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Conserved domains on  [gi|1889634278|ref|WP_182721303|]
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MULTISPECIES: response regulator [unclassified Pseudoalteromonas]

Protein Classification

response regulator( domain architecture ID 13127340)

response regulator containing a DUF3369 domain, with similarity to RpfG, a cyclic di-GMP phosphodiesterase that positively regulates virulence factor synthesis and negatively regulates biofilm formation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
 293-511 1.40e-67

HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms];


:

Pssm-ID: 441808 [Multi-domain]  Cd Length: 316  Bit Score: 220.23  E-value: 1.40e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 293 QRHLIKIFSQ-NVQLAFENVQLQSEIEATQQELVYRLSEAVEQRSTETGNHVKRVAHICHILAEGYGLSKHDADLVRLAS 371
Cdd:COG2206    97 ESLLAELFEElRLGLLEELKKLVEELDELLPDALLALLAALDAKDPYTYGHSVRVAVLALALARELGLSEEELEDLGLAA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 372 PLHDVGKVGIPDAILNKPAKLEPQEWEVMKTHTDKGYTILKDSPHeiVSTGAIIAKEHHEKWDGSGYPQGLSGNAINVFG 451
Cdd:COG2206   177 LLHDIGKIGIPDEILNKPGKLTDEEFEIIKKHPEYGYEILKKLPG--LSEVAEIVLQHHERLDGSGYPRGLKGEEIPLLA 254

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 452 RIVALADVYDALRHKRCYKEPWTLQNVVDEINAEKGTHFEPKMVEVFNEKLDELEAVLSR 511
Cdd:COG2206   255 RILAVADVYDALTSDRPYRKALSPEEALEELRKGAGTQFDPELVEAFIKVLGIYPPVVEI 314
DUF3369 pfam11849
Domain of unknown function (DUF3369); This domain is functionally uncharacterized. This domain ...
 145-317 5.08e-50

Domain of unknown function (DUF3369); This domain is functionally uncharacterized. This domain is found in bacteria. This presumed domain is about 170 amino acids in length. The domain appears to be related to the GAF domain.


:

Pssm-ID: 432127 [Multi-domain]  Cd Length: 168  Bit Score: 168.87  E-value: 5.08e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 145 IMSSLRSYRDIISIEQSREGLEKIIVASRDIFSAHSIEHFIEGVMQQLTSLLGIADQAMYattlVAQNPEHEKNKKLIVC 224
Cdd:pfam11849   1 VTAALRSYRDLRTIERSRRGLEKIIEASADLFELRSLQEFAEGVLTQLAALLNLKKDGLV----CVSSGIAAASGNFYVL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 225 SGTGDFEKSEGKELDEVLQAEQLSACHQALNDKSIIYKDNYLFAYCSSEYNHNSMLFISGvPKDLTDTQRHLIKIFSQNV 304
Cdd:pfam11849  77 AATGKFESLIGKPLSDLLDPEVRELLERALASKRSIFEDDYVGLYFRTSSGSEGVIYLET-TRPLSELDRELLEVFCNNI 155

                         170
                  ....*....|...
gi 1889634278 305 QLAFENVQLQSEI 317
Cdd:pfam11849 156 SVAFDNVYLNEEL 168
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 23-161 2.41e-19

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


:

Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 84.25  E-value: 2.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  23 WKVLIVDDEPEVHAVTKLALSDFEFQNkrlEFISAYSGAEAKELIKEH-PDaaIVLLDVVMEtDDAGLQVAKFIREEakN 101
Cdd:COG4565     4 IRVLIVEDDPMVAELLRRYLERLPGFE---VVGVASSGEEALALLAEHrPD--LILLDIYLP-DGDGLELLRELRAR--G 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 102 NHIRIILRTGQPGQAPERQViINYDINDYKSKtELTAQKLFTVImSSLRSYRDIISIEQS 161
Cdd:COG4565    76 PDVDVIVITAARDPETVREA-LRAGVVDYLIK-PFTFERLREAL-ERYLEYRRLLREDQE 132
 
Name Accession Description Interval E-value
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
 293-511 1.40e-67

HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms];


