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Conserved domains on  [gi|2279496592|ref|WP_256200643|]
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response regulator transcription factor family protein [Verrucomicrobium spinosum]

Protein Classification

response regulator transcription factor family protein( domain architecture ID 13408757)

two-component system response regulator transcription factor family protein; contains a C-terminal DNA-binding domain and may bind DNA upon phosphorylation and function as a transcriptional regulator

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10651 super family cl32550
transcriptional regulator NarL; Provisional
166-369 4.73e-46

transcriptional regulator NarL; Provisional


The actual alignment was detected with superfamily member PRK10651:

Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 156.73  E-value: 4.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 166 MTPPLTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQAR 245
Cdd:PRK10651    3 NQEPATILLIDDHPMLRTGVKQLISMAPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 246 ILVYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAAGGSYLPPELEQRLA---------DLRLCVGISMRERE 316
Cdd:PRK10651   83 IVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQAAAGEMVLSEALTPVLAaslranratTERDVNQLTPRERD 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2279496592 317 ILELIAKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEAIRRGI 369
Cdd:PRK10651  163 ILKLIAQGLPNKMIARRLDITESTVKVHVKHMLKKMKLKSRVEAAVWVHQERI 215
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
2-127 8.01e-24

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


:

Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 98.92  E-value: 8.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592   2 ETRSLVSELRVPSRENADLVAALQAIVDEHPLGCGPVLKLEVSGPMPPLPSRTVHHLRMIAREGVTNALKHARAGCIRLS 81
Cdd:COG4585   107 ELRRLVRGLRPPALDDLGLAAALEELAERLLRAAGIRVELDVDGDPDRLPPEVELALYRIVQEALTNALKHAGATRVTVT 186
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2279496592  82 LGVEGSRLRMTIADDGQGFDAEALHGgqrGHFGCIGIEERCAKFGG 127
Cdd:COG4585   187 LEVDDGELTLTVRDDGVGFDPEAAPG---GGLGLRGMRERAEALGG 229
 
Name Accession Description Interval E-value
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
166-369 4.73e-46

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 156.73  E-value: 4.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 166 MTPPLTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQAR 245
Cdd:PRK10651    3 NQEPATILLIDDHPMLRTGVKQLISMAPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 246 ILVYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAAGGSYLPPELEQRLA---------DLRLCVGISMRERE 316
Cdd:PRK10651   83 IVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQAAAGEMVLSEALTPVLAaslranratTERDVNQLTPRERD 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2279496592 317 ILELIAKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEAIRRGI 369
Cdd:PRK10651  163 ILKLIAQGLPNKMIARRLDITESTVKVHVKHMLKKMKLKSRVEAAVWVHQERI 215
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
172-288 6.37e-41

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: 139.95  E-value: 6.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEPDIEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2279496592 252 FAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAA 288
Cdd:cd17535    81 HDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
169-371 7.54e-38

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: 132.32  E-value: 7.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 169 PLTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAilrahdpqarilv 248
Cdd:COG2197     1 MIRVLIVDDHPLVREGLRALLEAEPDIEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALR------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 249 ystfahddevqmaldagaagylqktasrdELLTAlrrvaaggsylppeleqrladlrlcvgismREREILELIAKGHANK 328
Cdd:COG2197    68 -----------------------------RLLTP------------------------------REREVLRLLAEGLSNK 88
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2279496592 329 QIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEAIRRGIVR 371
Cdd:COG2197    89 EIAERLGISERTVKTHVSNILRKLGVRNRTELVLLALRLGLLD 131
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
172-284 2.02e-27

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: 104.16  E-value: 2.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEG--YVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2279496592 252 FAHDDEVQMALDAGAAGYLQKTASRDELLTALR 284
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
2-127 8.01e-24

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 98.92  E-value: 8.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592   2 ETRSLVSELRVPSRENADLVAALQAIVDEHPLGCGPVLKLEVSGPMPPLPSRTVHHLRMIAREGVTNALKHARAGCIRLS 81
Cdd:COG4585   107 ELRRLVRGLRPPALDDLGLAAALEELAERLLRAAGIRVELDVDGDPDRLPPEVELALYRIVQEALTNALKHAGATRVTVT 186
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2279496592  82 LGVEGSRLRMTIADDGQGFDAEALHGgqrGHFGCIGIEERCAKFGG 127
Cdd:COG4585   187 LEVDDGELTLTVRDDGVGFDPEAAPG---GGLGLRGMRERAEALGG 229
HTH_LUXR smart00421
helix_turn_helix, Lux Regulon; lux regulon (activates the bioluminescence operon
313-364 1.43e-18

helix_turn_helix, Lux Regulon; lux regulon (activates the bioluminescence operon


Pssm-ID: 197715 [Multi-domain]  Cd Length: 58  Bit Score: 78.72  E-value: 1.43e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2279496592  313 REREILELIAKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEA 364
Cdd:smart00421   7 REREVLRLLAEGLTNKEIAERLGISEKTVKTHLSNIMRKLGVRSRTQAVRLA 58
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
58-127 3.41e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 70.28  E-value: 3.41e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592  58 LRMIAREGVTNALKHARAGCIRLSLGVEGSRLRMTIADDGQGFDAEAlhGGQRGHFGCIGIEERCAKFGG 127
Cdd:cd16917     1 LYRIVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPA--PPGGGGFGLLGMRERAELLGG 68
PRK11644 PRK11644
signal transduction histidine-protein kinase/phosphatase UhpB;
3-127 4.24e-12

signal transduction histidine-protein kinase/phosphatase UhpB;


Pssm-ID: 236945 [Multi-domain]  Cd Length: 495  Bit Score: 67.31  E-value: 4.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592   3 TRSLVSELRVPSRENADLVAALQAIVDE-HPLGCGPVLKLEVSGPMPPLPSRTVHHLRMIAREGVTNALKHARAGCIRLS 81
Cdd:PRK11644  355 VRRLLGRLRPRQLDDLTLEQAIRSLMREmELEDRGIVSHLDWRIDESALSETQRVTLFRVCQEGLNNIVKHADASAVTLQ 434
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2279496592  82 LGVEGSRLRMTIADDGQGFDAEALHGGqrghFGCIGIEERCAKFGG 127
Cdd:PRK11644  435 GWQQDERLMLVIEDDGSGLPPGSGQQG----FGLRGMRERVTALGG 476
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
57-105 8.38e-06

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 44.18  E-value: 8.38e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2279496592   57 HLRMIAREGVTNALKHARA-GCIRLSLGVEGSRLRMTIADDGQGFDAEAL 105
Cdd:smart00387   5 RLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHVEITVEDNGPGIPPEDL 54
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
50-105 1.22e-05

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 44.20  E-value: 1.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592  50 LPSRTVHHLRMIAREGVTNALKHARAGC----IRLSLGVEGSRLRMTIADDGQGFDAEAL 105
Cdd:pfam13581  24 LPEELLDEVELAVGEACTNAVEHAYREGpegpVEVRLTSDGGGLVVTVADSGPPFDPLTL 83
sigma70-ECF TIGR02937
RNA polymerase sigma factor, sigma-70 family; This model encompasses all varieties of the ...
235-352 2.91e-03

RNA polymerase sigma factor, sigma-70 family; This model encompasses all varieties of the sigma-70 type sigma factors including the ECF subfamily. A number of sigma factors have names with a different number than 70 (i.e. sigma-38), but in fact, all except for the Sigma-54 family (TIGR02395) are included within this family. Several Pfam models hit segments of these sequences including Sigma-70 region 2 (pfam04542) and Sigma-70, region 4 (pfam04545), but not always above their respective trusted cutoffs.


Pssm-ID: 274357 [Multi-domain]  Cd Length: 158  Bit Score: 38.10  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 235 AILRAHDPQARILVYSTF----AHDDEVQMAL------------DAGAAGYLQKTAsRDELLTALRRVAAGGSYLPPELE 298
Cdd:TIGR02937   5 ELYERYLPLVYRYARRYLgddaDAEDLVQEAFlkllealdrfdpEGSFKAWLFRIA-RNLILDYLRRKRRLRRELDLLEE 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2279496592 299 ---------------QRLADLRLCV-GISMREREILELIA-KGHANKQIAALFAISEDTVKRHVSHILEKL 352
Cdd:TIGR02937  84 lldsdpspeeeleqeEEREALREALeKLPEREREVLVLRYlEGLSYKEIAEILGISVGTVKRRLKRARKKL 154
 
Name Accession Description Interval E-value
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
166-369 4.73e-46

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 156.73  E-value: 4.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 166 MTPPLTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQAR 245
Cdd:PRK10651    3 NQEPATILLIDDHPMLRTGVKQLISMAPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 246 ILVYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAAGGSYLPPELEQRLA---------DLRLCVGISMRERE 316
Cdd:PRK10651   83 IVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQAAAGEMVLSEALTPVLAaslranratTERDVNQLTPRERD 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2279496592 317 ILELIAKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEAIRRGI 369
Cdd:PRK10651  163 ILKLIAQGLPNKMIARRLDITESTVKVHVKHMLKKMKLKSRVEAAVWVHQERI 215
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
172-288 6.37e-41

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: 139.95  E-value: 6.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEPDIEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2279496592 252 FAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAA 288
Cdd:cd17535    81 HDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
169-371 7.54e-38

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: 132.32  E-value: 7.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 169 PLTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAilrahdpqarilv 248
Cdd:COG2197     1 MIRVLIVDDHPLVREGLRALLEAEPDIEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALR------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 249 ystfahddevqmaldagaagylqktasrdELLTAlrrvaaggsylppeleqrladlrlcvgismREREILELIAKGHANK 328
Cdd:COG2197    68 -----------------------------RLLTP------------------------------REREVLRLLAEGLSNK 88
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2279496592 329 QIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEAIRRGIVR 371
Cdd:COG2197    89 EIAERLGISERTVKTHVSNILRKLGVRNRTELVLLALRLGLLD 131
PRK15369 PRK15369
two component system response regulator;
169-369 1.12e-37

