPVDRDALYKAIDD-ALEQSAPATderwreaivTRSPLMlrlleqarmvaqsdvsvLINGQ 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506340081 253 PGTGKTSVGQAIAEALGRR---FHRISLAGLRD---EAELRGHRRtyvGALPGRVLQSYARLGVAN-PVFMLDEI 320
Cdd:PRK15115 166 SGTGKEILAQAIHNASPRAskpFIAINCGALPEqllESELFGHAR---GAFTGAVSNREGLFQAAEgGTLFLDEI 237
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
119-243 2.88e-23

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: 97.86  E-value: 2.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:COG4566    1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGH 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKPVNLDELRATV-AALAKEKTAPASFR 243
Cdd:COG4566   81 GDVPMAVRAMKAGAVDFLEKPFDDQALLDAVrRALARDRARRAERA 126
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
119-232 3.73e-23

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: 94.60  E-value: 3.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:cd17554    2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAY 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 506340081 199 ATVDTAVEAMRQGAvyYLAKPVNLDELRATVAAL 232
Cdd:cd17554   82 SEYKSDFSSWAADA--YVVKSSDLTELKETIKRL 113
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
120-229 3.83e-23

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: 94.84  E-value: 3.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRL---SPATRVMLVT 196
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELeggGRRTPIIALT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 197 GFATVDTAVEAMRQGAVYYLAKPVNLDELRATV 229
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
499-667 5.81e-23

Predicted archaeal serine protease, S18 family [General function prediction only];


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 97.36  E-value: 5.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 499 VYADYGGEIISVEA-IRMEGTGELLLTGS--LGEVLRESARTAlSLVRSRagELGVDPGLFatqDVHVHIPAGSIPKEGS 575
Cdd:COG1750   37 VSGTGEGVVINITVtVTYPGSGRVYVSTSplTGPDTQASARIA-ALVASL--LAGVDLSSY---DVYISIESDSPIVGGP 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 576 SAGLTVAVALASLFSGRPLRPDVAMTGEITLTGNVLPVGGIREKILAAARAGMREVLVPEANRPEVAAMAGEDSPEVL-- 653
Cdd:COG1750  111 SAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQAILTGYNTQVGETVDLve 190
                        170       180
                 ....*....|....*....|..
gi 506340081 654 --------VRHVATVFAALPLA 667
Cdd:COG1750  191 ygkelgvkVIEVSTIADALQYF 212
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
120-229 8.74e-23

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: 93.68  E-value: 8.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLV--TG 197
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIalTG 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 506340081 198 FATVDTAVEAMRQGAVYYLAKPVNLDELRATV 229
Cdd:cd17580   81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
120-229 1.06e-22

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: 93.77  E-value: 1.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYG 82
                         90       100       110
                 ....*....|....*....|....*....|
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDELRATV 229
Cdd:cd17553   83 ELDMIQESKELGALTHFAKPFDIDEIRDAV 112
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
247-389 1.94e-22

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 93.43  E-value: 1.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  247 LCFSGPPGTGKTSVGQAIAEALGRRFHRISLAGLRDeaelrghrrTYVGALPGRVLQSYARLGVANP-VFMLDEIDKIGK 325
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506340081  326 D-------FRGDPAAVFLEMLDPEQNSQfvdnyleapfdlSRTLFIATANDLAELSGPLRDRLEVVPFRGY 389
Cdd:pfam00004  72 SrgsggdsESRRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
121-219 2.31e-22

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: 92.09  E-value: 2.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 121 LVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFAT 200
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80
                         90
                 ....*....|....*....
gi 506340081 201 VDTAVEAMRQGAVYYLAKP 219
Cdd:cd17574   81 EEDKVLGLELGADDYITKP 99
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
119-229 1.70e-21

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 93.73  E-value: 1.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRK-EGYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVT 196
Cdd:COG3279    3 KILIVDDEPLARERLERLLEKyPDLEVVGeASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTT 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 197 GFAtvDTAVEAMRQGAVYYLAKPVNLDELRATV 229
Cdd:COG3279   83 AYD--EYALEAFEVNAVDYLLKPIDEERLAKAL 113
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
119-227 2.26e-21

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: 89.81  E-value: 2.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGY-KVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLsPATR---VML 194
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRAL-PGLEdvpIVM 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 195 VTGFATVDTAVEAMRQGAVYYLAKPVNLDELRA 227
Cdd:cd17551   81 ITADTDREVRLRALEAGATDFLTKPFDPVELLA 113
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
120-224 1.75e-20

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: 87.33  E-value: 1.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd19919    3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAHS 82
                         90       100
                 ....*....|....*....|....*
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDE 224
Cdd:cd19919   83 DLDSAVSAYQGGAFEYLPKPFDIDE 107
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
120-233 5.05e-20

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: 86.03  E-value: 5.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKE-GYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTG 197
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEpDIEVVGeAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 506340081 198 FATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALA 233
Cdd:cd17535   81 HDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVA 116
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
121-232 4.88e-19

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: 83.04  E-value: 4.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 121 LVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFAT 200
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 506340081 201 VDTAVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:cd17625   81 VEDRVKGLDLGADDYLPKPFSLAELLARIRAL 112
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
119-233 4.17e-18

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: 80.37  E-value: 4.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDED-IARANLEHVLRKEGYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVT 196
Cdd:cd19925    2 NVLIVEDDPmVAEIHRAYVEQVPGFTVIGtAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVT 81
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 506340081 197 GFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALA 233
Cdd:cd19925   82 AANDVETVREALRLGVVDYLIKPFTFERLRQRLERYR 118
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
118-232 4.81e-18

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: 80.33  E-value: 4.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 118 FHVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTG 197
Cdd:cd17537    1 ATVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITG 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 506340081 198 FATVDTAVEAMRQGAVYYLAKPVNLDEL-RATVAAL 232
Cdd:cd17537   81 HGDVPMAVEAMKAGAVDFLEKPFRDQVLlDAIEQAL 116
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
120-219 7.10e-18

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 79.47  E-value: 7.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRR-SEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQgKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISGG 81
                         90       100
                 ....*....|....*....|.
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKP 219
Cdd:cd18160   82 AAAAPELLSDAVGDNATLKKP 102
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
120-227 1.05e-17

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: 79.21  E-value: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVR--RSEFDLIVTDLKMDKMDGLQLLaEARRLSPATRVMLVTG 197
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRenKDEFDLVITDVHMPDMDGFEFL-ELIRLEMDLPVIMMSA 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 506340081 198 FATVDTAVEAMRQGAVYYLAKPVNLDELRA 227
Cdd:cd17584   80 DGSTSTVMKGLAHGACDYLLKPVSIEDLKN 109
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
119-220 3.22e-17

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: 77.54  E-value: 3.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLlaeARRL--SPATR---VM 193
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEV---CRRLkeDPETRhipVI 77
                         90       100
                 ....*....|....*....|....*..
gi 506340081 194 LVTGFATVDTAVEAMRQGAVYYLAKPV 220
Cdd:cd17538   78 MITALDDREDRIRGLEAGADDFLSKPI 104
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
119-230 4.36e-17

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: 77.73  E-value: 4.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLsPATR----VML 194
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKL-PAYKftpiLML 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 506340081 195 VTgfatvdTAVEAMRQ-----GAVYYLAKPVNLDELRATVA 230
Cdd:cd17562   81 TT------ESSDEKKQegkaaGATGWLVKPFDPEQLLEVVK 115
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
120-230 9.58e-17

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: 76.42  E-value: 9.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLlaeARRL--SPATR---VML 194
Cdd:cd17548    2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEA---TRLLkeDPATRdipVIA 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 506340081 195 VTGFATVDTAVEAMRQGAVYYLAKPVNLDELRATVA 230
Cdd:cd17548   79 LTAYAMKGDREKILEAGCDGYISKPIDTREFLETVA 114
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
120-230 1.54e-16

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: 78.46  E-value: 1.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLvTGF 198
Cdd:COG3707    6 VLVVDDEPLRRADLREGLREAGYEVVAeAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPAPVILL-TAY 84
                         90       100       110
                 ....*....|....*....|....*....|..
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKPVNLDELRATVA 230
Cdd:COG3707   85 SDPELIERALEAGVSAYLVKPLDPEDLLPALE 116
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
120-227 1.54e-16