Pssm-ID: 441808 [Multi-domain]  Cd Length: 316  Bit Score: 220.23  E-value: 1.40e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 293 QRHLIKIFSQ-NVQLAFENVQLQSEIEATQQELVYRLSEAVEQRSTETGNHVKRVAHICHILAEGYGLSKHDADLVRLAS 371
Cdd:COG2206    97 ESLLAELFEElRLGLLEELKKLVEELDELLPDALLALLAALDAKDPYTYGHSVRVAVLALALARELGLSEEELEDLGLAA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 372 PLHDVGKVGIPDAILNKPAKLEPQEWEVMKTHTDKGYTILKDSPHeiVSTGAIIAKEHHEKWDGSGYPQGLSGNAINVFG 451
Cdd:COG2206   177 LLHDIGKIGIPDEILNKPGKLTDEEFEIIKKHPEYGYEILKKLPG--LSEVAEIVLQHHERLDGSGYPRGLKGEEIPLLA 254

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 452 RIVALADVYDALRHKRCYKEPWTLQNVVDEINAEKGTHFEPKMVEVFNEKLDELEAVLSR 511
Cdd:COG2206   255 RILAVADVYDALTSDRPYRKALSPEEALEELRKGAGTQFDPELVEAFIKVLGIYPPVVEI 314
DUF3369 pfam11849
Domain of unknown function (DUF3369); This domain is functionally uncharacterized. This domain ...
 145-317 5.08e-50

Domain of unknown function (DUF3369); This domain is functionally uncharacterized. This domain is found in bacteria. This presumed domain is about 170 amino acids in length. The domain appears to be related to the GAF domain.


Pssm-ID: 432127 [Multi-domain]  Cd Length: 168  Bit Score: 168.87  E-value: 5.08e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 145 IMSSLRSYRDIISIEQSREGLEKIIVASRDIFSAHSIEHFIEGVMQQLTSLLGIADQAMYattlVAQNPEHEKNKKLIVC 224
Cdd:pfam11849   1 VTAALRSYRDLRTIERSRRGLEKIIEASADLFELRSLQEFAEGVLTQLAALLNLKKDGLV----CVSSGIAAASGNFYVL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 225 SGTGDFEKSEGKELDEVLQAEQLSACHQALNDKSIIYKDNYLFAYCSSEYNHNSMLFISGvPKDLTDTQRHLIKIFSQNV 304
Cdd:pfam11849  77 AATGKFESLIGKPLSDLLDPEVRELLERALASKRSIFEDDYVGLYFRTSSGSEGVIYLET-TRPLSELDRELLEVFCNNI 155

                         170
                  ....*....|...
gi 1889634278 305 QLAFENVQLQSEI 317
Cdd:pfam11849 156 SVAFDNVYLNEEL 168
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 339-477 1.10e-23

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 97.02  E-value: 1.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 339 TGNHVKRVAHICHILAEGYGLSKHDADLVRLASPLHDVGKVGIPDAILNkpaklepQEWEVMKTHTDKGYTILKDS---- 414
Cdd:cd00077     3 RFEHSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAITE-------EESELEKDHAIVGAEILRELllee 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889634278 415 -PHEIVSTGAIIAKEHHEKWDGSGYPQGLSGNAINVFGRIVALADVYDALR----HKRCYKEPWTLQN 477
Cdd:cd00077    76 vIKLIDELILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRrdsrEKRRRIAEEDLEE 143
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 23-161 2.41e-19

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 84.25  E-value: 2.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  23 WKVLIVDDEPEVHAVTKLALSDFEFQNkrlEFISAYSGAEAKELIKEH-PDaaIVLLDVVMEtDDAGLQVAKFIREEakN 101
Cdd:COG4565     4 IRVLIVEDDPMVAELLRRYLERLPGFE---VVGVASSGEEALALLAEHrPD--LILLDIYLP-DGDGLELLRELRAR--G 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 102 NHIRIILRTGQPGQAPERQViINYDINDYKSKtELTAQKLFTVImSSLRSYRDIISIEQS 161
Cdd:COG4565    76 PDVDVIVITAARDPETVREA-LRAGVVDYLIK-PFTFERLREAL-ERYLEYRRLLREDQE 132
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 339-463 2.20e-17

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 77.66  E-value: 2.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 339 TGNHVKRVAHICHILAEGYGLSkhDADLVRLASPLHDVGKVGIPDAIlnkpaklepQEWEVMKTHTDKGYTILKDSPH-E 417
Cdd:pfam01966   1 RLEHSLRVALLARELAEELGEL--DRELLLLAALLHDIGKGPFGDEK---------PEFEIFLGHAVVGAEILRELEKrL 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1889634278 418 IVSTGAIIAKEHHEKWDGSGYPqglsgNAINVFGRIVALADVYDAL 463
Cdd:pfam01966  70 GLEDVLKLILEHHESWEGAGYP-----EEISLEARIVKLADRLDAL 110
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 339-471 9.87e-16