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 134.82  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 169 PLTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAkrgEDALEVYQLRQ---PGVVLMDLQLPGITGVQATAILRAHDPQAR 245
Cdd:PRK15369    3 NYKILLVDDHELIINGIKNMLAPYPRYKIVGQV---DNGLEVYNACRqlePDIVILDLGLPGMNGLDVIPQLHQRWPAMN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 246 ILVYStfAHDDE--VQMALDAGAAGYLQKTASRDELLTALRRVAAGGSYLPPEL--EQRLADLRLCVG----ISMREREI 317
Cdd:PRK15369   80 ILVLT--ARQEEhmASRTLAAGALGYVLKKSPQQILLAAIQTVAVGKRYIDPALnrEAILALLNADDTnpplLTPRERQI 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2279496592 318 LELIAKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEAIRRGI 369
Cdd:PRK15369  158 LKLITEGYTNRDIAEQLSISIKTVETHRLNMMRKLDVHKVAELLNWARRLGL 209
PRK09483 PRK09483
response regulator; Provisional
170-369 5.64e-37

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 132.92  E-value: 5.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 170 LTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQAT-AILRaHDPQARILV 248
Cdd:PRK09483    2 INVLLVDDHELVRAGIRRILEDIKGIKVVGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATrKILR-YTPDVKIIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 249 YSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAAGGSYLPPELEQRLADLRLC-------VGISMREREILELI 321
Cdd:PRK09483   81 LTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIRSVHSGQRYIASDIAQQMALSQIEpatenpfASLSERELQIMLMI 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2279496592 322 AKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEAIRRGI 369
Cdd:PRK09483  161 TKGQKVNEISEQLNLSPKTVNSYRYRMFSKLNISGDVELTHLAIRHGL 208
PRK10360 PRK10360
transcriptional regulator UhpA;
170-354 1.30e-33

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 123.55  E-value: 1.30e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 170 LTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQ---------ATAILRAH 240
Cdd:PRK10360    2 ITVALIDDHLIVRSGFAQLLGLEPDLQVVAEFGSGREALAGLPGRGVQVCICDISMPDISGLEllsqlpkgmATIMLSVH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 241 DPQARIlvystfahddevQMALDAGAAGYLQKTASRDELLTALRRVAAGGSYLPPELEQRLADLRLcVGISMREREILEL 320
Cdd:PRK10360   82 DSPALV------------EQALNAGARGFLSKRCSPDELIAAVHTVATGGCYLTPDIAIKLASGRQ-DPLTKRERQVAEK 148
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2279496592 321 IAKGHANKQIAALFAISEDTVKRHVSHILEKLGV 354
Cdd:PRK10360  149 LAQGMAVKEIAAELGLSPKTVHVHRANLMEKLGV 182
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
167-361 2.79e-32

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 120.73  E-value: 2.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 167 TPPLTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARI 246
Cdd:PRK10403    4 ATPFQVLIVDDHPLMRRGVRQLLELDPGFEVVAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 247 LVYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAAGGSYLPPELEQRLADlRLCVG--------ISMREREIL 318
Cdd:PRK10403   84 IILTVSDASSDVFALIDAGADGYLLKDSDPEVLLEAIRAGAKGSKVFSERVNQYLRE-REMFGaeedpfsvLTERELDVL 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2279496592 319 ELIAKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQAT 361
Cdd:PRK10403  163 HELAQGLSNKQIASVLNISEQTVKVHIRNLLRKLNVRSRVAAT 205
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
171-368 3.08e-32

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: 119.82  E-value: 3.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEG-DVKVVGEAkrgEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVY 249
Cdd:COG4566     1 TVYIVDDDEAVRDSLAFLLESAGlRVETFASA---EAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 250 StfAHDDeVQMALDA---GAAGYLQKTASRDELLTALRRVAAGGSYLPPELEQRLADLRLCVGISMREREILELIAKGHA 326
Cdd:COG4566    78 T--GHGD-VPMAVRAmkaGAVDFLEKPFDDQALLDAVRRALARDRARRAERARRAELRARLASLTPREREVLDLVVAGLS 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2279496592 327 NKQIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEAIRRG 368
Cdd:COG4566   155 NKQIARELGISPRTVEVHRANVMEKLGARSLAELVRLALALG 196
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
172-284 2.02e-27

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: 104.16  E-value: 2.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEG--YVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2279496592 252 FAHDDEVQMALDAGAAGYLQKTASRDELLTALR 284
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
171-272 9.81e-27

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: 102.16  E-value: 9.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYS 250
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEAGFEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILS 80
                          90       100
                  ....*....|....*....|..
gi 2279496592 251 TFAHDDEVQMALDAGAAGYLQK 272
Cdd:COG4753    81 GYSDFEYAQEAIKLGADDYLLK 102
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
172-288 1.02e-26

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: 102.43  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLIELDPDFTVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTV 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2279496592 252 FAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAA 288
Cdd:cd19931    81 SDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAAS 117
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
172-288 4.05e-26

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: 100.81  E-value: 4.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:cd19930     1 VLIAEDQEMVRGALAALLELEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2279496592 252 FAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAA 288
Cdd:cd19930    81 FGRPGYFRRALAAGVDGYVLKDRPIEELADAIRTVHA 117
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
168-291 1.39e-24

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: 97.23  E-value: 1.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 168 PPLTVLIVDDHFVVRSGLAAALEVEGdVKVVgEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHD--PQAR 245
Cdd:COG0784     4 GGKRILVVDDNPDNRELLRRLLERLG-YEVT-TAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPrlPDIP 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2279496592 246 ILVYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAAGGS 291
Cdd:COG0784    82 IIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
2-127 8.01e-24

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 98.92  E-value: 8.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592   2 ETRSLVSELRVPSRENADLVAALQAIVDEHPLGCGPVLKLEVSGPMPPLPSRTVHHLRMIAREGVTNALKHARAGCIRLS 81
Cdd:COG4585   107 ELRRLVRGLRPPALDDLGLAAALEELAERLLRAAGIRVELDVDGDPDRLPPEVELALYRIVQEALTNALKHAGATRVTVT 186
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2279496592  82 LGVEGSRLRMTIADDGQGFDAEALHGgqrGHFGCIGIEERCAKFGG 127
Cdd:COG4585   187 LEVDDGELTLTVRDDGVGFDPEAAPG---GGLGLRGMRERAEALGG 229
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
172-288 3.78e-23

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: 93.17  E-value: 3.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEG-DVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYS 250
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIDWEElGFEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2279496592 251 tfAHDD-E-VQMALDAGAAGYLQKTASRDELLTALRRVAA 288
Cdd:cd17536    81 --GYDDfEyAQKAIRLGVVDYLLKPVDEEELEEALEKAKE 118
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
171-286 4.94e-23

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: 92.73  E-value: 4.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGdVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYS 250
Cdd:cd17542     2 KVLIVDDAAFMRMMLKDILTKAG-YEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCS 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2279496592 251 TFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRV 286
Cdd:cd17542    81 AMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKV 116
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
168-323 2.93e-22

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: 97.34  E-value: 2.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 168 PPLTVLIVDDHFVVRSGLAAALEVEGdVKVVgEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARIL 247
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAG-YEVE-TAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVI 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2279496592 248 VYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAAggsylPPELEQRLADLRLCVGISMREREILELIAK 323
Cdd:COG2204    79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALE-----RRRLRRENAEDSGLIGRSPAMQEVRRLIEK 149
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
169-353 3.13e-22

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: 93.10  E-value: 3.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 169 PLTVLIVDDHFVVRSGLAAALEVEG-DVKVvgeAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARIL 247
Cdd:COG0745     1 MPRILVVEDDPDIRELLADALEREGyEVDT---AADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 248 VYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVA--------AGGSYLPPELEQRLADLRLcVGISMREREILE 319
Cdd:COG0745    78 MLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLrrraaevlRVGDLLDLAAREVTRDGEP-VELTPKEFRLLE 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2279496592 320 LIAKgHANK---------QIAALFAISEDTVKRHVSHILEKLG 353
Cdd:COG0745   157 LLMR-NPGRvvsreqlleEVWGYDYGDDRTVDVHISRLRKKLE 198
GerE COG5905
Spore transcriptional regulator GerE (stand-alone HTH domain) [Cell cycle control, cell ...
307-370 3.68e-22

Spore transcriptional regulator GerE (stand-alone HTH domain) [Cell cycle control, cell division, chromosome partitioning, Transcription];


Pssm-ID: 444607 [Multi-domain]  Cd Length: 76  Bit Score: 88.86  E-value: 3.68e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2279496592 307 CVGISMREREILELIAKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEAIRRGIV 370
Cdd:COG5905    10 PSLLTKREREVLELLAEGLTNKEIARQLFISEKTVKNHVSNILRKLGVRNRVQAVVWALRLGLL 73
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
167-288 6.76e-22

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 90.41  E-value: 6.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 167 TPPLTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARI 246
Cdd:COG4565     1 MKMIRVLIVEDDPMVAELLRRYLERLPGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2279496592 247 LVYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAA 288
Cdd:COG4565    81 IVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLE 122
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
169-286 3.04e-20

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 88.33  E-value: 3.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 169 PLTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARIlV 248
Cdd:COG3279     1 MMKILIVDDEPLARERLERLLEKYPDLEVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPI-I 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2279496592 249 YSTfAHDDEVQMALDAGAAGYLQKTASRDELLTALRRV 286
Cdd:COG3279    80 FTT-AYDEYALEAFEVNAVDYLLKPIDEERLAKALEKA 116
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
173-272 8.17e-20

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: 83.43  E-value: 8.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 173 LIVDDHFVVRSGLAAALEVEGDVkvVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYSTF 252
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYE--VDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAK 78
                          90       100
                  ....*....|....*....|
gi 2279496592 253 AHDDEVQMALDAGAAGYLQK 272
Cdd:cd00156    79 ADEEDAVRALELGADDYLVK 98
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
169-287 8.58e-20

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: 85.73  E-value: 8.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 169 PLTVLIVDDHFVVRSGLAAALEVEGdVKVVgEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQAR--I 246
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAG-YEVV-EAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADipI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2279496592 247 LVYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVA 287
Cdd:COG3706    79 IFLTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVA 119
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
168-306 7.09e-19