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: 76.22  E-value: 1.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYK-VRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEAR---RLSpATRVMLV 195
Cdd:cd19923    3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRadgALS-HLPVLMV 81
                         90       100       110
                 ....*....|....*....|....*....|..
gi 506340081 196 TGFATVDTAVEAMRQGAVYYLAKPVNLDELRA 227
Cdd:cd19923   82 TAEAKKENVIAAAQAGVNNYIVKPFTAATLKE 113
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
120-232 3.94e-16

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: 74.73  E-value: 3.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:cd17627   81 SVSDRVAGLDAGADDYLVKPFALEELLARVRAL 113
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
120-220 5.26e-16

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: 74.08  E-value: 5.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLlaeARRL--SPATR---VML 194
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEV---CRRLkaDPATRhipVIF 77
                         90       100
                 ....*....|....*....|....*.
gi 506340081 195 VTGFATVDTAVEAMRQGAVYYLAKPV 220
Cdd:cd19920   78 LTALTDTEDKVKGFELGAVDYITKPF 103
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
120-219 6.74e-16

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: 73.95  E-value: 6.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEAL---------AEVRRSEFDLIVTDLKMDKMDGLQLLAEARRlSPAT 190
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALnklenlakeGNDLSKELDLIITDIEMPKMDGYELTFELRD-DPRL 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 506340081 191 R---VMLVTGFATVDTAVEAMRQGAVYYLAKP 219
Cdd:cd19924   80 AnipVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
120-225 3.80e-15

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: 72.04  E-value: 3.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKE-GYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPaTRVMLVTG 197
Cdd:cd17541    3 VLIVDDSAVMRKLLSRILESDpDIEVVGtARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERP-TPVVMVSS 81
                         90       100       110
                 ....*....|....*....|....*....|
gi 506340081 198 FAT--VDTAVEAMRQGAVYYLAKPVNLDEL 225
Cdd:cd17541   82 LTEegAEITLEALELGAVDFIAKPSGGISL 111
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
120-229 4.52e-15

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: 71.68  E-value: 4.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLvTGF 198
Cdd:cd19932    3 VLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIAPIVLL-TAY 81
                         90       100       110
                 ....*....|....*....|....*....|.
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKPVNLDELRATV 229
Cdd:cd19932   82 SQQDLVERAKEAGAMAYLVKPFSESDLIPAI 112
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
120-234 4.80e-15

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: 71.75  E-value: 4.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAK 234
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVKPFALEELLARLRALLR 115
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
120-229 6.47e-15

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: 71.16  E-value: 6.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:cd17542    3 VLIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSAM 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKPVNLDELRATV 229
Cdd:cd17542   83 GQEEMVKEAIKAGAKDFIVKPFQPERVLEAV 113
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
120-219 7.47e-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: 7.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDE-DIARAnLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:cd19935    1 ILVVEDEkKLAEY-LKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTAR 79
                         90       100
                 ....*....|....*....|.
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKP 219
Cdd:cd19935   80 DSVEDRVKGLDLGADDYLVKP 100
fixJ PRK09390
response regulator FixJ; Provisional
115-241 1.05e-14

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 73.11  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 115 APDFHVLVVDDEDIARANLEHVLRKEGYKVR---GAANGLEALAEVRrseFDLIVTDLKMDKMDGLQLLAEARRLSPATR 191
Cdd:PRK09390   1 SDKGVVHVVDDDEAMRDSLAFLLDSAGFEVRlfeSAQAFLDALPGLR---FGCVVTDVRMPGIDGIELLRRLKARGSPLP 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 506340081 192 VMLVTGFATVDTAVEAMRQGAVYYLAKPVNLDELRATV-AALAKEKTAPAS 241
Cdd:PRK09390  78 VIVMTGHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIeRALAQAPEAAKS 128
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
120-232 1.23e-14

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: 70.46  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17615    2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKD 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:cd17615   82 SVEDRIAGLTAGGDDYVTKPFSLEEVVARLRAL 114
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
120-237 1.52e-14

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: 70.26  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGY--KVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTG 197
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEHPDieIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 506340081 198 FAtvDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEKT 237
Cdd:cd17532   81 YD--EYAVEAFELNAVDYLLKPFSEERLAEALAKLRKRLS 118
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
121-232 1.75e-14

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: 69.99  E-value: 1.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 121 LVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRlSPATR----VMLVT 196
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRS-DPKTSsipiIMLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 506340081 197 GFATVDTAVeAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:cd19937   80 KGEEFDKVL-GLELGADDYITKPFSPRELLARVKAV 114
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
120-232 2.96e-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: 69.62  E-value: 2.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTKPFHIEELLARLRAL 113
PRK10643 PRK10643
two-component system response regulator PmrA;
120-232 3.30e-14

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 72.38  E-value: 3.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:PRK10643   3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTARD 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:PRK10643  83 TLEDRVAGLDVGADDYLVKPFALEELHARIRAL 115
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
120-219 4.04e-14

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: 68.72  E-value: 4.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                         90       100
                 ....*....|....*....|
gi 506340081 200 TVDTAVEAMRQGAVYYLAKP 219
Cdd:cd19926   81 SLDTAIEALKAGAFDFLTKP 100
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
120-234 6.22e-14

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of this subfamily are 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 belongs to the nitrogen regulatory protein C (NtrC) family of response regulators, which activate transcription by RNA polymerase (RNAP) in response to a change in the environment. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Proteins in this subfamily contain an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 68.93  E-value: 6.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRkEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17596    3 ILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGYT 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 506340081 200 TVDTAVEAMRQGAVY-YLAKPVNLDELRATVAALAK 234
Cdd:cd17596   82 DSEDIIAGINEAGIYqYLTKPWHPDQLLLTVRNAAR 117
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
120-220 6.46e-14

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: 68.14  E-value: 6.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRR-SEFDLIVTDLKM-DKMDGLQLLAEARRLSPATRVMLVTG 197
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESgPDIDLLVTDVIMpGGMNGSQLAEEARRRRPDLKVLLTSG 80
                         90       100
                 ....*....|....*....|....
gi 506340081 198 FATVdtAVEAMRQGA-VYYLAKPV 220
Cdd:cd18161   81 YAEN--AIEGGDLAPgVDVLSKPF 102
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
119-225 7.29e-14

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: 68.18  E-value: 7.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:cd17619    2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSEVGIILVTGRD 81
                         90       100
                 ....*....|....*....|....*..
gi 506340081 199 ATVDTAVeAMRQGAVYYLAKPVNLDEL 225
Cdd:cd17619   82 DEVDRIV-GLEIGADDYVTKPFNPREL 107
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
119-225 1.04e-13

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: 67.93  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRR-SEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTG 197
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQhPDIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIGI 81
                         90       100       110
                 ....*....|....*....|....*....|
gi 506340081 198 FATVDTAVEA--MRQGAVYYLAKPVNLDEL 225
Cdd:cd17544   82 SASGDNALSArfIKAGANDFLTKPFLPEEF 111
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
120-219 3.26e-13

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 65.99  E-value: 3.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                         90       100
                 ....*....|....*....|
gi 506340081 200 TVDTAVEAMRQGAVYYLAKP 219
Cdd:cd19928   81 TLMTAVKAAERGAFEYLPKP 100
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
120-229 3.41e-13

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: 66.28  E-value: 3.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRG-AANGLEALAEVRRSEFDLIVTDLKM-DKMDGLQLLAEARRLSPaTRVMLVTG 197
Cdd:cd17534    3 ILIVEDEAIIALDLKEILESLGYEVVGiADSGEEAIELAEENKPDLILMDINLkGDMDGIEAAREIREKFD-IPVIFLTA 81
                         90       100       110
                 ....*....|....*....|....*....|..
gi 506340081 198 FATVDTAVEAMRQGAVYYLAKPVNLDELRATV 229
Cdd:cd17534   82 YSDEETLERAKETNPYGYLVKPFNERELKAAI 113
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
119-171 8.77e-13

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: 63.36  E-value: 8.77e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 506340081   119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKM 171
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMM 54
orf27 CHL00148
Ycf27; Reviewed
119-234 1.45e-12

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 67.82  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLvTGF 198
Cdd:CHL00148   8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKESDVPIIML-TAL 86
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 506340081 199 ATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAK 234
Cdd:CHL00148  87 GDVSDRITGLELGADDYVVKPFSPKELEARIRSVLR 122
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
120-219 1.58e-12

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: 64.11  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSpATRVMLVTGFA 199
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWS-AVPVIVLSARD 79
                         90       100
                 ....*....|....*....|
gi 506340081 200 TVDTAVEAMRQGAVYYLAKP 219
Cdd:cd17620   80 EESDKIAALDAGADDYLTKP 99
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
118-232 2.01e-12