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 73.48  E-value: 9.87e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  339 TGNHVKRVAHICHILAEGYGLskHDADLVRLASPLHDVGKVGIPDAILNKPaklepqewEVMKTHTDKGYTILKDSPH-- 416
Cdd:smart00471   5 VFEHSLRVAQLAAALAEELGL--LDIELLLLAALLHDIGKPGTPDSFLVKT--------SVLEDHHFIGAEILLEEEEpr 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1889634278  417 EIVSTGAIIAKEHHEKWDgsgypqGLSGNAINVFGRIVALADVYDALRHKRCYKE 471
Cdd:smart00471  75 ILEEILRTAILSHHERPD------GLRGEPITLEARIVKVADRLDALRADRRYRR 123
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
 24-120 1.32e-09

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 56.02  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFefqnKRLEFISAYSGAEAKELIKEH-PDAaiVLLDVVMETDDaGLQVAKFIREEAKNN 102
Cdd:cd17552     3 RILVIDDEEDIREVVQACLEKL----AGWEVLTASSGQEGLEKAATEqPDA--ILLDVMMPDMD-GLATLKKLQANPETQ 75

                          90
                  ....*....|....*...
gi 1889634278 103 HIRIILRTGQpGQAPERQ 120
Cdd:cd17552    76 SIPVILLTAK-AQPSDRQ 92
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 25-133 5.70e-09

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: 53.69  E-value: 5.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  25 VLIVDDEPEVHAVTKLALSDFEFqnkrlEFISAYSGAEAKELIKEH-PDaaIVLLDVVMETDDaGLQVAKFIREEakNNH 103
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGY-----VVAEADDGKEALELLKEErPD--LILLDINMPGMD-GLELLKRIRRR--DPT 70

                          90       100       110
                  ....*....|....*....|....*....|
gi 1889634278 104 IRIILRTGQpGQAPERQVIINYDINDYKSK 133
Cdd:pfam00072  71 TPVIILTAH-GDEDDAVEALEAGADDFLSK 99
PRK13557 PRK13557
histidine kinase; Provisional
 8-119 2.03e-06

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 50.44  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278   8 SDEPEETIDEIE-HGTWKVLIVDDEPEVHAVTKLALSDFEFqnkRLEfiSAYSGAEAKELIKEHPDAAIVLLDVVMETDD 86
Cdd:PRK13557  400 NPEQEPKARAIDrGGTETILIVDDRPDVAELARMILEDFGY---RTL--VASNGREALEILDSHPEVDLLFTDLIMPGGM 474

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1889634278  87 AGLQVAKfireEAKNNH--IRIILRTGQPGQAPER 119
Cdd:PRK13557  475 NGVMLAR----EARRRQpkIKVLLTTGYAEASIER 505
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 24-82 1.41e-05

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: 42.56  E-value: 1.41e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278   24 KVLIVDDEPEVHAVTKLALSDFEFqnkrlEFISAYSGAEAKELIKEH-PDaaIVLLDVVM 82
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGY-----EVDEATDGEEALELLKEEkPD--LILLDIMM 54
 
Name Accession Description Interval E-value
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
 293-511 1.40e-67

HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms];


Pssm-ID: 441808 [Multi-domain]  Cd Length: 316  Bit Score: 220.23  E-value: 1.40e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 293 QRHLIKIFSQ-NVQLAFENVQLQSEIEATQQELVYRLSEAVEQRSTETGNHVKRVAHICHILAEGYGLSKHDADLVRLAS 371
Cdd:COG2206    97 ESLLAELFEElRLGLLEELKKLVEELDELLPDALLALLAALDAKDPYTYGHSVRVAVLALALARELGLSEEELEDLGLAA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 372 PLHDVGKVGIPDAILNKPAKLEPQEWEVMKTHTDKGYTILKDSPHeiVSTGAIIAKEHHEKWDGSGYPQGLSGNAINVFG 451
Cdd:COG2206   177 LLHDIGKIGIPDEILNKPGKLTDEEFEIIKKHPEYGYEILKKLPG--LSEVAEIVLQHHERLDGSGYPRGLKGEEIPLLA 254

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 452 RIVALADVYDALRHKRCYKEPWTLQNVVDEINAEKGTHFEPKMVEVFNEKLDELEAVLSR 511
Cdd:COG2206   255 RILAVADVYDALTSDRPYRKALSPEEALEELRKGAGTQFDPELVEAFIKVLGIYPPVVEI 314
DUF3369 pfam11849
Domain of unknown function (DUF3369); This domain is functionally uncharacterized. This domain ...
 145-317 5.08e-50

Domain of unknown function (DUF3369); This domain is functionally uncharacterized. This domain is found in bacteria. This presumed domain is about 170 amino acids in length. The domain appears to be related to the GAF domain.