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: 84.45  E-value: 7.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 168 PPLTVLIVDDHFVVRSGLAAALEVEGdVKVVgEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARI- 246
Cdd:COG3437     5 QAPTVLIVDDDPENLELLRQLLRTLG-YDVV-TAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIp 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2279496592 247 -LVYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAAGGSYLpPELEQRLADLRL 306
Cdd:COG3437    83 vIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQ-RELDDLVLYLKL 142
HTH_LUXR smart00421
helix_turn_helix, Lux Regulon; lux regulon (activates the bioluminescence operon
313-364 1.43e-18

helix_turn_helix, Lux Regulon; lux regulon (activates the bioluminescence operon


Pssm-ID: 197715 [Multi-domain]  Cd Length: 58  Bit Score: 78.72  E-value: 1.43e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2279496592  313 REREILELIAKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEA 364
Cdd:smart00421   7 REREVLRLLAEGLTNKEIAERLGISEKTVKTHLSNIMRKLGVRSRTQAVRLA 58
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
170-353 1.98e-18

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 82.64  E-value: 1.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 170 LTVLIVDDHFVVRSGLAAALEvEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVY 249
Cdd:PRK09958    1 MNAIIIDDHPLAIAAIRNLLI-KNDIEILAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 250 StfAHDDEV--QMALDAGAAGYLQKTASRDELLTALRRVAAGGSYLPPELE----------QRLADLrlcvgiSMREREI 317
Cdd:PRK09958   80 S--AKNDHFygKHCADAGANGFVSKKEGMNNIIAAIEAAKNGYCYFPFSLNrfvgsltsdqQKLDSL------SKQEISV 151
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2279496592 318 LELIAKGHANKQIAALFAISEDTVKRHVSHILEKLG 353
Cdd:PRK09958  152 MRYILDGKDNNDIAEKMFISNKTVSTYKSRLMEKLE 187
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
172-284 2.31e-18

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: 80.13  E-value: 2.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPqARILVYST 251
Cdd:cd17541     3 VLIVDDSAVMRKLLSRILESDPDIEVVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERP-TPVVMVSS 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2279496592 252 FAHD--DEVQMALDAGAAGYLQK---------TASRDELLTALR 284
Cdd:cd17541    82 LTEEgaEITLEALELGAVDFIAKpsggisldlEEIAEELIEKIK 125
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
172-283 3.14e-18

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: 79.77  E-value: 3.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGdVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPqARILVYST 251
Cdd:cd19932     3 VLIAEDEALIRMDLREMLEEAG-YEVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENI-APIVLLTA 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2279496592 252 FAHDDEVQMALDAGAAGYLQKTASRDELLTAL 283
Cdd:cd19932    81 YSQQDLVERAKEAGAMAYLVKPFSESDLIPAI 112
LuxR_C_like cd06170
C-terminal DNA-binding domain of LuxR-like proteins. This domain contains a helix-turn-helix ...
313-366 3.69e-18

C-terminal DNA-binding domain of LuxR-like proteins. This domain contains a helix-turn-helix motif and binds DNA. Proteins belonging to this group are response regulators; some act as transcriptional activators, others as transcriptional repressors. Many are active as homodimers. Many are two domain proteins in which the DNA binding property of the C-terminal DNA binding domain is modulated by modifications of the N-terminal domain. For example in the case of Lux R which participates in the regulation of gene expression in response to fluctuations in cell-population density (quorum-sensing), a signaling molecule, the pheromone Acyl HSL (N-acyl derivatives of homoserine lactone), binds to the N-terminal domain and leads to LuxR dimerization. For others phophorylation of the N-terminal domain leads to multimerization, for example Escherichia coli NarL and Sinorhizobium melilot FixJ. NarL controls gene expression of many respiratory-related operons when environmental nitrate or nitrite is present under anerobic conditions. FixJ is involved in the transcriptional activation of nitrogen fixation genes. The group also includes small proteins which lack an N-terminal signaling domain, such as Bacillus subtilis GerE. GerE is dimeric and acts in conjunction with sigmaK as an activator or a repressor modulating the expression of various genes in particular those encoding the spore-coat. These LuxR family regulators may share a similar organization of their target binding sites. For example the LuxR dimer binds the lux box, a 20bp inverted repeat, GerE dimers bind two 12bp consensus sequences in inverted orientation having the central four bases overlap, and the NarL dimer binds two 7bp inverted repeats separated by 2 bp.


Pssm-ID: 99777 [Multi-domain]  Cd Length: 57  Bit Score: 77.57  E-value: 3.69e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2279496592 313 REREILELIAKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEAIR 366
Cdd:cd06170     4 REREVLRLLAEGKTNKEIADILGISEKTVKTHLRNIMRKLGVKSRTQLVAYAIR 57
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
169-355 6.73e-18

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 81.46  E-value: 6.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 169 PLTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILV 248
Cdd:PRK09935    3 PASVIIMDTHPIIRMSIEVLLQKNSELQIVLKTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 249 YSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAAGGSYLPPELEQRLADLRLCVG------ISMREREILELIA 322
Cdd:PRK09935   83 LSSKSECFYAGRAIQAGANGFVSKCNDQNDIFHAVQMILSGYTFFPSETLNYIKSNKCSTNsstdtvLSNREVTILRYLV 162
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2279496592 323 KGHANKQIAALFAISEDTVKRHVSHILEKLGVH 355
Cdd:PRK09935  163 SGLSNKEIADQLLLSNKTVSAHKSNIYGKLGLH 195
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
172-288 9.39e-18

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: 78.35  E-value: 9.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRaHDPQARILVYST 251
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPDIEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLS-KLAKPPLIVFVT 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2279496592 252 fAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAA 288
Cdd:cd17532    80 -AYDEYAVEAFELNAVDYLLKPFSEERLAEALAKLRK 115
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
172-283 1.61e-17

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: 77.51  E-value: 1.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEG-DVKVVGEakrGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQAR---IL 247
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGyEVDVAEN---GQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRrtpII 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2279496592 248 VYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTAL 283
Cdd:cd17546    78 ALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
166-285 2.54e-16

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 79.89  E-value: 2.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 166 MTPPLTVLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQAR 245
Cdd:PRK11361    1 MTAINRILIVDDEDNVRRMLSTAFALQG--FETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTP 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2279496592 246 ILVYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRR 285
Cdd:PRK11361   79 VILMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQR 118
GerE pfam00196
Bacterial regulatory proteins, luxR family;
311-364 5.61e-16

Bacterial regulatory proteins, luxR family;


Pssm-ID: 425517 [Multi-domain]  Cd Length: 57  Bit Score: 71.46  E-value: 5.61e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2279496592 311 SMREREILELIAKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEA 364
Cdd:pfam00196   4 SPREREVLRWLAAGKSNKEIADELGISEKTVKVHRSNIMRKLNVHSRVELVRMA 57
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
168-324 2.99e-15

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: 73.45  E-value: 2.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 168 PPLTVLIVDDHFVVRSGLAAALEVEGdVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPqARIL 247
Cdd:COG3707     2 RGLRVLVVDDEPLRRADLREGLREAG-YEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP-APVI 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2279496592 248 VYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAAGGSYLpPELEQRLADLRLcvgiSMREREILElIAKG 324
Cdd:COG3707    80 LLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFREL-RALRRELAKLRE----ALEERKLIE-RAKG 150
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
58-127 3.41e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 70.28  E-value: 3.41e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592  58 LRMIAREGVTNALKHARAGCIRLSLGVEGSRLRMTIADDGQGFDAEAlhGGQRGHFGCIGIEERCAKFGG 127
Cdd:cd16917     1 LYRIVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPA--PPGGGGFGLLGMRERAELLGG 68
fixJ PRK09390
response regulator FixJ; Provisional
171-369 1.30e-14

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 71.96  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEG-DVKVVGEAkrgEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVY 249
Cdd:PRK09390    5 VVHVVDDDEAMRDSLAFLLDSAGfEVRLFESA---QAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 250 StfAHDDeVQMALDA---GAAGYLQKTASRDELLTALRRV------AAGGSYLPPELEQRLADLrlcvgiSMREREILEL 320
Cdd:PRK09390   82 T--GHGD-VPLAVEAmklGAVDFIEKPFEDERLIGAIERAlaqapeAAKSEAVAADIRARIASL------SERERQVMDG 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2279496592 321 IAKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEAIRRGI 369
Cdd:PRK09390  153 LVAGLSNKVIARDLDISPRTVEVYRANVMTKMQAGSLSELVRMALRAGR 201
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
171-283 3.82e-14

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: 68.20  E-value: 3.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGdVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPG-ITGVQATAILRAhdpQARI-LV 248
Cdd:cd17534     2 KILIVEDEAIIALDLKEILESLG-YEVVGIADSGEEAIELAEENKPDLILMDINLKGdMDGIEAAREIRE---KFDIpVI 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2279496592 249 YSTfAHDDE--VQMALDAGAAGYLQKTASRDELLTAL 283
Cdd:cd17534    78 FLT-AYSDEetLERAKETNPYGYLVKPFNERELKAAI 113
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
171-285 7.01e-14

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: 67.18  E-value: 7.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYS 250
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAG--YEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIA 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2279496592 251 TFAH----DDEvqMALDAGAAGYLQKTASRDELLTALRR 285
Cdd:cd17548    79 LTAYamkgDRE--KILEAGCDGYISKPIDTREFLETVAK 115
CsgD COG2771
DNA-binding transcriptional regulator, CsgD family [Transcription];
205-370 4.47e-13

DNA-binding transcriptional regulator, CsgD family [Transcription];


Pssm-ID: 442052 [Multi-domain]  Cd Length: 188  Bit Score: 67.09  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 205 EDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALR 284
Cdd:COG2771    23 LLLLLLLAALLLLLALLLLAALLLLAAAAAALAAALAAALLLGLLLLLLIALLLLLLLLLALLLLLALLALLAALLARLA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 285 RVAAGGSYLPPELEQRLADLRLCVGISMREREILELIAKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEA 364
Cdd:COG2771   103 ALLLALALAALLLAALARLLARAPGLTPREREVLRLLAEGLTLKEIARILGISERTVRTHLKRIYRKLGVSSRAELVALA 182

                  ....*.
gi 2279496592 365 IRRGIV 370
Cdd:COG2771   183 LRLGLI 188
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
171-283 5.84e-13