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: 64.10  E-value: 2.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 118 FHVLVVDDEDIARANLEHVLRK-EGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVT 196
Cdd:cd17593    1 MKVLICDDSSMARKQLARALPAdWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVS 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 506340081 197 GfatvDTAVEAMRQ----GAVYYLAKPVNLDELRATVAAL 232
Cdd:cd17593   81 G----DVQPEAKERvlelGALAFLKKPFDPEKLAQLLEEL 116
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
120-231 2.14e-12

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: 63.98  E-value: 2.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSNVPIIMLTAKDS 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 506340081 200 TVDTaVEAMRQGAVYYLAKPVNLDELRATVAA 231
Cdd:cd17614   81 EVDK-VLGLELGADDYVTKPFSNRELLARVKA 111
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
120-221 2.28e-12

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: 64.27  E-value: 2.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLlaeARRL--SPATR---VML 194
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYEL---CRKIksDPDLKdipVIL 77
                         90       100
                 ....*....|....*....|....*..
gi 506340081 195 VTGFATVDTAVEAMRQGAVYYLAKPVN 221
Cdd:cd17598   78 LTTLSDPRDVIRGLECGADNFITKPYD 104
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
108-233 2.64e-12

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 70.39  E-value: 2.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 108 ASRALRAAPDFHVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLS 187
Cdd:PRK10841 792 TDKAVSDNDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLG 871
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 506340081 188 PATRVMLVTGFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALA 233
Cdd:PRK10841 872 LTLPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVLKQTLTVYA 917
PRK10766 PRK10766
two-component system response regulator TorR;
117-225 2.92e-12

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 66.60  E-value: 2.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 117 DFHVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATrVMLVT 196
Cdd:PRK10766   2 SYHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRSTVG-IILVT 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 506340081 197 GFA-TVDTAVeAMRQGAVYYLAKPVNLDEL 225
Cdd:PRK10766  81 GRTdSIDRIV-GLEMGADDYVTKPLELREL 109
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
120-451 5.67e-12

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 68.36  E-value: 5.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVA-ALAKEK-------------------TAPA-----------SFRSPVLC 248
Cdd:PRK10923  86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVErAISHYQeqqqprniqvngpttdiigEAPAmqdvfriigrlSRSSISVL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 249 FSGPPGTGKTSVGQAIAEALGRR---FHRISLAGL-RD--EAELRGHRRtyvGALPGRVLQSYARLGVAN-PVFMLDEId 321
Cdd:PRK10923 166 INGESGTGKELVAHALHRHSPRAkapFIALNMAAIpKDliESELFGHEK---GAFTGANTIRQGRFEQADgGTLFLDEI- 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 322 kigkdfrGD-PAAVFLEMLDPEQNSQF--VDNYleAPFDLSRTLFIATANDLAEL--SGPLRD----RLEVVPFRGYTTR 392
Cdd:PRK10923 242 -------GDmPLDVQTRLLRVLADGQFyrVGGY--APVKVDVRIIAATHQNLEQRvqEGKFREdlfhRLNVIRVHLPPLR 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506340081 393 EKV----RIAgEHLLPRQLREHG----LTHPfptVTEEALrqvvtghTREAGVRNLdRELGRICRKL 451
Cdd:PRK10923 313 ERRedipRLA-RHFLQVAARELGveakLLHP---ETEAAL-------TRLAWPGNV-RQLENTCRWL 367
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
119-232 6.11e-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: 63.20  E-value: 6.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEG--YKVRGAANGLEALAEVRR-SEF------DLIVTDLKMDKMDGLQLLAEARRlSPA 189
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDFLRGeGEYadaprpDLILLDLNMPRMDGFEVLREIKA-DPD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 506340081 190 TR----VMLVTGFATVDtAVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:cd17557   80 LRripvVVLTTSDAEED-IERAYELGANSYIVKPVDFEEFVEAIRSL 125
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
120-219 6.82e-12

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: 62.40  E-value: 6.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEAR-----RLSPatrVML 194
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRknadfDTIP---VIF 77
                         90       100
                 ....*....|....*....|....*
gi 506340081 195 VTGFATVDTAVEAMRQGAVYYLAKP 219
Cdd:cd19927   78 LTAKGMTSDRIKGYNAGCDGYLSKP 102
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
120-232 7.96e-12

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: 62.32  E-value: 7.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQVPVLMLTARGD 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 200 TVDTAVeAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:cd17623   81 DIDRIL-GLELGADDYLPKPFNPRELVARIRAI 112
PRK10610 PRK10610
chemotaxis protein CheY;
114-219 9.59e-12

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 62.68  E-value: 9.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 114 AAPDFHVLVVDDEDIARANLEHVLRKEGY-KVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATR- 191
Cdd:PRK10610   2 ADKELKFLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSAl 81
                         90       100
                 ....*....|....*....|....*....
gi 506340081 192 -VMLVTGFATVDTAVEAMRQGAVYYLAKP 219
Cdd:PRK10610  82 pVLMVTAEAKKENIIAAAQAGASGYVVKP 110
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
120-226 1.35e-11

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 61.89  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGY-KVRGAANGLEALAEVRRSEFDLIVTDLKMDK-MDGLQLLAEARR---LSPATRVML 194
Cdd:cd17589    1 FLIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELRHkklISPSTVFIM 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 506340081 195 VTG---FATVDTAVEAMRQGavyYLAKPVNLDELR 226
Cdd:cd17589   81 VTGessRAMVLSALELEPDD---YLLKPFTVSELR 112
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
120-231 1.40e-11

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: 61.72  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17626    3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAESGVPIVMLTAKSD 82
                         90       100       110
                 ....*....|....*....|....*....|..
gi 506340081 200 TVDTaVEAMRQGAVYYLAKPVNLDELRATVAA 231
Cdd:cd17626   83 TVDV-VLGLESGADDYVAKPFKPKELVARIRA 113
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
120-232 1.52e-11

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 61.66  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKPFHKDELVARIHAI 113
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
543-648 2.24e-11

Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 65.60  E-value: 2.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 543 RSRAGeLGVDPGLFATQDVHVHIPAGSIpkEGSSAGLTVAVALASLFSGRPLR--PDVAMTGEITLTGNVLPVGGIREKI 620
Cdd:COG3480  212 DGRAG-IGISLVTKVDFPFDVDIDLGDI--GGPSAGLMFALGIYDQLTPGDLTggKKIAGTGTIDADGTVGPIGGIDQKV 288
                         90       100
                 ....*....|....*....|....*...
gi 506340081 621 LAAARAGMREVLVPEANRPEVAAMAGED 648
Cdd:COG3480  289 VAARRAGATIFLAPASNCAEAVGTIPTG 316
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
120-219 2.75e-11

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: 60.29  E-value: 2.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSNVPVIMVTAKDS 80
                         90       100
                 ....*....|....*....|
gi 506340081 200 TVDTAVeAMRQGAVYYLAKP 219
Cdd:cd17621   81 EIDKVV-GLELGADDYVTKP 99
PRK11697 PRK11697
two-component system response regulator BtsR;
120-237 3.53e-11

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 63.71  E-value: 3.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEG-YKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAearRLSPAT--RVMLV 195
Cdd:PRK11697   4 VLIVDDEPLAREELRELLQEEGdIEIVGeCSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVG---MLDPEHmpYIVFV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 506340081 196 TGFAtvDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEKT 237
Cdd:PRK11697  81 TAFD--EYAIKAFEEHAFDYLLKPIDPARLAKTLARLRQERS 120
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
119-232 3.67e-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: 60.64  E-value: 3.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDED----IARANLEHVlrkEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRlSPATR--- 191
Cdd:cd17552    3 RILVIDDEEdireVVQACLEKL---AGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQA-NPETQsip 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 506340081 192 VMLVTGFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:cd17552   79 VILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKL 119
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
61-409 3.70e-11