Pssm-ID: 432127 [Multi-domain]  Cd Length: 168  Bit Score: 168.87  E-value: 5.08e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 145 IMSSLRSYRDIISIEQSREGLEKIIVASRDIFSAHSIEHFIEGVMQQLTSLLGIADQAMYattlVAQNPEHEKNKKLIVC 224
Cdd:pfam11849   1 VTAALRSYRDLRTIERSRRGLEKIIEASADLFELRSLQEFAEGVLTQLAALLNLKKDGLV----CVSSGIAAASGNFYVL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 225 SGTGDFEKSEGKELDEVLQAEQLSACHQALNDKSIIYKDNYLFAYCSSEYNHNSMLFISGvPKDLTDTQRHLIKIFSQNV 304
Cdd:pfam11849  77 AATGKFESLIGKPLSDLLDPEVRELLERALASKRSIFEDDYVGLYFRTSSGSEGVIYLET-TRPLSELDRELLEVFCNNI 155

                         170
                  ....*....|...
gi 1889634278 305 QLAFENVQLQSEI 317
Cdd:pfam11849 156 SVAFDNVYLNEEL 168
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 339-477 1.10e-23

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 97.02  E-value: 1.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 339 TGNHVKRVAHICHILAEGYGLSKHDADLVRLASPLHDVGKVGIPDAILNkpaklepQEWEVMKTHTDKGYTILKDS---- 414
Cdd:cd00077     3 RFEHSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAITE-------EESELEKDHAIVGAEILRELllee 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889634278 415 -PHEIVSTGAIIAKEHHEKWDGSGYPQGLSGNAINVFGRIVALADVYDALR----HKRCYKEPWTLQN 477
Cdd:cd00077    76 vIKLIDELILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRrdsrEKRRRIAEEDLEE 143
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 361-437 6.34e-21

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


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 91.38  E-value: 6.34e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889634278 361 KHDADLVRLASPLHDVGKVGIPDAILNKPAKLEPQEWEVMKTHTdkGYTILKDSPHEIVSTGAIIakehHEKWDGSG 437
Cdd:COG3437   134 DDLVLYLKLAAPLHDIGKIGIPDAILLKPGKLTPEEWEITHAHI--GAEILSGSLLPLLQLAAEI----HERWDGSG 204
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 23-161 2.41e-19

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 84.25  E-value: 2.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  23 WKVLIVDDEPEVHAVTKLALSDFEFQNkrlEFISAYSGAEAKELIKEH-PDaaIVLLDVVMEtDDAGLQVAKFIREEakN 101
Cdd:COG4565     4 IRVLIVEDDPMVAELLRRYLERLPGFE---VVGVASSGEEALALLAEHrPD--LILLDIYLP-DGDGLELLRELRAR--G 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 102 NHIRIILRTGQPGQAPERQViINYDINDYKSKtELTAQKLFTVImSSLRSYRDIISIEQS 161
Cdd:COG4565    76 PDVDVIVITAARDPETVREA-LRAGVVDYLIK-PFTFERLREAL-ERYLEYRRLLREDQE 132
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 339-463 2.20e-17

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 77.66  E-value: 2.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 339 TGNHVKRVAHICHILAEGYGLSkhDADLVRLASPLHDVGKVGIPDAIlnkpaklepQEWEVMKTHTDKGYTILKDSPH-E 417
Cdd:pfam01966   1 RLEHSLRVALLARELAEELGEL--DRELLLLAALLHDIGKGPFGDEK---------PEFEIFLGHAVVGAEILRELEKrL 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1889634278 418 IVSTGAIIAKEHHEKWDGSGYPqglsgNAINVFGRIVALADVYDAL 463
Cdd:pfam01966  70 GLEDVLKLILEHHESWEGAGYP-----EEISLEARIVKLADRLDAL 110
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 339-471 9.87e-16

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 73.48  E-value: 9.87e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  339 TGNHVKRVAHICHILAEGYGLskHDADLVRLASPLHDVGKVGIPDAILNKPaklepqewEVMKTHTDKGYTILKDSPH-- 416
Cdd:smart00471   5 VFEHSLRVAQLAAALAEELGL--LDIELLLLAALLHDIGKPGTPDSFLVKT--------SVLEDHHFIGAEILLEEEEpr 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1889634278  417 EIVSTGAIIAKEHHEKWDgsgypqGLSGNAINVFGRIVALADVYDALRHKRCYKE 471
Cdd:smart00471  75 ILEEILRTAILSHHERPD------GLRGEPITLEARIVKVADRLDALRADRRYRR 123
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 24-153 3.26e-15