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: 64.77  E-value: 5.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEG-DVKVVGEAkrgEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILV- 248
Cdd:cd17563     2 SLLLVDDDEVFAERLARALERRGfEVETAHSV---EEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVl 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2279496592 249 --YSTFAhddevqMALDA---GAAGYLQKTASRDELLTAL 283
Cdd:cd17563    79 tgYASIA------TAVEAiklGADDYLAKPADADEILAAL 112
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
166-296 8.61e-13

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: 66.09  E-value: 8.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 166 MTPPLTVLIVDDHFVVRSGLAAALEVEGDVkvVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQAR 245
Cdd:COG4567     1 SAEDRSLLLVDDDEAFARVLARALERRGFE--VTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDAR 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2279496592 246 ILVYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAAGGSYLPPE 296
Cdd:COG4567    79 IVVLTGYASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAPPEN 129
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
171-286 1.33e-12

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: 63.86  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGdVKVVgEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQAR--ILV 248
Cdd:cd17562     2 KILAVDDSASIRQMVSFTLRGAG-YEVV-EAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFtpILM 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2279496592 249 YSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRV 286
Cdd:cd17562    80 LTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKV 117
PRK11697 PRK11697
two-component system response regulator BtsR;
170-301 1.69e-12

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 66.41  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 170 LTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILrahDPQAR-ILV 248
Cdd:PRK11697    2 IKVLIVDDEPLAREELRELLQEEGDIEIVGECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGML---DPEHMpYIV 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2279496592 249 YSTfAHDDEVQMALDAGAAGYLQKTASRDEL---LTALRRVAAGGSYLPPELEQRL 301
Cdd:PRK11697   79 FVT-AFDEYAIKAFEEHAFDYLLKPIDPARLaktLARLRQERSPQDVLLPEAQPPL 133
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
172-272 1.92e-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: 62.95  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDpQARILVYST 251
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHG--YRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWS-AVPVIVLSA 77
                          90       100
                  ....*....|....*....|.
gi 2279496592 252 FAHDDEVQMALDAGAAGYLQK 272
Cdd:cd17620    78 RDEESDKIAALDAGADDYLTK 98
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
173-272 2.41e-12

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: 62.43  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 173 LIVDDHFVVRSGLAAALEVEG-DVKVvgeAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGyEVDT---AADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTA 77
                          90       100
                  ....*....|....*....|.
gi 2279496592 252 FAHDDEVQMALDAGAAGYLQK 272
Cdd:cd17574    78 KDEEEDKVLGLELGADDYITK 98
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
171-272 2.47e-12

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: 62.99  E-value: 2.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYS 250
Cdd:cd17555     2 TILVIDDDEVVRESIAAYLEDSG--FQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVS 79
                          90       100
                  ....*....|....*....|...
gi 2279496592 251 -TFAHDDEVQmALDAGAAGYLQK 272
Cdd:cd17555    80 gAGVMSDAVE-ALRLGAWDYLTK 101
PRK11644 PRK11644
signal transduction histidine-protein kinase/phosphatase UhpB;
3-127 4.24e-12

signal transduction histidine-protein kinase/phosphatase UhpB;


Pssm-ID: 236945 [Multi-domain]  Cd Length: 495  Bit Score: 67.31  E-value: 4.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592   3 TRSLVSELRVPSRENADLVAALQAIVDE-HPLGCGPVLKLEVSGPMPPLPSRTVHHLRMIAREGVTNALKHARAGCIRLS 81
Cdd:PRK11644  355 VRRLLGRLRPRQLDDLTLEQAIRSLMREmELEDRGIVSHLDWRIDESALSETQRVTLFRVCQEGLNNIVKHADASAVTLQ 434
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2279496592  82 LGVEGSRLRMTIADDGQGFDAEALHGGqrghFGCIGIEERCAKFGG 127
Cdd:PRK11644  435 GWQQDERLMLVIEDDGSGLPPGSGQQG----FGLRGMRERVTALGG 476
UhpB COG3851
Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction ...
3-127 4.78e-12

Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction mechanisms];


Pssm-ID: 443060 [Multi-domain]  Cd Length: 493  Bit Score: 66.95  E-value: 4.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592   3 TRSLVSELRVPSRENADLVAALQAIVDE----HPlgcGPVLKLEVSGPMPPLPSRTVHHLRMIAREGVTNALKHARAGCI 78
Cdd:COG3851   345 TRRLLDRLRPAVLDELGLEEALRELPRElafeEP---GISCQLDLRGDPSLLDDTLQLTLYRLVQEALTNILKHAEASQI 421
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2279496592  79 RLSLGVEGSRLRMTIADDGQGFDAEALHGGqrghFGCIGIEERCAKFGG 127
Cdd:COG3851   422 RISLSQDKRLLSLEIRDDGIGLPPELRAKG----FGLRGMRERVRALGG 466
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
172-286 2.49e-11

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: 60.20  E-value: 2.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYSt 251
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEG--YEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMIS- 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2279496592 252 fAHDDeVQMALDA---GAAGYLQKTASRDELLTALRRV 286
Cdd:cd17550    78 -GHGT-IETAVKAtklGAYDFIEKPLSLDRLLLTIERA 113
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
171-286 3.19e-11

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: 59.93  E-value: 3.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGdVKVVGeAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYS 250
Cdd:cd17554     2 KILVVDDEENIRELYKEELEDEG-YEVVT-AGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICT 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2279496592 251 TFAHDDEVQMALDAGAagYLQKTASRDELLTALRRV 286
Cdd:cd17554    80 AYSEYKSDFSSWAADA--YVVKSSDLTELKETIKRL 113
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
172-284 4.52e-11

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


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 59.32  E-value: 4.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEG--YEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTA 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2279496592 252 FAHDDEVQMALDAGAAGYLQKTASRDELLTALR 284
Cdd:cd17627    79 RDSVSDRVAGLDAGADDYLVKPFALEELLARVR 111
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
172-285 4.95e-11

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: 59.49  E-value: 4.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGDVKVvgEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:cd17553     3 ILIVDDQYGIRILLNEVFNKEGYQTF--QAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTA 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2279496592 252 FAHDDEVQMALDAGAAGYLQKTASRDELLTALRR 285
Cdd:cd17553    81 YGELDMIQESKELGALTHFAKPFDIDEIRDAVKK 114
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
172-285 6.18e-11

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: 59.43  E-value: 6.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGdVKVVGEAkRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYSt 251
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAG-FRVRAFA-DAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILIT- 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2279496592 252 fAHDDeVQMALDA---GAAGYLQKTASRDELLTALRR 285
Cdd:cd17549    78 -GHGD-VPMAVEAmraGAYDFLEKPFDPERLLDVVRR 112
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
170-287 6.86e-11

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: 59.18  E-value: 6.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 170 LTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVY 249
Cdd:cd19925     1 INVLIVEDDPMVAEIHRAYVEQVPGFTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVV 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2279496592 250 STFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVA 287
Cdd:cd19925    81 TAANDVETVREALRLGVVDYLIKPFTFERLRQRLERYR 118
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
170-226 7.29e-11

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: 57.19  E-value: 7.29e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2279496592  170 LTVLIVDDHFVVRSGLAAALEVEGDVkvVGEAKRGEDALEVYQLRQPGVVLMDLQLP 226
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYE--VDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
171-286 1.50e-10

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 58.20  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDH----FVVRSGLAAAlEVEGDVKVVGEakrGEDALEVyqLRQ---------PGVVLMDLQLPGITGVQATAIL 237
Cdd:cd17557     1 TILLVEDNpgdaELIQEAFKEA-GVPNELHVVRD---GEEALDF--LRGegeyadaprPDLILLDLNMPRMDGFEVLREI 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2279496592 238 RAhDPQAR---ILVYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRV 286
Cdd:cd17557    75 KA-DPDLRripVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSL 125
MalT COG2909
ATP-, maltotriose- and DNA-dependent transcriptional regulator MalT [Transcription];
269-371 2.12e-10

ATP-, maltotriose- and DNA-dependent transcriptional regulator MalT [Transcription];


Pssm-ID: 442153 [Multi-domain]  Cd Length: 184  Bit Score: 59.33  E-value: 2.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 269 YLQKTASRDELLTALRRVAAGGSYLppeleqRLADLRLCVGISMREREILE--LIAKGHANKQIAALFAISEDTVKRHVS 346
Cdd:COG2909    86 ALDPEEALALLERLLALAEAAGRLL------LRALALRALGDREEALAALRrrLLAEGLSNKEIAERLFISVNTVKTHLR 159
                          90       100
                  ....*....|....*....|....*
gi 2279496592 347 HILEKLGVHDRAQATAEAIRRGIVR 371
Cdd:COG2909   160 NIYRKLGVRSRTEAVARARELGLLA 184
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
170-286 7.27e-10

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: 56.01  E-value: 7.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 170 LTVLIVDDHFVVRSGLAAALEVEGDVKVVgEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVY 249
Cdd:cd17593     1 MKVLICDDSSMARKQLARALPADWDVEIT-FAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVV 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2279496592 250 STFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRV 286
Cdd:cd17593    80 SGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLEEL 116
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
169-272 1.22e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 59.01  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 169 PLTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPqARILV 248
Cdd:PRK00742    3 KIRVLVVDDSAFMRRLISEILNSDPDIEVVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRP-TPVVM 81
                          90       100
                  ....*....|....*....|....*.
gi 2279496592 249 YSTFAHDD-EVQM-ALDAGAAGYLQK 272
Cdd:PRK00742   82 VSSLTERGaEITLrALELGAVDFVTK 107
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
171-285 3.09e-09

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: 54.14  E-value: 3.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGdVKVVGEAkRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYS 250
Cdd:cd17537     2 TVYVVDDDEAVRDSLAFLLRSVG-LAVKTFT-SASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFIT 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2279496592 251 tfAHDDeVQMALDA---GAAGYLQKTASRDELLTALRR 285
Cdd:cd17537    80 --GHGD-VPMAVEAmkaGAVDFLEKPFRDQVLLDAIEQ 114
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
171-284 4.15e-09

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: 53.99  E-value: 4.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGDVKVVGEAkRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARI-LVY 249
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAGYLEVVSFT-DPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVpIVM 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2279496592 250 STFAHDDEV-QMALDAGAAGYLQKTASRDELLTALR 284
Cdd:cd17551    81 ITADTDREVrLRALEAGATDFLTKPFDPVELLARVR 116
PRK10600 PRK10600
nitrate/nitrite two-component system sensor histidine kinase NarX;
4-121 5.30e-09

nitrate/nitrite two-component system sensor histidine kinase NarX;