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 65.32  E-value: 3.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  61 LAYLDFLLGLPWAAVTPDRLDLAQAEAVLDARHHGLGQIKDRVLEYLASRALRAAPDFHVLVVDDEDIARANLEH--VLR 138
Cdd:COG0464    5 LALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLalLAA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 139 KEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFATVDTAVEAMRQGAVYYLAK 218
Cdd:COG0464   85 LLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 219 pvNLDELRATVAALAKEKTAPASFRSPV---LCFSGPPGTGKTSVGQAIAEALGRRFHRISLAGLRDEaelrghrrtYVG 295
Cdd:COG0464  165 --VKEELRELVALPLKRPELREEYGLPPprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK---------YVG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 296 ALPGRVLQSYAR-LGVANPVFMLDEIDKIGKDfRGDPAAVFLEMldpEQNS--QFVDNYleapfdLSRTLFIATANDLAE 372
Cdd:COG0464  234 ETEKNLREVFDKaRGLAPCVLFIDEADALAGK-RGEVGDGVGRR---VVNTllTEMEEL------RSDVVVIAATNRPDL 303
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 506340081 373 LSGPLRDRL-EVVPFRGYTTREKVRIAGEHLLPRQLRE 409
Cdd:COG0464  304 LDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLDE 341
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
120-229 4.29e-11

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: 60.36  E-value: 4.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEG--YKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTG 197
Cdd:cd19930    1 VLIAEDQEMVRGALAALLELEDdlEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 506340081 198 FATVDTAVEAMRQGAVYYLAKPVNLDELRATV 229
Cdd:cd19930   81 FGRPGYFRRALAAGVDGYVLKDRPIEELADAI 112
PRK13557 PRK13557
histidine kinase; Provisional
108-225 4.70e-11

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 65.85  E-value: 4.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 108 ASRALRAAPDFHVLVVDDE----DIARAnlehVLRKEGYKVRGAANGLEALAEVRRS-EFDLIVTDLKM-DKMDGLQLLA 181
Cdd:PRK13557 406 KARAIDRGGTETILIVDDRpdvaELARM----ILEDFGYRTLVASNGREALEILDSHpEVDLLFTDLIMpGGMNGVMLAR 481
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 506340081 182 EARRLSPATRVMLVTGFAtvDTAVEAMRQGAVYY--LAKPVNLDEL 225
Cdd:PRK13557 482 EARRRQPKIKVLLTTGYA--EASIERTDAGGSEFdiLNKPYRRAEL 525
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
247-373 9.67e-11

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 60.76  E-value: 9.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 247 LCFSGPPGTGKTSVGQAIAEALGRRFHRISLAGLRDEAelrghrRTYVGALPGRVLQSYARLgvANPVFMLDEIDKIGKD 326
Cdd:cd19481   29 ILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNLRKIFERARRL--APCILFIDEIDAIGRK 100
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 506340081 327 fRGDPA---------AVFLEMLDPEQNsqfvdnyleapfdLSRTLFIATANDLAEL 373
Cdd:cd19481  101 -RDSSGesgelrrvlNQLLTELDGVNS-------------RSKVLVIAATNRPDLL 142
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
119-231 1.35e-10

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: 59.00  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSpATRVMLVTGF 198
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARS-DVPIIIISGD 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 506340081 199 ATVDTA-VEAMRQGAVYYLAKPVNLDELRATVAA 231
Cdd:cd17594   80 RRDEIDrVVGLELGADDYLAKPFGLRELLARVRA 113
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
119-232 2.57e-10

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


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 58.41  E-value: 2.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRlSPATR---VMLV 195
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKR-DEMTRdipIIML 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 506340081 196 TGFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:cd17618   81 TARGEEEDKVRGLEAGADDYITKPFSPRELVARIKAV 117
ompR PRK09468
osmolarity response regulator; Provisional
119-240 2.89e-10

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 61.14  E-value: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLlaeARRLSPATR----VML 194
Cdd:PRK09468   7 KILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSI---CRRLRSQNNptpiIML 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 506340081 195 VTGFATVDTAVeAMRQGAVYYLAKPVNLDELRATVAALAKEKTAPA 240
Cdd:PRK09468  84 TAKGEEVDRIV-GLEIGADDYLPKPFNPRELLARIRAVLRRQAPEL 128
PRK11517 PRK11517
DNA-binding response regulator HprR;
120-241 2.99e-10

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 60.68  E-value: 2.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLaEARRLSPATRVMLVTGFA 199
Cdd:PRK11517   3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQIL-QTLRTAKQTPVICLTARD 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEKTAPAS 241
Cdd:PRK11517  82 SVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQHHALNS 123
PRK15479 PRK15479
transcriptional regulator TctD;
120-232 3.38e-10

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 60.51  E-value: 3.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARAnLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:PRK15479   4 LLAEDNRELAHW-LEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTARS 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:PRK15479  83 AVADRVKGLNVGADDYLPKPFELEELDARLRAL 115
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
120-219 5.21e-10

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: 56.68  E-value: 5.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKSTLPVIFLTSKDD 80
                         90       100
                 ....*....|....*....|
gi 506340081 200 TVDTaVEAMRQGAVYYLAKP 219
Cdd:cd19936   81 EIDE-VFGLRMGADDYITKP 99
pleD PRK09581
response regulator PleD; Reviewed
120-237 7.59e-10

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 61.46  E-value: 7.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDiarAN---LEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLlaeARRL--SPATR--- 191
Cdd:PRK09581   5 ILVVDDIP---ANvklLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEV---CRRLksDPATThip 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 506340081 192 VMLVTGFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEKT 237
Cdd:PRK09581  79 VVMVTALDDPEDRVRGLEAGADDFLTKPINDVALFARVKSLTRLKM 124
PRK15347 PRK15347
two component system sensor kinase;
119-225 9.45e-10

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 61.97  E-value: 9.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRlSPATR---VMLV 195
Cdd:PRK15347 692 QILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRD-DPNNLdpdCMIV 770
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 506340081 196 TGFATV-----DTAVEAmrqGAVYYLAKPVNLDEL 225
Cdd:PRK15347 771 ALTANAapeeiHRCKKA---GMNHYLTKPVTLAQL 802
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
223-384 9.67e-10

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 57.54  E-value: 9.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 223 DELRATVAALAKEKTAPAsfrspvLCFSGPPGTGKTSVGQAIAEAL---GRRFHRISLAGLRDEAELRGHRRTYvgalPG 299
Cdd:cd00009    4 EEAIEALREALELPPPKN------LLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHF----LV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 300 RVLQSYARLGvANPVFMLDEIDKIGKDFRGDpaavFLEMLDPEqnsqfvdNYLEAPFDLSRTLFIATANDLAELSGPLRD 379
Cdd:cd00009   74 RLLFELAEKA-KPGVLFIDEIDSLSRGAQNA----LLRVLETL-------NDLRIDRENVRVIGATNRPLLGDLDRALYD 141

                 ....*
gi 506340081 380 RLEVV 384
Cdd:cd00009  142 RLDIR 146
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
120-219 2.16e-09

phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues.


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 55.07  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLS--PATRVMLVTG 197
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSalKDTPIIMLTG 80
                         90       100
                 ....*....|....*....|..
gi 506340081 198 FATVDTAVEAMRQGAVYYLAKP 219
Cdd:cd17602   81 KDGLVDRIRAKMAGASGYLTKP 102
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
119-188 4.07e-09

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: 55.28  E-value: 4.07e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506340081 119 HVLVVDDEDIARANLEHVLRKE-GYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEArrLSP 188
Cdd:COG2197    3 RVLIVDDHPLVREGLRALLEAEpDIEVVGeAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL--LTP 72
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
120-219 8.20e-09

phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase output domain; This family is composed of uncharacterized fusion proteins containing a REC domain and a thioredoxin reductase domain. Thioredoxin reductase catalyzes the reduction of thioredoxin and is thus a central component in the thioredoxin system. Fusion proteins containing REC and thioredoxin reductase domains could play an important role in the environmental regulation of the cellular dithiol-disulfide ratio. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 54.26  E-value: 8.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDE-DIARANLEHVLRKEG--YKVRGAANG---LEALAEVRR--SEFDLIVTDLKMDKMDGLQLLAEARRLSPATR 191
Cdd:cd17595    3 ILTVDDDpQVLRAVARDLRRQYGkdYRVLRADSGaeaLDALKELKLrgEAVALFLVDQRMPEMDGVEFLEKAMELFPEAK 82
                         90       100
                 ....*....|....*....|....*....
gi 506340081 192 VMLVTGFATVDTAVEAMRQGAV-YYLAKP 219
Cdd:cd17595   83 RVLLTAYADTDAAIRAINDVQLdYYLLKP 111
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
119-232 1.14e-08

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 53.54  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDE-DIARAnLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTG 197
Cdd:cd19938    1 RILIVEDEpKLAQL-LIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFSDVPIIMVTAR 79
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 506340081 198 FATVDTAVeAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:cd19938   80 VEEIDRLL-GLELGADDYICKPYSPREVVARVKAI 113
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
104-232 1.54e-08