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: 72.19  E-value: 3.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFEFqnkrlEFISAYSGAEAKELIKEH-PDaaIVLLDVVM-ETDdaGLQVAKFIREEAKN 101
Cdd:COG0784     7 RILVVDDNPDNRELLRRLLERLGY-----EVTTAEDGAEALELLRAGpPD--LILLDINMpGMD--GLELLRRIRALPRL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1889634278 102 NHIRIILRTGQPGQApERQVIINYDINDYKSKTeLTAQKLFTVIMSSLRSYR 153
Cdd:COG0784    78 PDIPIIALTAYADEE-DRERALEAGADDYLTKP-VDPEELLEALRRLLARAS 127
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 22-205 7.16e-14

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: 69.94  E-value: 7.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  22 TWKVLIVDDEPEVHAVTKLALSDFEFqnkrlEFISAYSGAEAKELIKEH-PDaaIVLLDVVM-ETDdaGLQVAKFIREEA 99
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAGY-----EVVEAADGEEALELLQEHrPD--LILLDLEMpDMD--GLELCRRLRADP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 100 KNNHIRIILRTGQPGQApERQVIINYDINDYKSK----TELTAQ---------KLFTVIMSSlrsyrdiISIEQSREGLE 166
Cdd:COG3706    72 RTADIPIIFLTALDDEE-DRARALEAGADDYLTKpfdpEELLARvdlvaryggEEFAILLPG-------TDLEGALAVAE 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1889634278 167 KIIVASRDIFSAH---SIehfieGVMQqlTSLLGIADqAMYA 205
Cdd:COG3706   144 RIREAVAELPSLRvtvSI-----GVAG--DSLLKRAD-ALYQ 177
HD_5 pfam13487
HD domain; HD domains are metal dependent phosphohydrolases.
 391-453 6.55e-12

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 433249 [Multi-domain]  Cd Length: 64  Bit Score: 60.69  E-value: 6.55e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889634278 391 KLEPQEWEVMKTHTDKGYTILKDSPHeIVSTGAIIAKEHHEKWDGSGYPQGLSGNAINVFGRI 453
Cdd:pfam13487   2 TLTPEEREIINRHPEHTARLLSTLPR-LPKEVAEIIAQHHERLDGSGYPRGLKGEEIPLGARI 63
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
 24-130 2.19e-10

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


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 57.48  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFE-FQnkrlEFISAYSGAEAKELIKEH-PDaaIVLLDVVM-ETDdaGLQVAKFIREEak 100
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEAgFE----VVGEAENGEEALELLEEHkPD--LVITDINMpGMD--GLELLEAIREL-- 70

                          90       100       110
                  ....*....|....*....|....*....|
gi 1889634278 101 NNHIRIILRTGQPGQAPERQViINYDINDY 130
Cdd:COG4753    71 DPDTKIIILSGYSDFEYAQEA-IKLGADDY 99
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
 24-108 9.02e-10

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: 58.43  E-value: 9.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFEFqnkrlEFISAYSGAEAKELIKEH-PDaaIVLLDVVMETDDaGLQVAKFIREEAKnn 102
Cdd:COG0745     3 RILVVEDDPDIRELLADALEREGY-----EVDTAADGEEALELLEEErPD--LILLDLMLPGMD-GLEVCRRLRARPS-- 72


                  ....*.
gi 1889634278 103 HIRIIL 108
Cdd:COG0745    73 DIPIIM 78
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
 24-120 1.32e-09

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 56.02  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFefqnKRLEFISAYSGAEAKELIKEH-PDAaiVLLDVVMETDDaGLQVAKFIREEAKNN 102
Cdd:cd17552     3 RILVIDDEEDIREVVQACLEKL----AGWEVLTASSGQEGLEKAATEqPDA--ILLDVMMPDMD-GLATLKKLQANPETQ 75

                          90
                  ....*....|....*...
gi 1889634278 103 HIRIILRTGQpGQAPERQ 120
Cdd:cd17552    76 SIPVILLTAK-AQPSDRQ 92
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 26-111 1.46e-09

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: 55.31  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  26 LIVDDEPEVHAVTKLALSDFEFqnkrlEFISAYSGAEAKELIKEH-PDaaIVLLDVVMETDDaGLQVAKFIREEAKnnHI 104
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGY-----EVDTAADGEEALELLREErPD--LVLLDLMMPGMD-GLELLRKLRELPP--DI 70