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 57.76  E-value: 5.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592   4 RSLVSELRVPSREnADLVAALQAIVDEHPLGCGPVLKLEVSGPMPPLPSRTVHHLRMIAREGVTNALKHARAGCIRLSLG 83
Cdd:PRK10600  417 RELLTTFRLQLTE-PGLRPALEASCEEFSARFGFPVKLDYQLPPRLVPSHQAIHLLQIAREALSNALKHAQASEVVVTVA 495
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2279496592  84 VEGSRLRMTIADDGQGFDAEAlhgGQRGHFGCIGIEER 121
Cdd:PRK10600  496 QNQNQVKLSVQDNGCGVPENA---ERSNHYGLIIMRDR 530
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
171-272 1.02e-08

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: 52.50  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGdVKVVgEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAhDPQAR----I 246
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEG-YEVL-TADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKE-DPETRhipvI 77
                          90       100
                  ....*....|....*....|....*.
gi 2279496592 247 LVYSTFAHDDEVQmALDAGAAGYLQK 272
Cdd:cd17538    78 MITALDDREDRIR-GLEAGADDFLSK 102
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
172-280 1.45e-08

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 52.39  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYSt 251
Cdd:cd17619     3 ILIVEDEPVTRATLKSYFEQEG--YDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSEVGIILVTG- 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2279496592 252 faHDDEVQ--MALDAGAAGYLQKTASRDELL 280
Cdd:cd17619    80 --RDDEVDriVGLEIGADDYVTKPFNPRELL 108
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
171-286 3.43e-08

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: 51.48  E-value: 3.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGdVKVVgEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAhDPQAR----I 246
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLERAG-FDVV-EAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKR-DEMTRdipiI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2279496592 247 LVYSTFAHDDEVQmALDAGAAGYLQKTASRDELLTALRRV 286
Cdd:cd17618    79 MLTARGEEEDKVR-GLEAGADDYITKPFSPRELVARIKAV 117
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
171-284 4.70e-08

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: 50.81  E-value: 4.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEG-DVKVvgeAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVY 249
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGwDVET---AADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFL 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2279496592 250 STF-AHDDEVQmALDAGAAGYLQKTASRDELLTALR 284
Cdd:cd17615    78 TAKdSVEDRIA-GLTAGGDDYVTKPFSLEEVVARLR 112
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
174-272 5.23e-08

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: 50.35  E-value: 5.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 174 IVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYSTFA 253
Cdd:cd17565     3 IVDDDKNIIKILSDIIEDDDLGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQVS 82
                          90
                  ....*....|....*....
gi 2279496592 254 HDDEVQMALDAGAAGYLQK 272
Cdd:cd17565    83 DKEMIGKAYQAGIEFFINK 101
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
50-108 5.46e-08

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 51.07  E-value: 5.46e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2279496592  50 LPSRTVHHLRMIAREGVTNALKHARA----GCIRLSLGVEGSRLRMTIADDGQGFDAEALHGG 108
Cdd:COG2172    27 LDEDDADDLVLAVSEAVTNAVRHAYGgdpdGPVEVELELDPDGLEIEVRDEGPGFDPEDLPDP 89
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
172-283 5.90e-08

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: 50.53  E-value: 5.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEG-DVKVVGeakRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARI-LVY 249
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGaEVTTAH---SGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTpAIA 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2279496592 250 ST-FAHDDEVQMALDAGAAGYLQKTASRDELLTAL 283
Cdd:cd17580    78 LTgYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
171-285 9.48e-08

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: 49.96  E-value: 9.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEG-DVKVVgeaKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVY 249
Cdd:cd19919     2 TVWIVDDDSSIRWVLERALAGAGlTVTSF---ENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIM 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2279496592 250 STFAHDDEVQMALDAGAAGYLQKTASRDELLTALRR 285
Cdd:cd19919    79 TAHSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVER 114
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
171-284 1.25e-07

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: 49.71  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGdVKVVgEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQA-RILV- 248
Cdd:cd17569     2 TILLVDDEPNILKALKRLLRREG-YEVL-TATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTvRILLt 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2279496592 249 -YStfahddEVQMALDAGAAG----YLQKTASRDELLTALR 284
Cdd:cd17569    80 gYA------DLDAAIEAINEGeiyrFLTKPWDDEELKETIR 114
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
172-272 1.42e-07

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: 49.14  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHD--PQARILVY 249
Cdd:cd17561     4 VLIADDNREFVQLLEEYLNSQPDMEVVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRleKRPKIIML 83
                          90       100
                  ....*....|....*....|...
gi 2279496592 250 STFAHDDEVQMALDAGAAGYLQK 272
Cdd:cd17561    84 TAFGQEDITQRAVELGASYYILK 106
PRK10840 PRK10840
transcriptional regulator RcsB; Provisional
170-354 1.43e-07

transcriptional regulator RcsB; Provisional


Pssm-ID: 182771 [Multi-domain]  Cd Length: 216  Bit Score: 51.76  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 170 LTVLIVDDHFVVRSGLAAALEVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGIT---GVQATAILRAHDPQARI 246
Cdd:PRK10840    4 MNVIIADDHPIVLFGIRKSLEQIEWVNVVGEFEDSTALINNLPKLDAHVLITDLSMPGDKygdGITLIKYIKRHFPSLSI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 247 LVYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAAGGSYLPPELEQRL--------ADLRLcvgiSMREREIL 318
Cdd:PRK10840   84 IVLTMNNNPAILSAVLDLDIEGIVLKQGAPTDLPKALAALQKGKKFTPESVSRLLekisaggyGDKRL----SPKESEVL 159
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2279496592 319 ELIAKGHANKQIAALFAISEDTVKRHVSHILEKLGV 354
Cdd:PRK10840  160 RLFAEGFLVTEIAKKLNRSIKTISSQKKSAMMKLGV 195
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
15-101 3.43e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Erythrobacter litoralis blue light-activated histidine kinase 2; This domain family includes the histidine kinase-like ATPase (HATPase) domain of blue light-activated histidine kinase 2 of Erythrobacter litoralis (EL346). Signaling commonly occurs within HK dimers, however EL346 functions as a monomer. Also included in this family are the HATPase domains of ethanolamine utilization sensory transduction histidine kinase (EutW), whereby regulation of ethanolamine, a carbon and nitrogen source for gut bacteria, results in autophosphorylation and subsequent phosphoryl transfer to a response regulator (EutV) containing an RNA-binding domain. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory PAS sensor domain, while some have an N-terminal histidine kinase domain.


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 48.95  E-value: 3.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592  15 RENADLVAAlqAIVDEHPLGcgpVLKLEVSGPMPPLPSRTVHHLRMIAREGVTNALKHA---RA-GCIRLSLGVEGSRLR 90
Cdd:cd16951     2 GEYINRIAS--AINAIHAVG---DIRINITGDTGPVSSEVATAIGLVVNELLQNALKHAfsdREgGTITIRSVVDGDYLR 76
                          90
                  ....*....|.
gi 2279496592  91 MTIADDGQGFD 101
Cdd:cd16951    77 ITVIDDGVGLP 87
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
172-284 3.82e-07

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: 48.14  E-value: 3.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEG-DVKVVgeaKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHdPQARILVYS 250
Cdd:cd17622     3 ILLVEDDPKLARLIADFLESHGfNVVVE---HRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPK-YQGPILLLT 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2279496592 251 TFAHDDEVQMALDAGAAGYLQKTASRDELLTALR 284
Cdd:cd17622    79 ALDSDIDHILGLELGADDYVVKPVEPAVLLARLR 112
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
16-114 4.82e-07

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 51.44  E-value: 4.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592  16 ENADLVAALQAIVDEH-PLGCGPVLKLEVSGPMPPLPSRTVHHLRMIAREGVTNALKHA----RAGCIRLSLGVEGSRLR 90
Cdd:COG3920   357 EGVDLRDYLRELLEPLrDSYGGRGIRIELDGPDVELPADAAVPLGLILNELVTNALKHAflsgEGGRIRVSWRREDGRLR 436
                          90       100
                  ....*....|....*....|....
gi 2279496592  91 MTIADDGQGFDAEALHGGQRGhFG 114
Cdd:COG3920   437 LTVSDNGVGLPEDVDPPARKG-LG 459
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
171-272 5.45e-07

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: 47.50  E-value: 5.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQP-GVVLMDLQLPGITGVQATAILRAHDPQARILVY 249
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAG--YAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARKIDPDVKILFI 78
                          90       100
                  ....*....|....*....|....
gi 2279496592 250 STFAhDDEVQMALDA-GAAGYLQK 272
Cdd:cd18160    79 SGGA-AAAPELLSDAvGDNATLKK 101
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
172-286 5.92e-07

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: 47.66  E-value: 5.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEG-DVKVVgeaKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYS 250
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGyEVVLI---EDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISNVPIIFISS 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2279496592 251 TFAHDDEVqMALDAGAAGYLQKTASRDELLTALRRV 286
Cdd:cd18159    78 RDDNMDQV-MAINMGGDDYITKPFDLDVLLAKIKAI 112
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
173-288 6.35e-07

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: 47.65  E-value: 6.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 173 LIVDDHFVVRSGLAAALEVEG-DVKVvgeAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGyEVVT---AYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIML 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2279496592 252 FAHDDEVQ--MALDAGAAGYLQKTASRDELLTalrRVAA 288
Cdd:cd19937    78 TAKGEEFDkvLGLELGADDYITKPFSPRELLA---RVKA 113
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
172-272 7.95e-07

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: 47.12  E-value: 7.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEG-DVKVvgeAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAhDPQAR---IL 247
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGyRVLV---ATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKA-DPATRhipVI 76
                          90       100
                  ....*....|....*....|....*
gi 2279496592 248 VYSTFAHDDEVQMALDAGAAGYLQK 272
Cdd:cd19920    77 FLTALTDTEDKVKGFELGAVDYITK 101
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
171-294 1.52e-06