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 58.21  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  104 LEYLASRALRAAPDFHVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEA 183
Cdd:PRK09959  945 VEAKAEQPITLPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKL 1024
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 506340081  184 RRLSPATRVMLVTGFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:PRK09959 1025 REQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
ChlI pfam13541
Subunit ChlI of Mg-chelatase;
566-637 2.11e-08

Subunit ChlI of Mg-chelatase;


Pssm-ID: 433293 [Multi-domain]  Cd Length: 121  Bit Score: 52.84  E-value: 2.11e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506340081  566 PAgSIPKEGSSAGLTVAVALASLFSGRPLRPDVAMTGEITLTGNVLPVGGIREKILAAARAGMREVLVPEAN 637
Cdd:pfam13541  51 PA-DLKKEGSSFDLPIAIGILAAQGQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
120-219 2.91e-08

pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response regulators (PRRs), also called APRRs, comprise a core group of clock components that controls the pace of the central oscillator of the circadian clock, an endogenous time-keeping mechanism that enables organisms to adapt to external daily cycles. The coordinated sequential expression of PRR9 (APRR9), PRR7 (APRR7), PRR5 (APRR5), PRR3 (APRR3), and PRR1 (APRR1) results in circadian waves that may be at the basis of the endogenous circadian clock. PRRs contain an N-terminal pseudo receiver (psREC) domain that resembles the receiver domain of a two-component response regulator, but lacks an aspartate residue that accepts a phosphoryl group from the sensor kinase, and a CCT motif at the C-terminus that contains a putative nuclear localization signal. The psREC domain is involved in protein-protein interactions.


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 52.02  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEA--LAEVRRSEFDLIVTDLKMDKMDGLQLLA-----EARRLSPatrV 192
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAwdVLEDEQNEIDLILTEVDLPVSSGFKLLSyimrhKICKNIP---V 77
                         90       100
                 ....*....|....*....|....*..
gi 506340081 193 MLVTGFATVDTAVEAMRQGAVYYLAKP 219
Cdd:cd17582   78 IMMSSQDSVGVVFKCLSKGAADYLVKP 104
PRK10693 PRK10693
two-component system response regulator RssB;
147-247 3.30e-08

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 55.77  E-value: 3.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 147 AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTgfATVDTA--VEAMRQGAVYYLAKPV-NLD 223
Cdd:PRK10693   3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVIS--ATENMAdiAKALRLGVQDVLLKPVkDLN 80
                         90       100
                 ....*....|....*....|....
gi 506340081 224 ELRATVAALakekTAPASFRSPVL 247
Cdd:PRK10693  81 RLREMVFAC----LYPSMFNSRVE 100
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
120-227 3.79e-08

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: 52.02  E-value: 3.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRR--SEFDLIVTDLKMDKMDGLQLLAEARRLSPAT-RVMLVT 196
Cdd:cd19933    3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASaeHSFQLVLLDLCMPEMDGFEVALRIRKLFGRReRPLIVA 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 197 GFATVDTAVEA--MRQGAVYYLAKPVNLDELRA 227
Cdd:cd19933   83 LTANTDDSTREkcLSLGMNGVITKPVSLHALGD 115
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
120-219 4.03e-08

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: 51.84  E-value: 4.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDD-EDIARANLEHVLRKEGYKVRGAA-NGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEAR--RLSPATRVMLV 195
Cdd:cd17561    4 VLIADDnREFVQLLEEYLNSQPDMEVVGVAhNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRrmRLEKRPKIIML 83
                         90       100
                 ....*....|....*....|....
gi 506340081 196 TGFATVDTAVEAMRQGAVYYLAKP 219
Cdd:cd17561   84 TAFGQEDITQRAVELGASYYILKP 107
PRK10430 PRK10430
two-component system response regulator DcuR;
120-219 5.12e-08

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 54.34  E-value: 5.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDED-IARANLEHVLRKEGYKVRGAANGLEALAEV---RRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLV 195
Cdd:PRK10430   4 VLIVDDDAmVAELNRRYVAQIPGFQCCGTASTLEQAKEIifnSDTPIDLILLDIYMQQENGLDLLPVLHEAGCKSDVIVI 83
                         90       100
                 ....*....|....*....|....
gi 506340081 196 TGFATVDTAVEAMRQGAVYYLAKP 219
Cdd:PRK10430  84 SSAADAATIKDSLHYGVVDYLIKP 107
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
120-232 1.07e-07

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 53.27  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSeFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDS-IDLLLLDVMMPKKNGIDTLKELRQTHQTPVIMLTARGS 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 200 TVDTaVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:PRK10955  83 ELDR-VLGLELGADDYLPKPFNDRELVARIRAI 114
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
120-236 1.16e-07

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 52.72  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKE-GYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTG 197
Cdd:PRK10651   9 ILLIDDHPMLRTGVKQLISMApDITVVGeASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFSV 88
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 506340081 198 FATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEK 236
Cdd:PRK10651  89 SNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQAAAGE 127
PRK11173 PRK11173
two-component response regulator; Provisional
119-227 1.33e-07

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 53.10  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLqLLAEARRLSPATRVMLVTGf 198
Cdd:PRK11173   5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGL-LLARELREQANVALMFLTG- 82
                         90       100       110
                 ....*....|....*....|....*....|....
gi 506340081 199 atVDTAVE---AMRQGAVYYLAKPVNLDEL--RA 227
Cdd:PRK11173  83 --RDNEVDkilGLEIGADDYITKPFNPRELtiRA 114
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
120-251 1.49e-07

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 52.88  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSpATRVMLVTGFA 199
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWS-AIPVIVLSARS 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDELRATV-AALAKEKTAPASfrSPVLCFSG 251
Cdd:PRK10529  83 EESDKIAALDAGADDYLSKPFGIGELQARLrVALRRHSATPAP--DPLVKFSD 133
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
120-239 1.60e-07

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 52.62  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:PRK09836   3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTALG 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEKTAP 239
Cdd:PRK09836  83 TIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGAAV 122
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
119-246 2.24e-07

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 52.27  E-value: 2.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTG- 197
Cdd:PRK11083   5 TILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTAr 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 506340081 198 FATVDTAVeAMRQGAVYYLAKPVNLDELRATVAALAKeKTAPASFRSPV 246
Cdd:PRK11083  85 SDEVDRLV-GLEIGADDYVAKPFSPREVAARVRTILR-RVKKFAAPSPV 131
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
249-397 2.54e-07

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 52.19  E-value: 2.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 249 FSGPPGTGKTSVGQAIAEALGRRFHRISLAGLRDEaelrghrrtYVGALPGRVLQSYARLGVANPVFMLDEIDKIGKDfR 328
Cdd:COG1223   40 FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS---------YLGETARNLRKLFDFARRAPCVIFFDEFDAIAKD-R 109
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506340081 329 GDPAAV---------FLEMLDPEQnsqfvdnyleapfdlSRTLFIATANDLAELSGPLRDRL-EVVPFRGYTTREKVRI 397
Cdd:COG1223  110 GDQNDVgevkrvvnaLLQELDGLP---------------SGSVVIAATNHPELLDSALWRRFdEVIEFPLPDKEERKEI 173
PRK15369 PRK15369
two component system response regulator;
120-237 2.58e-07

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 51.62  E-value: 2.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRK-EGYKVRGAA-NGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTG 197
Cdd:PRK15369   6 ILLVDDHELIINGIKNMLAPyPRYKIVGQVdNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMNILVLTA 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 506340081 198 FATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEKT 237
Cdd:PRK15369  86 RQEEHMASRTLAAGALGYVLKKSPQQILLAAIQTVAVGKR 125
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
120-232 2.95e-07

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 49.29  E-value: 2.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHvLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd19939    3 LIVEDELELARLTRDY-LIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHSHVPILMLTARTE 81
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 200 TVDTaVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:cd19939   82 EMDR-VLGLEMGADDYLCKPFSPRELLARVRAL 113
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
120-225 2.98e-07

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


Pssm-ID: 381149 [Multi-domain]  Cd Length: 110  Bit Score: 49.40  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEdiarANLEHV----LRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLV 195
Cdd:cd19922    1 ILLLEKE----RNLAHFlsleLQKEGYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAEKLSRIKPASVIIVL 76
                         90       100       110
                 ....*....|....*....|....*....|
gi 506340081 196 TGFATVDTAVEAMRQGAVYYLAKPVNLDEL 225
Cdd:cd19922   77 DHWEDLQEELEEVQRFAVSYVVKPVLISNL 106
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
247-381 3.74e-07