                  ....*..
gi 1889634278 105 RIILRTG 111
Cdd:cd00156    71 PVIVLTA 77
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
 24-110 2.31e-09

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: 54.81  E-value: 2.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSdfefqNKRLEFISAYSGAEAKELIKEH-PDaaIVLLDVVMETDDaGLQVAKFIREEAKNN 102
Cdd:cd17538     1 KILVVDDEPANRELLEALLS-----AEGYEVLTADSGQEALALAEEElPD--LILLDVMMPGMD-GFEVCRRLKEDPETR 72


                  ....*...
gi 1889634278 103 HIRIILRT 110
Cdd:cd17538    73 HIPVIMIT 80
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 24-112 3.01e-09

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: 58.82  E-value: 3.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFEFqnkrlEFISAYSGAEAKELIKEHPdAAIVLLDVVMEtDDAGLQVAKFIREEakNNH 103
Cdd:COG2204     4 RILVVDDDPDIRRLLKELLERAGY-----EVETAASGEEALALLREEP-PDLVLLDLRMP-GMDGLELLRELRAL--DPD 74


                  ....*....
gi 1889634278 104 IRIILRTGQ 112
Cdd:COG2204    75 LPVILLTGY 83
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
 25-122 5.00e-09

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 53.89  E-value: 5.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  25 VLIVDDEPEVHAVTKLALSDFEFQnkrleFISAYSGAEAKELIKEHPDAAIVLLDVVMETDDAGLQVAKFIReeAKNNHI 104
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYT-----VLEAASGDEALDLLESGPDIDLLVTDVIMPGGMNGSQLAEEAR--RRRPDL 73

                          90       100
                  ....*....|....*....|....*
gi 1889634278 105 RIILRTGQ-------PGQAPERQVI 122
Cdd:cd18161    74 KVLLTSGYaenaiegGDLAPGVDVL 98
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 25-133 5.70e-09

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: 53.69  E-value: 5.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  25 VLIVDDEPEVHAVTKLALSDFEFqnkrlEFISAYSGAEAKELIKEH-PDaaIVLLDVVMETDDaGLQVAKFIREEakNNH 103
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGY-----VVAEADDGKEALELLKEErPD--LILLDINMPGMD-GLELLKRIRRR--DPT 70

                          90       100       110
                  ....*....|....*....|....*....|
gi 1889634278 104 IRIILRTGQpGQAPERQVIINYDINDYKSK 133
Cdd:pfam00072  71 TPVIILTAH-GDEDDAVEALEAGADDFLSK 99
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
 26-108 8.39e-08

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: 50.10  E-value: 8.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  26 LIVDDEPEVHAVTKLALSDFEFqnkrlEFISAYSGAEAKELIKEH-PDaaIVLLDVVM-ETDdaGLQVAKFIREeaKNNH 103
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGY-----EVDTAADGEEALELAREEqPD--LIILDVMLpGMD--GFEVCRRLRE--KGSD 69


                  ....*
gi 1889634278 104 IRIIL 108
Cdd:cd17574    70 IPIIM 74
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
 24-108 4.82e-07

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 50.97  E-value: 4.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFEFqnkrLEFI-SAYSGAEAKELIKEH-PDaaIVLLDVVMEtDDAGLQVAKFIREeaKN 101
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKYPD----LEVVgEASNGEEALELLEEHkPD--LVFLDIQMP-GLDGFELARQLRE--LD 73


                  ....*..
gi 1889634278 102 NHIRIIL 108
Cdd:COG3279    74 PPPPIIF 80
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
 25-111 5.33e-07

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


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 48.49  E-value: 5.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  25 VLIVDDEPEV-HAVTKLalsdfeFQNKRLEF---ISAYSGAEAKELIKEH-PDaaIVLLDVVM-ETDdaGLQVAKFIREe 98
Cdd:cd17536     1 VLIVDDEPLIrEGLKKL------IDWEELGFevvGEAENGEEALELIEEHkPD--IVITDIRMpGMD--GLELIEKIRE- 69

                          90
                  ....*....|...
gi 1889634278  99 aKNNHIRIILRTG 111
Cdd:cd17536    70 -LYPDIKIIILSG 81
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
 25-145 5.50e-07

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: 48.23  E-value: 5.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  25 VLIVDDEPEVHAVTKLALSDFEFQnkrleFISAYSGAEAKELIKEHPDaAIVLLDVVM-ETDdaGLQVAKFIRE-EAKNN 102
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYE-----VDVAENGQEALELLKEEPF-DLVLMDLQMpVMD--GLEATRRIRElEGGGR 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1889634278 103 HIRIILRTGQpGQAPERQVIINYDINDYKSKTeLTAQKLFTVI 145
Cdd:cd17546    73 RTPIIALTAN-ALEEDREKCLEAGMDDYLSKP-VKLDQLKEVL 113
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
 341-463 8.59e-07

HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal structure and biogenesis, General function prediction only];


Pssm-ID: 441028 [Multi-domain]  Cd Length: 191  Bit Score: 49.51  E-value: 8.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278 341 NHVKRVAHICHILAEGYGLskhDADLVRLASPLHDVGKVgipdailnkpaklepQEWEVMKTHTDKGYTILKD------- 413
Cdd:COG1418    21 QHSLRVAKLAGLIAAEEGA---DVEVAKRAALLHDIGKA---------------KDHEVEGSHAEIGAELARKyleslgf 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1889634278 414 SPHEIVSTGAIIAKeHHekWDGSGYPQglsgnaiNVFGRIVALADVYDAL 463
Cdd:COG1418    83 PEEEIEAVVHAIEA-HS--FSGGIEPE-------SLEAKIVQDADRLDAL 122
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
 25-111 1.08e-06

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: 47.45  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  25 VLIVDDEPEVHAVTKLALSDFEFqnkrlEFISAYSGAEAKELIKEH-PDaaIVLLDVVMETDDaGLQVAKFIREEAKNNH 103
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGA-----EVTTAHSGEEALEAAQRFrPD--VILSDIGMPGMD-GYELARRLRELPWLAN 72


                  ....*...
gi 1889634278 104 IRIILRTG 111
Cdd:cd17580    73 TPAIALTG 80
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
 24-107 1.92e-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: 46.74  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFEFQnkrleFISAYSGAEAKELIKEHPDAAIVLLDVVM-ETDdaGLQVAKFIREEAKNN 102
Cdd:cd17544     2 KVLVVDDSATSRNHLRALLRRHNFQ-----VLEAANGQEALEVLEQHPDIKLVITDYNMpEMD--GFELVREIRKKYSRD 74


                  ....*
gi 1889634278 103 HIRII 107
Cdd:cd17544    75 QLAII 79
PRK13557 PRK13557
histidine kinase; Provisional
 8-119 2.03e-06

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 50.44  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278   8 SDEPEETIDEIE-HGTWKVLIVDDEPEVHAVTKLALSDFEFqnkRLEfiSAYSGAEAKELIKEHPDAAIVLLDVVMETDD 86
Cdd:PRK13557  400 NPEQEPKARAIDrGGTETILIVDDRPDVAELARMILEDFGY---RTL--VASNGREALEILDSHPEVDLLFTDLIMPGGM 474

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1889634278  87 AGLQVAKfireEAKNNH--IRIILRTGQPGQAPER 119
Cdd:PRK13557  475 NGVMLAR----EARRRQpkIKVLLTTGYAEASIER 505
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
 24-111 2.99e-06

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 47.60  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFEFqnkrlEFISAYSGAEAKELIKEHPdAAIVLLDVVMEtDDAGLQVAKFIREeaKNNH 103
Cdd:COG4567     6 SLLLVDDDEAFARVLARALERRGF-----EVTTAASVEEALALLEQAP-PDYAVLDLRLG-DGSGLDLIEALRE--RDPD 76


                  ....*...
gi 1889634278 104 IRIILRTG 111
Cdd:COG4567    77 ARIVVLTG 84
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
 24-114 3.81e-06

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: 45.67  E-value: 3.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHavtklALSDFEFQNKRLEFISAYSGAEAKELIK-EHPDaaIVLLDVVMETDDaGLQVAKFIREEAKNn 102
Cdd:cd17554     2 KILVVDDEENIR-----ELYKEELEDEGYEVVTAGNGEEALEKLEsEDPD--LVILDIKMPGMD-GLETLRKIREKKPD- 72

                          90
                  ....*....|..
gi 1889634278 103 hIRIILRTGQPG 114
Cdd:cd17554    73 -LPVIICTAYSE 83
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
 24-107 5.05e-06

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: 45.48  E-value: 5.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFEFQNkrleFISAYSGAEAKELIKEH-PDaaIVLLDVVMETDDAGLQVAKFIReeaKNN 102
Cdd:cd17534     2 KILIVEDEAIIALDLKEILESLGYEV----VGIADSGEEAIELAEENkPD--LILMDINLKGDMDGIEAAREIR---EKF 72


                  ....*
gi 1889634278 103 HIRII 107
Cdd:cd17534    73 DIPVI 77
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
 24-111 6.97e-06