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 48.65  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYS 250
Cdd:PRK10529    3 NVLIVEDEQAIRRFLRTALEGDG--MRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWSAIPVIVLSA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2279496592 251 TFAHDDEVQmALDAGAAGYLQKTASRDELLT----ALRRVAAGGSYLP 294
Cdd:PRK10529   81 RSEESDKIA-ALDAGADDYLSKPFGIGELQArlrvALRRHSATPAPDP 127
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
169-286 1.76e-06

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 49.85  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 169 PLTVLIVDDHFVvRSGLAAALeVEGDVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILV 248
Cdd:PRK11107  667 PLTVMAVDDNPA-NLKLIGAL-LEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNTPI 744
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2279496592 249 YSTFAH--DDEVQMALDAGAAGYLQKTAsrDEllTALRRV 286
Cdd:PRK11107  745 IAVTAHamAGERERLLSAGMDDYLAKPI--DE--AMLKQV 780
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
172-279 1.79e-06

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 46.36  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEgDVKVVgEAKRGEDALEVYQlRQPGV--VLMDLQLPGITGVQATAILRAHDPQARILVY 249
Cdd:cd17544     3 VLVVDDSATSRNHLRALLRRH-NFQVL-EAANGQEALEVLE-QHPDIklVITDYNMPEMDGFELVREIRKKYSRDQLAII 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2279496592 250 STFAHDDEVQMA--LDAGAAGYLQKTASRDEL 279
Cdd:cd17544    80 GISASGDNALSArfIKAGANDFLTKPFLPEEF 111
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
172-272 1.80e-06

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: 46.22  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGdVKVVgEAKRGEDALEVYQ-LRQPG--------VVLMDLQLPGITGVQATAILRAhDP 242
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLG-FEIA-EAVDGEEALNKLEnLAKEGndlskeldLIITDIEMPKMDGYELTFELRD-DP 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2279496592 243 Q---ARILVYSTFAHDDEVQMALDAGAAGYLQK 272
Cdd:cd19924    78 RlanIPVILNSSLSGEFSRARGKKVGADAYLAK 110
PRK10766 PRK10766
two-component system response regulator TorR;
171-280 2.14e-06

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 48.11  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYs 250
Cdd:PRK10766    4 HILVVEDEPVTRARLQGYFEQEG--YTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRSTVGIILVT- 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2279496592 251 tfAHDDEVQ--MALDAGAAGYLQKTASRDELL 280
Cdd:PRK10766   81 --GRTDSIDriVGLEMGADDYVTKPLELRELL 110
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
172-272 2.66e-06

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: 45.51  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYSt 251
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEG--YAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLT- 77
                          90       100
                  ....*....|....*....|....
gi 2279496592 252 fAHD---DEVQmALDAGAAGYLQK 272
Cdd:cd19935    78 -ARDsveDRVK-GLDLGADDYLVK 99
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
171-287 3.21e-06

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: 46.21  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGDVKVVGEAkrgEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYS 250
Cdd:cd17596     2 TILVVDDEVRSLEALRRTLEEDFDVLTAASA---EEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIIS 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2279496592 251 TFAHDDEVQMAL-DAGAAGYLQKTASRDELLTALRRVA 287
Cdd:cd17596    79 GYTDSEDIIAGInEAGIYQYLTKPWHPDQLLLTVRNAA 116
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
172-284 3.43e-06

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 45.54  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEG-DVKVVGeakRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAhDPQARILVYS 250
Cdd:cd17626     3 ILVVDDDAALAEMIGIVLRGEGfDPAFCG---DGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA-ESGVPIVMLT 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2279496592 251 TFAHDDEVQMALDAGAAGYLQKTASRDELLTALR 284
Cdd:cd17626    79 AKSDTVDVVLGLESGADDYVAKPFKPKELVARIR 112
PRK10100 PRK10100
transcriptional regulator CsgD;
313-364 4.61e-06

transcriptional regulator CsgD;


Pssm-ID: 182241 [Multi-domain]  Cd Length: 216  Bit Score: 47.17  E-value: 4.61e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2279496592 313 REREILELIAKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEA 364
Cdd:PRK10100  159 REKEILNKLRIGASNNEIARSLFISENTVKTHLYNLFKKIAVKNRTQAVSWA 210
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
166-287 5.09e-06

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 47.26  E-value: 5.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 166 MTPPlTVLIVDDHFVVRSGLAAALEVEG-DVKVVGeakRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQA 244
Cdd:PRK11083    1 MQQP-TILLVEDEQAIADTLVYALQSEGfTVEWFE---RGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPAL 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2279496592 245 RILVYStfAHDDEVQ--MALDAGAAGYLQKTASRDELL----TALRRVA 287
Cdd:PRK11083   77 PVIFLT--ARSDEVDrlVGLEIGADDYVAKPFSPREVAarvrTILRRVK 123
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
170-272 5.45e-06

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: 45.02  E-value: 5.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 170 LTVLIVDDHFVVRSGLAAALEvEGDVKVVGEAKRGEDALEvyQLRQPGV--VLMDLQLPGITGVQATAILRAHDPQAR-- 245
Cdd:cd19923     1 MKVLVVDDFSTMRRIIKNLLK-ELGFNNVEEAEDGVDALE--KLKAGGFdfVITDWNMPNMDGLELLKTIRADGALSHlp 77
                          90       100
                  ....*....|....*....|....*..
gi 2279496592 246 ILVYSTFAHDDEVQMALDAGAAGYLQK 272
Cdd:cd19923    78 VLMVTAEAKKENVIAAAQAGVNNYIVK 104
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
57-105 8.38e-06

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 44.18  E-value: 8.38e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2279496592   57 HLRMIAREGVTNALKHARA-GCIRLSLGVEGSRLRMTIADDGQGFDAEAL 105
Cdd:smart00387   5 RLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHVEITVEDNGPGIPPEDL 54
PRK11173 PRK11173
two-component response regulator; Provisional
166-272 8.83e-06

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 46.55  E-value: 8.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 166 MTPPlTVLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQAr 245
Cdd:PRK11173    1 MQTP-HILIVEDELVTRNTLKSIFEAEG--YDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQANVA- 76
                          90       100
                  ....*....|....*....|....*....
gi 2279496592 246 iLVYSTfAHDDEVQ--MALDAGAAGYLQK 272
Cdd:PRK11173   77 -LMFLT-GRDNEVDkiLGLEIGADDYITK 103
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
172-284 8.99e-06

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: 44.40  E-value: 8.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGDVkvVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYA--VDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTA 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2279496592 252 FAHDDEVQMALDAGAAGYLQKTASRDELLTALR 284
Cdd:cd17624    79 RDGVDDRVAGLDAGADDYLVKPFALEELLARLR 111
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
173-285 1.09e-05

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: 44.13  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 173 LIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALE-----VYQLrqpgvVLMDLQLPGITGVQATAILRAHDPQARIL 247
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEG--YTVDVCFDGEEGLEyalsgIYDL-----IILDIMLPGMDGLEVLKSLREEGIETPVL 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2279496592 248 VYSTF-AHDDEVQmALDAGAAGYLQKTASRDELL----TALRR 285
Cdd:cd17625    74 LLTALdAVEDRVK-GLDLGADDYLPKPFSLAELLarirALLRR 115
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
50-105 1.22e-05

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 44.20  E-value: 1.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592  50 LPSRTVHHLRMIAREGVTNALKHARAGC----IRLSLGVEGSRLRMTIADDGQGFDAEAL 105
Cdd:pfam13581  24 LPEELLDEVELAVGEACTNAVEHAYREGpegpVEVRLTSDGGGLVVTVADSGPPFDPLTL 83
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
172-286 1.31e-05

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: 43.94  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEG--FNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSG 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2279496592 252 FAHDDEVQMALDAGAAGYLQKTASRDELLTALRRV 286
Cdd:cd17616    79 LADIEDKVKGLGFGADDYMTKPFHKDELVARIHAI 113
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
172-248 1.43e-05

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: 44.08  E-value: 1.43e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGDVKVVgEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILV 248
Cdd:cd17552     4 ILVIDDEEDIREVVQACLEKLAGWEVL-TASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPV 79
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
172-288 1.75e-05

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: 43.57  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEG-DVKVvgeAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYs 250
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGyEVVT---AYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSNVPIIMLT- 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2279496592 251 tfAHDDEVQ--MALDAGAAGYLQKTASRDELLTalrRVAA 288
Cdd:cd17614    77 --AKDSEVDkvLGLELGADDYVTKPFSNRELLA---RVKA 111
PRK10935 PRK10935
nitrate/nitrite two-component system sensor histidine kinase NarQ;
57-127 1.80e-05

nitrate/nitrite two-component system sensor histidine kinase NarQ;


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 46.38  E-value: 1.80e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2279496592  57 HLRMIAREGVTNALKHARAGCIRLS-LGVEGSRLRMTIADDGQGFD--AEALhggqrGHFGcIGI-EERCAKFGG 127
Cdd:PRK10935  471 HLLQIIREATLNAIKHANASEIAVScVTNPDGEHTVSIRDDGIGIGelKEPE-----GHYG-LNImQERAERLGG 539
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
171-284 2.24e-05

phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The GGDEF response regulator WspR is part of the Wsp system that is homologous to chemotaxis systems and also includes the membrane-bound receptor protein WspA. In response to growth on surfaces, WspR is phosphorylated by the Wsp signal transduction complex and is activated, functioning as a diguanylate cyclase (DGC) that catalyzes c-di-GMP synthesis. WspR is a hybrid response regulator-diguanylate cyclase, containing an N-terminal REC domain and a C-terminal GGDEF domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 43.55  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGDVkVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHdPQAR---IL 247
Cdd:cd17575     2 MVLLVDDQAIIGEAVRRALADEEDI-DFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRAN-PATRdipII 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2279496592 248 VYSTfAHDDEVQM-ALDAGAAGYLQKTASRDELLTALR 284
Cdd:cd17575    80 VLST-KEEPEVKSeAFALGANDYLVKLPDKIELVARIR 116
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
58-101 2.61e-05

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 42.26  E-value: 2.61e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2279496592  58 LRMIAREGVTNALKHARAGC----IRLSLGVEGSRLRMTIADDGQGFD 101
Cdd:cd16936     1 VELAVSEAVTNAVRHAYRHDgpgpVRLELDLDPDRLRVEVTDSGPGFD 48
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
171-284 2.85e-05