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 49.60  E-value: 3.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  247 LCFSGPPGTGKTSVGQAIAEAL-GRRFHRISL-AGLRdEAELRGHRRtYVGALPGRVLQSYARLGVANPVFMLDEIDKIG 324
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAALsNRPVFYVQLtRDTT-EEDLFGRRN-IDPGGASWVDGPLVRAAREGEIAVLDEINRAN 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506340081  325 KDfrgdpAAVFLEMLDPEQNSQFVDNYLEAPFDLSRTLFIATANDL----AELSGPLRDRL 381
Cdd:pfam07728  80 PD-----VLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPLdrglNELSPALRSRF 135
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
120-234 4.15e-07

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 52.46  E-value: 4.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKE-GYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMlvtg 197
Cdd:PRK00742   6 VLVVDDSAFMRRLISEILNSDpDIEVVGtAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRPTPVVM---- 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 506340081 198 FATV-----DTAVEAMRQGAVYYLAKPV-----NLD----ELRATVAALAK 234
Cdd:PRK00742  82 VSSLtergaEITLRALELGAVDFVTKPFlgislGMDeykeELAEKVRAAAR 132
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
120-225 5.23e-07

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: 48.88  E-value: 5.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKE-GYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTG 197
Cdd:cd19931    1 VLLIDDHPLLRKGIKQLIELDpDFTVVGeASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTV 80
                         90       100
                 ....*....|....*....|....*...
gi 506340081 198 FATVDTAVEAMRQGAVYYLAKPVNLDEL 225
Cdd:cd19931   81 SDAEDDVVTALRAGADGYLLKDMEPEDL 108
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
115-234 6.51e-07

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 50.62  E-value: 6.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 115 APDFHVLVVDDEDIARANLEHVLRKE-GYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRV 192
Cdd:PRK10403   4 ATPFQVLIVDDHPLMRRGVRQLLELDpGFEVVAeAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQI 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 506340081 193 MLVTGFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAK 234
Cdd:PRK10403  84 IILTVSDASSDVFALIDAGADGYLLKDSDPEVLLEAIRAGAK 125
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
120-233 9.17e-07

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


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 48.21  E-value: 9.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYK-VRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGF 198
Cdd:cd17530    3 VLVLDDDPFQCMMAATILEDLGPGnVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMSGL 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 506340081 199 -----ATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALA 233
Cdd:cd17530   83 dggilESAETLAGANGLNLLGTLSKPFSPEELTELLTKYT 122
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
566-664 1.00e-06

Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 51.96  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 566 PAgSIPKEGSSAGLTVAVAL---ASLFSGRPLRpDVAMTGEITLTGNVLPVGGIREKILAAARAGMREVLVPEANRPEvA 642
Cdd:COG0606   70 PA-DLPKEGSRFDLPIALGIlaaSGQIPAEALE-DYVFLGELSLDGSLRPVRGVLPAALAAREAGIRRLIVPAANAAE-A 146
                         90       100
                 ....*....|....*....|...
gi 506340081 643 AMAGEdsPEVL-VRHVATVFAAL 664
Cdd:COG0606  147 ALVPG--IEVYgASSLLEVVAFL 167
PRK10816 PRK10816
two-component system response regulator PhoP;
120-241 1.01e-06

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 50.12  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARE 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEKTAPAS 241
Cdd:PRK10816  83 SWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMRRNSGLAS 124
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
122-220 2.86e-06

phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar proteins; Bacillus subtilis GlnL is part of the GlnK-GlnL (formerly YcbA-YcbB) two-component system that positively regulates the expression of the glsA-glnT (formerly ybgJ-ybgH) operon in response to glutamine. It contains a REC domain and a DNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 46.11  E-value: 2.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 122 VVDDEDIARANLEHVLRKE--GYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17565    3 IVDDDKNIIKILSDIIEDDdlGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQVS 82
                         90       100
                 ....*....|....*....|.
gi 506340081 200 TVDTAVEAMRQGAVYYLAKPV 220
Cdd:cd17565   83 DKEMIGKAYQAGIEFFINKPI 103
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
120-222 3.33e-06

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 46.59  E-value: 3.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEAL-----------AEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSP 188
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALeflgledeedsSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 506340081 189 ATRVMLVTGFA-TVDTAV-EAMRQGAVYYLAKPVNL 222
Cdd:cd17581   81 LKEIPVVIMSSeNIPTRIsRCLEEGAEDFLLKPVKL 116
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
249-368 3.41e-06

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 47.58  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  249 FSGPPGTGKTSVGQAIAEALG---RRFHRISLAGLRDE---AELRGHRRTYVGALPGRVLQSYARLGVANPVFmLDEIDK 322
Cdd:pfam07724   8 FLGPTGVGKTELAKALAELLFgdeRALIRIDMSEYMEEhsvSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL-IDEIEK 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 506340081  323 IGKD-FRgdpaaVFLEMLDpeqNSQFVDNYlEAPFDLSRTLFIATAN 368
Cdd:pfam07724  87 AHPGvQN-----DLLQILE---GGTLTDKQ-GRTVDFKNTLFIMTGN 124
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
120-229 4.95e-06

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: 45.88  E-value: 4.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAAN---GlEALAEVRrsEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVT 196
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESlkdG-EYYIDIR--NYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLS 77
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 197 GFATVDTAVEAMRQGAVYYLAKPVNLDELRATV 229
Cdd:cd17573   78 DNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
LonB COG1067
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ...
573-647 6.52e-06

Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440686 [Multi-domain]  Cd Length: 742  Bit Score: 49.56  E-value: 6.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 573 EGSSAGLTVAVALASLFSGRPLRPDVAMTGEITLTGNVLPVGGIREKI-----LAAAR--AGMREVLVPEAN------RP 639
Cdd:COG1067  592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIegffdVCKARglTGKQGVIIPAANvknlmlRD 671
                         90
                 ....*....|
gi 506340081 640 EV--AAMAGE 647
Cdd:COG1067  672 EVveAVKAGQ 681
PLN03029 PLN03029
type-a response regulator protein; Provisional
118-237 1.10e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 46.95  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 118 FHVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEV--------------------RRSEFDLIVTDLKMDKMDGL 177
Cdd:PLN03029   9 FHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLglheddrsnpdtpsvspnshQEVEVNLIITDYCMPGMTGY 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506340081 178 QLLAEARRlSPATR---VMLVTGFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEKT 237
Cdd:PLN03029  89 DLLKKIKE-SSSLRnipVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDLNRLKPHMMKTKS 150
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
64-339 1.22e-05

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 48.23  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  64 LDFLLGLPWAAVTPDRLDLAQAEAVLDARHHGLGQIKDRVLEYLASRALRAAPDFHVLVVDDEDIARANLEHVLRKEGYK 143
Cdd:COG1401   36 LRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 144 VRGAANGLEALAEvrRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFATVDTAVEAMRQGAVYYLAKPVNLD 223
Cdd:COG1401  116 VGLLLELAERSDA--LEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLE 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 224 ELRATVAALAKEKTAP-------ASFRSPVLCFSGPPGTGKTSVGQAIAEALG----RRFHRISL-AGLRDEAELRGHR- 290
Cdd:COG1401  194 SEDDYLKDLLREKFEEtleaflaALKTKKNVILAGPPGTGKTYLARRLAEALGgednGRIEFVQFhPSWSYEDFLLGYRp 273
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 506340081 291 RTYVGAL---PGRVLQSY--ARLGVANPVFM-LDEIDkigkdfRGDPAAVFLEML 339
Cdd:COG1401  274 SLDEGKYeptPGIFLRFClkAEKNPDKPYVLiIDEIN------RANVEKYFGELL 322
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
251-292 1.40e-05

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 48.13  E-value: 1.40e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 506340081 251 GPPGTGKTSVGQAIAEALGRRFHRIS--LAG---LR---DEAE--LRGHRRT 292
Cdd:COG2256   56 GPPGTGKTTLARLIANATDAEFVALSavTSGvkdIReviEEARerRAYGRRT 107
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
116-241 1.50e-05

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 48.40  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 116 PDFHVLVVddEDI------ARAnlehVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPA 189
Cdd:PRK11091 524 PALNILLV--EDIelnvivARS----VLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPR 597
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 506340081 190 TRVM-LVTGFATV----DTAVEAMRQGAvyyLAKPVNLDELRATVAALAKEKTAPAS 241
Cdd:PRK11091 598 EDLPpLVALTANVlkdkKEYLDAGMDDV---LSKPLSVPALTAMIKKFWDTQDDEES 651
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
121-232 1.79e-05