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 42.82  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 171 TVLIVDDHFVVRSGLAAALEVEGdVKVVGEAKRGEDAlEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYS 250
Cdd:cd17594     1 HVLVVDDDAAMRHLLILYLRERG-FDVTAAADGAEEA-RLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSDVPIIIISG 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2279496592 251 TFAHDDEVQMALDAGAAGYLQKTASRDELLTALR 284
Cdd:cd17594    79 DRRDEIDRVVGLELGADDYLAKPFGLRELLARVR 112
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
13-106 5.66e-05

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 44.13  E-value: 5.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592  13 PSRENADLVAALQAIVDE-HPLGCGPVLKLEVSGPMPPLPSRT-VHHLRMIAREGVTNALKHARAGC-IRLSLGVEGSRL 89
Cdd:COG2205    86 LELEPVDLAELLEEAVEElRPLAEEKGIRLELDLPPELPLVYAdPELLEQVLANLLDNAIKYSPPGGtITISARREGDGV 165
                          90
                  ....*....|....*..
gi 2279496592  90 RMTIADDGQGFDAEALH 106
Cdd:COG2205   166 RISVSDNGPGIPEEELE 182
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
36-242 6.32e-05

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 44.93  E-value: 6.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592  36 GPVLKLEVSGPMPPL----PSRtvhhLRMIAREGVTNALKHARAGCIRLSLGVE-GSRLRMTIADDGQGFDAEAL----- 105
Cdd:PRK11091  377 GLRFDLEPLLPLPHKvitdGTR----LRQILWNLISNAVKFTQQGGVTVRVRYEeGDMLTFEVEDSGIGIPEDELdkifa 452
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 106 --------HGGQRghfgcigieercAKFGGIASGVLRR-AGHHPGDRTDAGKIRPG------------RPWASRQTTAAP 164
Cdd:PRK11091  453 myyqvkdsHGGKP------------ATGTGIGLAVSKRlAQAMGGDITVTSEEGKGscftltihapavAEEVEDAFDEDD 520
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 165 LMTPPLTVLIVDD----HFVVRSglaaALEVEG-DVKVvgeAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRA 239
Cdd:PRK11091  521 MPLPALNILLVEDielnVIVARS----VLEKLGnSVDV---AMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRE 593

                  ...
gi 2279496592 240 HDP 242
Cdd:PRK11091  594 RYP 596
orf27 CHL00148
Ycf27; Reviewed
172-286 6.49e-05

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 43.94  E-value: 6.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:CHL00148    9 ILVVDDEAYIRKILETRLSIIG--YEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKESDVPIIMLTAL 86
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2279496592 252 FAHDDEVqMALDAGAAGYLQKTASRDEL----LTALRRV 286
Cdd:CHL00148   87 GDVSDRI-TGLELGADDYVVKPFSPKELeariRSVLRRT 124
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
172-272 6.98e-05

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: 41.41  E-value: 6.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEG-DVKVvgeAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYs 250
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGfEVTV---ATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSNVPVIMVT- 76
                          90       100
                  ....*....|....*....|....
gi 2279496592 251 tfAHDDEVQ--MALDAGAAGYLQK 272
Cdd:cd17621    77 --AKDSEIDkvVGLELGADDYVTK 98
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
172-284 7.29e-05

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: 41.80  E-value: 7.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEG-DVKVVgeaKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYS 250
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGyKVTHV---ETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVIT 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2279496592 251 tfAHdDEVQMALDA---GAAGYLQKTASRDELLTALR 284
Cdd:cd17572    78 --AH-GSVDIAVEAmrlGAYDFLEKPFDADRLRVTVR 111
PRK04841 PRK04841
HTH-type transcriptional regulator MalT;
313-364 9.58e-05

HTH-type transcriptional regulator MalT;


Pssm-ID: 235315 [Multi-domain]  Cd Length: 903  Bit Score: 44.55  E-value: 9.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2279496592 313 REREILELIAKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQATAEA 364
Cdd:PRK04841  842 REWQVLGLIYSGYSNEQIAGELDVAATTIKTHIRNLYQKLGIAHRQEAVQHA 893
PRK15347 PRK15347
two component system sensor kinase;
151-283 1.25e-04

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 44.25  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 151 PGRPWA----------SRQTTAAPLMTPPLTVLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVL 220
Cdd:PRK15347  662 PGRLYDllqqiiqgapNEPVINLPLQPWQLQILLVDDVETNRDIIGMMLVELG--QQVTTAASGTEALELGRQHRFDLVL 739
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2279496592 221 MDLQLPGITGVQATAILRAH----DPQARILVYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTAL 283
Cdd:PRK15347  740 MDIRMPGLDGLETTQLWRDDpnnlDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARAL 806
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
8-105 1.83e-04

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 42.97  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592   8 SELRVPSRENADLVAALQAIVDEH-PLGCGPVLKLEVSGPMPPLPSRT-VHHLRMIAREGVTNALKHARAG-CIRLSLGV 84
Cdd:COG0642   172 AGKLELEPEPVDLAELLEEVVELFrPLAEEKGIELELDLPDDLPTVRGdPDRLRQVLLNLLSNAIKYTPEGgTVTVSVRR 251
                          90       100
                  ....*....|....*....|.
gi 2279496592  85 EGSRLRMTIADDGQGFDAEAL 105
Cdd:COG0642   252 EGDRVRISVEDTGPGIPPEDL 272
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
57-105 1.93e-04

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 40.43  E-value: 1.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2279496592  57 HLRMIAREGVTNALKHA-RAGCIRLSLgVEGSRLRMTIADDGQGFDAEAL 105
Cdd:pfam02518   5 RLRQVLSNLLDNALKHAaKAGEITVTL-SEGGELTLTVEDNGIGIPPEDL 53
ompR PRK09468
osmolarity response regulator; Provisional
172-286 2.72e-04

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 41.88  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEG-DVKVVGEAKRGEDAL--EVYQLrqpgVVLmDLQLPGITGVQATAILRAHDPQARILV 248
Cdd:PRK09468    8 ILVVDDDMRLRALLERYLTEQGfQVRSAANAEQMDRLLtrESFHL----MVL-DLMLPGEDGLSICRRLRSQNNPTPIIM 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2279496592 249 YStfAHDDEVQ--MALDAGAAGYLQKTASRDELLTALRRV 286
Cdd:PRK09468   83 LT--AKGEEVDriVGLEIGADDYLPKPFNPRELLARIRAV 120
PRK10610 PRK10610
chemotaxis protein CheY;
170-272 2.77e-04

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 40.34  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 170 LTVLIVDDHFVVRSGLAAALEVEGdVKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQAR--IL 247
Cdd:PRK10610    6 LKFLVVDDFSTMRRIVRNLLKELG-FNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSAlpVL 84
                          90       100
                  ....*....|....*....|....*
gi 2279496592 248 VYSTFAHDDEVQMALDAGAAGYLQK 272
Cdd:PRK10610   85 MVTAEAKKENIIAAAQAGASGYVVK 109
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
172-284 2.95e-04

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: 40.05  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEG-DVKVVGeakRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYS 250
Cdd:cd19939     2 ILIVEDELELARLTRDYLIKAGlEVSVFT---DGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHSHVPILMLTA 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2279496592 251 TFAHDDEVqMALDAGAAGYLQKTASRDELLTALR 284
Cdd:cd19939    79 RTEEMDRV-LGLEMGADDYLCKPFSPRELLARVR 111
PRK10188 PRK10188
transcriptional regulator SdiA;
280-370 3.16e-04

transcriptional regulator SdiA;


Pssm-ID: 182292 [Multi-domain]  Cd Length: 240  Bit Score: 41.69  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 280 LTALRRVAAGGSYLPPELEQRL---------ADLRLCVGISM--------REREILELIAKGHANKQIAALFAISEDTVK 342
Cdd:PRK10188  133 LSFSRCSAREIPILSDELELRLqllvreslmALMRLEDEMVMtpemnfskREKEILKWTAEGKTSAEIAMILSISENTVN 212
                          90       100
                  ....*....|....*....|....*...
gi 2279496592 343 RHVSHILEKLGVHDRAQATAEAIRRGIV 370
Cdd:PRK10188  213 FHQKNMQKKFNAPNKTQIACYAAATGLI 240
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
172-284 3.33e-04

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: 39.96  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALevYQLRQ--PGVVLMDLQLPGITGVQATAILRAHDPQARILVY 249
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAG--YVVDVAEDGEEAL--FQGEEepYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLIL 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2279496592 250 StfAHDDEVQM--ALDAGAAGYLQKTASRDELLTALR 284
Cdd:cd19934    77 T--ARDSWQDKveGLDAGADDYLTKPFHIEELLARLR 111
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
170-306 4.46e-04

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 41.06  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 170 LTVLIVDDHFVVRSGLAAALEVEGDVkvvgeAKRGEDALEVYQLRQPG---VVLMDLQLPGITGVQATAILRAHDPQARI 246
Cdd:PRK09836    1 MKLLIVEDEKKTGEYLTKGLTEAGFV-----VDLADNGLNGYHLAMTGdydLIILDIMLPDVNGWDIVRMLRSANKGMPI 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 247 LVYSTFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRVAAGGSYLPPELEQRLADLRL 306
Cdd:PRK09836   76 LLLTALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGAAVIIESQFQVADLMV 135
PRK15201 PRK15201
fimbriae biosynthesis transcriptional regulator FimW;
311-359 5.58e-04

fimbriae biosynthesis transcriptional regulator FimW;


Pssm-ID: 185123  Cd Length: 198  Bit Score: 40.80  E-value: 5.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2279496592 311 SMREREILELIAKGHANKQIAALFAISEDTVKRHVSHILEKLGVHDRAQ 359
Cdd:PRK15201  135 SVTERHLLKLIASGYHLSETAALLSLSEEQTKSLRRSIMRKLHVKTEQQ 183
PRK04069 PRK04069
serine-protein kinase RsbW; Provisional
64-105 5.91e-04

serine-protein kinase RsbW; Provisional


Pssm-ID: 235217 [Multi-domain]  Cd Length: 161  Bit Score: 39.91  E-value: 5.91e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2279496592  64 EGVTNALKHA----RAGCIRLSLGVEGSRLRMTIADDGQGFDAEAL 105
Cdd:PRK04069   49 EACTNAVQHAykedEVGEIHIRFEIYEDRLEIVVADNGVSFDYETL 94
PRK11517 PRK11517
DNA-binding response regulator HprR;
170-284 5.93e-04

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 40.65  E-value: 5.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 170 LTVLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVY 249
Cdd:PRK11517    1 MKILLIEDNQRTQEWVTQGLSEAG--YVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQTPVICLT 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2279496592 250 STFAHDDEVQmALDAGAAGYLQKTASRDELLTALR 284
Cdd:PRK11517   79 ARDSVDDRVR-GLDSGANDYLVKPFSFSELLARVR 112
PRK10643 PRK10643
two-component system response regulator PmrA;
172-284 1.08e-03

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 40.02  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:PRK10643    3 ILIVEDDTLLLQGLILALQTEG--YACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTA 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2279496592 252 F-AHDDEVQmALDAGAAGYLQKTASRDELLTALR 284
Cdd:PRK10643   81 RdTLEDRVA-GLDVGADDYLVKPFALEELHARIR 113
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
172-266 1.36e-03

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: 37.71  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGdvKVVGEAKRGEDALEVYQLR-QPGVVLMDLQLPG-ITGVQATAILRAHDPQARILVY 249
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLG--YTVLEAASGDEALDLLESGpDIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLT 78
                          90
                  ....*....|....*..
gi 2279496592 250 STFAHDDEVQMALDAGA 266
Cdd:cd18161    79 SGYAENAIEGGDLAPGV 95
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
66-105 1.60e-03

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 40.31  E-value: 1.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2279496592  66 VTNALKHARAG-CIRLSLGVEGSRLRMTIADDGQGFDAEAL 105
Cdd:COG5002   290 LDNAIKYTPEGgTITVSLREEDDQVRISVRDTGIGIPEEDL 330
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
172-286 2.58e-03

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: 37.28  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEG-DVKVVGEakrGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHdPQARILVYS 250
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGfNVRAAHD---GEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKT-SQVPVLMLT 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2279496592 251 TFAHDDEVQMALDAGAAGYLQKTASRDELLTALRRV 286
Cdd:cd17623    77 ARGDDIDRILGLELGADDYLPKPFNPRELVARIRAI 112
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
194-284 2.58e-03

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 38.85  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 194 DVKVVGEAkRGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHdPQARILVYSTFAHDDEVQMALDAGAAGYLQKT 273
Cdd:PRK10701   25 DIDVTVEP-RGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPK-WQGPIVLLTSLDSDMNHILALEMGACDYILKT 102
                          90
                  ....*....|.
gi 2279496592 274 ASRDELLTALR 284
Cdd:PRK10701  103 TPPAVLLARLR 113
dpiA PRK10046
two-component response regulator DpiA; Provisional
166-285 2.61e-03

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 38.85  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 166 MTPPLTVLIVDDHFVVRSGLAAAL-EVEG--DVKVVGEAKRGEDALEVYqlrQPGVVLMDLQLP---GITGVQatAILRA 239
Cdd:PRK10046    1 MTAPLTLLIVEDETPLAEMHAEYIrHIPGfsQILLAGNLAQARMMIERF---KPGLILLDNYLPdgrGINLLH--ELVQA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2279496592 240 HDPQAriLVYSTFAHDDE-VQMALDAGAAGYLQKTASRDELLTALRR 285
Cdd:PRK10046   76 HYPGD--VVFTTAASDMEtVSEAVRCGVFDYLIKPIAYERLGQTLTR 120
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
68-106 2.71e-03

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 39.62  E-value: 2.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2279496592  68 NALKHA-----RAGCIRLSLGVEGSRLRMTIADDGQGFDAEALH 106
Cdd:COG2972   347 NAIEHGiepkeGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLE 390
sigma70-ECF TIGR02937
RNA polymerase sigma factor, sigma-70 family; This model encompasses all varieties of the ...
235-352 2.91e-03

RNA polymerase sigma factor, sigma-70 family; This model encompasses all varieties of the sigma-70 type sigma factors including the ECF subfamily. A number of sigma factors have names with a different number than 70 (i.e. sigma-38), but in fact, all except for the Sigma-54 family (TIGR02395) are included within this family. Several Pfam models hit segments of these sequences including Sigma-70 region 2 (pfam04542) and Sigma-70, region 4 (pfam04545), but not always above their respective trusted cutoffs.


Pssm-ID: 274357 [Multi-domain]  Cd Length: 158  Bit Score: 38.10  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 235 AILRAHDPQARILVYSTF----AHDDEVQMAL------------DAGAAGYLQKTAsRDELLTALRRVAAGGSYLPPELE 298
Cdd:TIGR02937   5 ELYERYLPLVYRYARRYLgddaDAEDLVQEAFlkllealdrfdpEGSFKAWLFRIA-RNLILDYLRRKRRLRRELDLLEE 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2279496592 299 ---------------QRLADLRLCV-GISMREREILELIA-KGHANKQIAALFAISEDTVKRHVSHILEKL 352
Cdd:TIGR02937  84 lldsdpspeeeleqeEEREALREALeKLPEREREVLVLRYlEGLSYKEIAEILGISVGTVKRRLKRARKKL 154
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
172-272 3.37e-03

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: 36.65  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEG-DVKVVGEakrGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYS 250
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGfSVETYTD---GASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKSTLPVIFLTS 77
                          90       100
                  ....*....|....*....|....
gi 2279496592 251 tfaHDDEVQ--MALDAGAAGYLQK 272
Cdd:cd19936    78 ---KDDEIDevFGLRMGADDYITK 98
Sigma70_r4_2 pfam08281
Sigma-70, region 4; Region 4 of sigma-70 like sigma-factors are involved in binding to the -35 ...
313-352 5.30e-03

Sigma-70, region 4; Region 4 of sigma-70 like sigma-factors are involved in binding to the -35 promoter element via a helix-turn-helix motif.


Pssm-ID: 400535 [Multi-domain]  Cd Length: 54  Bit Score: 34.74  E-value: 5.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2279496592 313 REREILELIA-KGHANKQIAALFAISEDTVKRHVSHILEKL 352
Cdd:pfam08281  14 RQREVFLLRYlEGLSYAEIAELLGISEGTVKSRLSRARKKL 54
RpoE COG1595
DNA-directed RNA polymerase specialized sigma subunit, sigma24 family [Transcription]; ...
269-352 5.47e-03

DNA-directed RNA polymerase specialized sigma subunit, sigma24 family [Transcription]; DNA-directed RNA polymerase specialized sigma subunit, sigma24 family is part of the Pathway/BioSystem: RNA polymerase


Pssm-ID: 441203 [Multi-domain]  Cd Length: 181  Bit Score: 37.67  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 269 YLQKTASRDELLTALRRVAAGGSYLP---PELEQRLADLRLCVG-ISMREREILELIA-KGHANKQIAALFAISEDTVKR 343
Cdd:COG1595    83 HLRKRRRRRELLDELAEELPDEAADPeeaLEAEELLEALLAALErLPPRQREVLVLRYlEGLSYAEIAEILGISEGTVKS 162

                  ....*....
gi 2279496592 344 HVSHILEKL 352
Cdd:COG1595   163 RLSRARKKL 171
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
4-106 5.97e-03

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


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 38.40  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592   4 RSLVSELR------VPSRENADLVAALQAIVD---EHPLGCGPVLKLEVSGPMPPLP------SRTVHHLrmiaregVTN 68
Cdd:COG5000   256 KRIVDEFLdfarlpEPQLEPVDLNELLREVLAlyePALKEKDIRLELDLDPDLPEVLadrdqlEQVLINL-------LKN 328
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2279496592  69 ALKH-ARAGCIRLSLGVEGSRLRMTIADDGQGFDAEALH 106
Cdd:COG5000   329 AIEAiEEGGEIEVSTRREDGRVRIEVSDNGPGIPEEVLE 367
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
172-285 7.29e-03

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 38.31  E-value: 7.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGDVKVVGEAkrGEDALEVYQLRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:PRK10923    6 VWVVDDDSSIRWVLERALAGAGLTCTTFEN--GNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTA 83
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2279496592 252 FAHDDEVQMALDAGAAGYLQKTASRDELLTALRR 285
Cdd:PRK10923   84 HSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVER 117
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
172-286 7.45e-03

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 37.47  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592 172 VLIVDDHFVVRSGLAAALEVEGDVKVVgeAKRGEDALEVYQlRQPGVVLMDLQLPGITGVQATAILRAHDPQARILVYST 251
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLEMEGFNVIV--AHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELRQTHQTPVIMLTAR 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2279496592 252 FAHDDEVqMALDAGAAGYLQKTASRDELLTALRRV 286
Cdd:PRK10955   81 GSELDRV-LGLELGADDYLPKPFNDRELVARIRAI 114
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
66-143 8.57e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA, YehU, Bacillus subtilis LytS, and some hybrid sensor histidine kinases; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. It also includes the HATPase domains of Escherichia coli YpdA and YehU, HKs of YpdA-YpdB and YehU-YehTCSs, which are involved together in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), some having accessory sensor domain(s) such as Cache, HAMP or GAF; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340401 [Multi-domain]  Cd Length: 103  Bit Score: 35.50  E-value: 8.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279496592  66 VTNALKHA-----RAGCIRLSLGVEGSRLRMTIADDGQGFDAEALHGG-----QRGHFGCIGIEERCAKFGGIASGVLRR 135
Cdd:cd16924    10 VENAIQHGlspltDKGVVTISALKEDNHVMIEVEDNGRGIDPKVLNILgkkpkEGNGIGLYNVHQRLILLFGEDYGIHIA 89

                  ....*...
gi 2279496592 136 AGHHPGDR 143
Cdd:cd16924    90 SEPDKGTR 97
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
66-105 9.80e-03

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


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 35.50  E-value: 9.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2279496592  66 VTNALKHARaGCIRLSLGVEGSRLRMTIADDGQGFDAEAL 105
Cdd:cd16950     9 VDNALRYGG-GWVEVSSDGEGNRTRIQVLDNGPGIAPEEV 47
 
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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