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: 44.19  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 121 LVVDDEDIaRANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFAT 200
Cdd:cd18159    3 IVEDDETI-ASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISNVPIIFISSRDDN 81
                         90       100       110
                 ....*....|....*....|....*....|..
gi 506340081 201 VDTaVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:cd18159   82 MDQ-VMAINMGGDDYITKPFDLDVLLAKIKAI 112
pleD PRK09581
response regulator PleD; Reviewed
119-229 1.80e-05

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 47.59  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEgYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLsPATR---VMLV 195
Cdd:PRK09581 157 RILLVDDDVSQAERIANILKEE-FRVVVVSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSK-ERTRyvpILLL 234
                         90       100       110
                 ....*....|....*....|....*....|....
gi 506340081 196 TGFATVDTAVEAMRQGAVYYLAKPVNLDELRATV 229
Cdd:PRK09581 235 VDEDDDPRLVKALELGVNDYLMRPIDKNELLARV 268
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
120-234 2.88e-05

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 45.83  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:PRK10710  13 ILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFSDIPIVMVTAKIE 92
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 506340081 200 TVDTAVeAMRQGAVYYLAKPVNLDELRATVAALAK 234
Cdd:PRK10710  93 EIDRLL-GLEIGADDYICKPYSPREVVARVKTILR 126
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
120-229 3.04e-05

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-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 the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 43.84  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEgYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSpATRVMLVTGFA 199
Cdd:cd17539    1 VLLVDDRPSSAERIAAMLSSE-HEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLE-RTRQLPILAVA 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 200 TVDTA---VEAMRQGAVYYLAKPVNLDELRATV 229
Cdd:cd17539   79 DPGDRgrlIRALEIGVNDYLVRPIDPNELLARV 111
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
120-253 3.25e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 46.41  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVL-RKEGYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPaTRVMLVTG 197
Cdd:PRK12555   3 IGIVNDSPLAVEALRRALaRDPDHEVVWvATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERP-CPILIVTS 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506340081 198 F--ATVDTAVEAMRQGAVYYLAKPV---------NLDELRATVAALAKEKTAPASFRSPVLCFSGPP 253
Cdd:PRK12555  82 LteRNASRVFEAMGAGALDAVDTPTlgigagleeYAAELLAKIDQIGRLLGRRLAPAAAPAAASAAP 148
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
225-386 3.56e-05

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 44.86  E-value: 3.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 225 LRATVAALAKEKTAPASFrspvlCFSGPPGTGKTSVGQAIAEAL---GRRFHRISLaGLRDEAE----LRGHRRTYVGAL 297
Cdd:cd19499   27 IRRARAGLSDPNRPIGSF-----LFLGPTGVGKTELAKALAELLfgdEDNLIRIDM-SEYMEKHsvsrLIGAPPGYVGYT 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 298 PGRVLQSYARLgvaNP--VFMLDEIDKIGKDFRGdpaaVFLEMLDpeqNSQFVDNYlEAPFDLSRTLFIATANDLAElsg 375
Cdd:cd19499  101 EGGQLTEAVRR---KPysVVLLDEIEKAHPDVQN----LLLQVLD---DGRLTDSH-GRTVDFKNTIIIMTSNHFRP--- 166
                        170
                 ....*....|.
gi 506340081 376 PLRDRLEVVPF 386
Cdd:cd19499  167 EFLNRIDEIVV 177
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
249-282 3.82e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 46.62  E-value: 3.82e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 506340081 249 FSGPPGTGKTSVGQAIAEALGRRFHRIS--LAGLRD 282
Cdd:PRK13342  41 LWGPPGTGKTTLARIIAGATDAPFEALSavTSGVKD 76
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
243-384 4.85e-05

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.90  E-value: 4.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081   243 RSPVLCFSGPPGTGKTSVGQAIAEALGR---RFHRISLAGLRDEAELRGHRRTYVGALPGRVLQSYARLGVA------NP 313
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPpggGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAlarklkPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506340081   314 VFMLDEIDKIGKDfrgdpaavflEMLDPEQNSQFVDNYLEAPFDLSRTLFIATANDLAELSGPLRDRLEVV 384
Cdd:smart00382  81 VLILDEITSLLDA----------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRR 141
dpiA PRK10046
two-component response regulator DpiA; Provisional
120-244 7.45e-05

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 44.62  E-value: 7.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDED-IARANLEHVLRKEGY-KVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTG 197
Cdd:PRK10046   7 LLIVEDETpLAEMHAEYIRHIPGFsQILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPGDVVFTTA 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 506340081 198 FATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEKTAPASFRS 244
Cdd:PRK10046  87 ASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRFRQRKHMLESIDS 133
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
251-323 1.15e-04

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 43.43  E-value: 1.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506340081 251 GPPGTGKTSVGQAIAEALGRRFHRISLAGLrdEAELRGHRRTYVgalpgRVLQSYARLGVANPVFmLDEIDKI 323
Cdd:cd19522   40 GPPGTGKTLLAKAVATECGTTFFNVSSSTL--TSKYRGESEKLV-----RLLFEMARFYAPTTIF-IDEIDSI 104
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
243-323 1.88e-04

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 43.05  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 243 RSP---VLCFsGPPGTGKTSVGQAIAEALGRRFHRISLAGLRDEAELRGHRRTyvgalpgRVLQSYARLGVANPVFmLDE 319
Cdd:cd19525   52 RGPpkgILLF-GPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMV-------RALFSVARCKQPAVIF-IDE 122

                 ....
gi 506340081 320 IDKI 323
Cdd:cd19525  123 IDSL 126
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
118-226 3.67e-04

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; 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 AgrA-like group of LytTR/AlgR family response regulators are Staphylococcus aureus accessory gene regulator protein A (AgrA) and Streptococcus pneumoniae response regulator ComE, which are members of two-component regulatory systems. AgrA is a global regulator that controls the synthesis of virulence factors and other exoproteins. ComE is part of the ComD-ComE system that is part of a quorum-sensing signaling pathway that controls the development of competence, a physiological state required for genetic transformation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381088 [Multi-domain]  Cd Length: 131  Bit Score: 41.07  E-value: 3.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 118 FHVLVVDDEDIARANLEHV----LRKEGY----KVRGAANGL-EALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSP 188
Cdd:cd17533    1 MNIFILEDDKIQRVRLEEIieniLKIENIeyviELTGKTEELlEKIKERGKNGIYFLDIDIKMEEKNGLEVAQKIRKYDP 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 506340081 189 ATRVMLVTG-----FATVDTAVEAMRqgavyYLAKPVNLDELR 226
Cdd:cd17533   81 YAIIIFVTThsefaPLTFEYKVAALD-----FILKPLKLEEFK 118
PRK13856 PRK13856
two-component response regulator VirG; Provisional
119-251 3.83e-04

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 42.49  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 119 HVLVVDDEDIARANLEHVLRKEGYKVRGAANGlEALAEVRRSE-FDLIVTDLKMDKMDGLQLLaeaRRLSPATRV-MLVT 196
Cdd:PRK13856   3 HVLVIDDDVAMRHLIVEYLTIHAFKVTAVADS-QQFNRVLASEtVDVVVVDLNLGREDGLEIV---RSLATKSDVpIIII 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 506340081 197 GFATVDTA--VEAMRQGAVYYLAKPVNLDELRATV-AALAKEKTAPASFRSPVLCFSG 251
Cdd:PRK13856  79 SGDRLEEAdkVVALELGATDFIAKPFGTREFLARIrVALRVRPNVVRTKDRRSFCFAD 136
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
120-232 4.41e-04

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: 40.44  E-value: 4.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARAnLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFA 199
Cdd:cd17622    4 LLVEDDPKLARL-IADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQGPILLLTALDS 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 200 TVDTaVEAMRQGAVYYLAKPVNLDELRATVAAL 232
Cdd:cd17622   83 DIDH-ILGLELGADDYVVKPVEPAVLLARLRAL 114
PRK09862 PRK09862
ATP-dependent protease;
508-664 4.53e-04

ATP-dependent protease;


Pssm-ID: 182120 [Multi-domain]  Cd Length: 506  Bit Score: 43.43  E-value: 4.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 508 ISVEAIRMEGTGELLLTGsLGEVLRESARtalSLVRSRAGELGVDpglFATQDVHVHIPAGSIPKEGSSAGLTVAVAL-- 585
Cdd:PRK09862  19 ITVEVHISKGLPGLTMVG-LPETTVKEAR---DRVRSAIINSGYE---YPAKKITINLAPADLPKEGGRYDLPIAIALla 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506340081 586 ASLFSGRPLRPDVAMTGEITLTGNVLPVGGIREKILAAARAGmREVLVPEANRPEVAAMAGEDSpeVLVRHVATVFAAL 664
Cdd:PRK09862  92 ASEQLTANKLDEYELVGELALTGALRGVPGAISSATEAIKSG-RKIIVAKDNEDEVGLINGEGC--LIADHLQAVCAFL 167
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
120-229 6.03e-04

phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is a hybrid stress regulator that contains an N-terminal sigma-like (SL) domain and a C-terminal REC domain. Phosphorylation of the REC domain is known to promote binding of the SL domain to an anti-sigma factor. PhyR thus functions as an anti-anti-sigma factor in its phosphorylated state. It is involved in the general stress response. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 39.92  E-value: 6.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRG-AANGLEALAEVRRSEFDLIVTDLKMDkmDGLQLLAEARRLSPATR--VMLVT 196
Cdd:cd17540    3 VLIIEDEPLIAMDLEQIVEDLGHQVVGiARTRDEAVALARRERPDLILADIQLA--DGSSGIDAVNEILTTHDvpVIFVT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 506340081 197 GFAtvDTAVEAMRQGAVYYLAKPVNLDELRATV 229
Cdd:cd17540   81 AYP--ERLLTGERPEPTFLITKPFDPEMVKAAI 111
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
120-224 8.43e-04

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 42.53  E-value: 8.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDiarANL-----------EHVLRkegykvrgAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLS- 187
Cdd:PRK11107 670 VMAVDDNP---ANLkligalleeqvEHVVL--------CDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPh 738
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 506340081 188 -PATRVMLVTGFATVDTAVEAMRQGAVYYLAKPVnlDE 224
Cdd:PRK11107 739 nQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPI--DE 774
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
251-273 8.52e-04

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 40.50  E-value: 8.52e-04
                         10        20
                 ....*....|....*....|...
gi 506340081 251 GPPGTGKTSVGQAIAEALGRRFH 273
Cdd:COG0703    5 GMMGAGKSTVGRLLAKRLGLPFV 27
PRK14084 PRK14084
DNA-binding response regulator;
120-237 9.82e-04

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 41.28  E-value: 9.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGY--KVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMlvtg 197
Cdd:PRK14084   3 ALIVDDEPLARNELTYLLNEIGGfeEINEAENVKETLEALLINQYDIIFLDINLMDESGIELAAKIQKMKEPPAII---- 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 506340081 198 FATV-DT-AVEAMRQGAVYYLAKPVNLDELRATV--AALAKEKT 237
Cdd:PRK14084  79 FATAhDQfAVKAFELNATDYILKPFEQKRIEQAVnkVRATKAKD 122
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
120-234 1.68e-03

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 40.47  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARR--LSPATRVMLVTG 197
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKResMTRDIPVVMLTA 84
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 506340081 198 FATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAK 234
Cdd:PRK10161  85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMR 121
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
120-225 1.95e-03

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 40.24  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 120 VLVVDDEDIARANLEHVLRK--EGYKVRGAANGLEALAEVRRSEFDLIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTG 197
Cdd:PRK09935   6 VIIMDTHPIIRMSIEVLLQKnsELQIVLKTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLFLSS 85
                         90       100
                 ....*....|....*....|....*...
gi 506340081 198 FATVDTAVEAMRQGAVYYLAKPVNLDEL 225
Cdd:PRK09935  86 KSECFYAGRAIQAGANGFVSKCNDQNDI 113
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
203-275 2.36e-03

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 40.54  E-value: 2.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506340081 203 TAVEAMRQGAVYYLAKPvnlDELRATVAALAKEKtapasfrsPVLcFSGPPGTGKTSVGQAIAEALGRRFHRI 275
Cdd:COG0714    2 TEARLRAEIGKVYVGQE---ELIELVLIALLAGG--------HLL-LEGVPGVGKTTLAKALARALGLPFIRI 62
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
249-330 2.74e-03

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 40.37  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081 249 FSGPPGTGKTSVGQAIAEALGRRFHRISLAGLRDEaelrghrrtYVGALPGRV--LQSYARlGVANPVFMLDEIDKIGKD 326
Cdd:COG1222  117 LYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK---------YIGEGARNVreVFELAR-EKAPSIIFIDEIDAIAAR 186

                 ....
gi 506340081 327 fRGD 330
Cdd:COG1222  187 -RTD 189
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
251-272 3.22e-03

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 38.69  E-value: 3.22e-03
                         10        20
                 ....*....|....*....|..
gi 506340081 251 GPPGTGKTSVGQAIAEALGRRF 272
Cdd:cd00464    6 GMMGAGKTTVGRLLAKALGLPF 27
PRK04182 PRK04182
cytidylate kinase; Provisional
250-288 3.84e-03

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 39.02  E-value: 3.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 506340081 250 SGPPGTGKTSVGQAIAEALGRRFhrISlAGL--RDEAELRG 288
Cdd:PRK04182   6 SGPPGSGKTTVARLLAEKLGLKH--VS-AGEifRELAKERG 43
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
4-536 3.92e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 40.63  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081    4 FQKrtEGALPPPPVSDIGQLRARIDSQELPHHAREAANRELERLEKTDPSAAEYGVGLAYLDFLLGLPWAAVTPDRLDLA 83
Cdd:COG3321   868 FQR--EDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLAL 945
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081   84 QAEAVLDARHHGLGQIKDRVLEYLASRALRAAPDFHVLVVDDEDIARANLEHVLRKEGYKVRGAANGLEALAEVRRSEFD 163
Cdd:COG3321   946 AAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALA 1025
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  164 LIVTDLKMDKMDGLQLLAEARRLSPATRVMLVTGFATVDTAVEAMRQGAVYYLAKPVNLDELRATVAALAKEKTAPASFR 243
Cdd:COG3321  1026 ALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAA 1105
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  244 SPVLCFSGppgtgktsVGQAIAEALGRRFHRISLAGLRDEAELRGHRRTYVGALPGRVLQSYARLGVANPVFMLDEIDKI 323
Cdd:COG3321  1106 LLLLALLA--------ALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLAL 1177
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  324 GKDFRGDPAAVFLEMLDPEQNSQFVDNYLEAPFDLSRTLFIATANDLAELSGPLRDRLEVVPFRGYTTREKVRIAGEHLL 403
Cdd:COG3321  1178 ALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLA 1257
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506340081  404 PRQLREHGLTHPFPTVTEEALRQVVTGHTREAGVRNLDRELGRicrklARLRLEQGEGAAPAEVDAALAAALLGPPPYRG 483
Cdd:COG3321  1258 ALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAA-----LLAAAAAAAAAAAAAAAAAALAAALLAAALAA 1332
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 506340081  484 ETAGAAPRLGVATGLVYADYGGEIISVEAIRMEGTGELLLTGSLGEVLRESAR 536
Cdd:COG3321  1333 LAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAV 1385
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
246-288 5.54e-03

cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by TIGR00017.


Pssm-ID: 274012 [Multi-domain]  Cd Length: 171  Bit Score: 38.17  E-value: 5.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 506340081  246 VLCFSGPPGTGKTSVGQAIAEALGRRFhrISlAGL--RDEAELRG 288
Cdd:TIGR02173   2 IITISGPPGSGKTTVAKILAEKLSLKL--IS-AGDifRELAAKMG 43
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
250-284 6.78e-03

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 37.47  E-value: 6.78e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 506340081 250 SGPPGTGKTSVGQAIAEALGrrFHRISLAGLRDEA 284
Cdd:cd02020    5 DGPAGSGKSTVAKLLAKKLG--LPYLDTGGIRTEE 37
aroK PRK00131
shikimate kinase; Reviewed
251-272 7.82e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 37.86  E-value: 7.82e-03
                         10        20
                 ....*....|....*....|..
gi 506340081 251 GPPGTGKTSVGQAIAEALGRRF 272
Cdd:PRK00131  11 GFMGAGKSTIGRLLAKRLGYDF 32
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
240-278 9.97e-03

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 37.15  E-value: 9.97e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 506340081 240 ASFRSPVLCFSGPPGTGKTSVGQAIAEALGRRFHRISLA 278
Cdd:cd17933    8 LVLRNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLA 46
 
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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