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: 45.13  E-value: 6.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEpEVHAVTkLALSdfeFQNKRLEFISAYSGAEAKELIKE-HPDAAIvlLDVVMEtDDAGLQVAKFIREeaKNN 102
Cdd:cd17563     2 SLLLVDDD-EVFAER-LARA---LERRGFEVETAHSVEEALALAREeKPDYAV--LDLRLG-GDSGLDLIPPLRA--LQP 71


                  ....*....
gi 1889634278 103 HIRIILRTG 111
Cdd:cd17563    72 DARIVVLTG 80
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 24-82 1.41e-05

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: 42.56  E-value: 1.41e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278   24 KVLIVDDEPEVHAVTKLALSDFEFqnkrlEFISAYSGAEAKELIKEH-PDaaIVLLDVVM 82
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGY-----EVDEATDGEEALELLKEEkPD--LILLDIMM 54
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
 26-110 1.54e-05

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: 44.19  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  26 LIVDDEPEVhavtkLALSDFEFQNKRLEFISAYSGAEAKELIK-EHPDaaIVLLDVVMETDDaGLQVAKFIREEAKNNHI 104
Cdd:cd19937     1 LVVDDEEDI-----VELLKYNLEKEGYEVVTAYDGEEALKRAKdEKPD--LIILDLMLPGID-GLEVCRILRSDPKTSSI 72


                  ....*.
gi 1889634278 105 RIILRT 110
Cdd:cd19937    73 PIIMLT 78
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
 25-107 2.44e-05

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: 43.65  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  25 VLIVDDEPEVHAVTKLALSdfefQNKRLEFIS-AYSGAEAKELIKEH-PDaaIVLLDVVMEtDDAGLQVAKFIREEakNN 102
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLE----SEPDIEVVGeAADGEEALALLRELrPD--VVLMDLSMP-GMDGIEALRRLRRR--YP 71


                  ....*
gi 1889634278 103 HIRII 107
Cdd:cd17535    72 DLKVI 76
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
 24-110 3.43e-05

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: 43.39  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSdfefqNKRLEFISAYSGAEAKELIKEH-PDaaIVLLDvVMETDDAGLQVAKFIREEAKNN 102
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLE-----RAGFDVVEAEDAESAVNLIVEPrPD--LILLD-WMLPGGSGIQFIRRLKRDEMTR 73


                  ....*...
gi 1889634278 103 HIRIILRT 110
Cdd:cd17618    74 DIPIIMLT 81
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
 25-112 5.58e-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: 42.41  E-value: 5.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  25 VLIVDDEPEVHAVTKlalsdFEFQNKRLEFISAYSGAEAKELIKE-HPDaaIVLLDVVMETDDaGLQVAKFIReeaKNNH 103
Cdd:cd17614     1 ILVVDDEKPISDILK-----FNLTKEGYEVVTAYDGREALEKVEEeQPD--LILLDLMLPEKD-GLEVCREVR---KTSN 69


                  ....*....
gi 1889634278 104 IRIILRTGQ 112
Cdd:cd17614    70 VPIIMLTAK 78
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
 24-112 5.89e-05

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 42.65  E-value: 5.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFEFQNkrleFISAYSGAEAKELIKEH-PDaaIVLLDVVM-ETDdaGLQVAKFIREEAKN 101
Cdd:cd17542     2 KVLIVDDAAFMRMMLKDILTKAGYEV----VGEAANGEEAVEKYKELkPD--LVTMDITMpEMD--GIEALKEIKKIDPN 73

                          90
                  ....*....|.
gi 1889634278 102 NHIRIILRTGQ 112
Cdd:cd17542    74 AKVIMCSAMGQ 84
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
 25-107 6.20e-05

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: 42.11  E-value: 6.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  25 VLIVDDEPEVHAVTKLALSDfefQNKRLEFisAYSGAEAKELIK-EHPDaaIVLLDVVMETDDaGLQVAKFIREEAKNNH 103
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRA---AGYRVLV--ATDGQQALQRAQaEPPD--LILLDVMMPGMD-GFEVCRRLKADPATRH 72


                  ....
gi 1889634278 104 IRII 107
Cdd:cd19920    73 IPVI 76
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
 24-107 7.47e-05

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: 42.14  E-value: 7.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPevhAVTKLALSDFEFQNkrLEFISAYSGAEAKELIKEH-PDaaIVLLDVVMETDDaGLQVAKFIREEAKNN 102
Cdd:cd17548     1 KILIVEDNP---LNMKLARDLLESAG--YEVLEAADGEEALEIARKEkPD--LILMDIQLPGMD-GLEATRLLKEDPATR 72


                  ....*
gi 1889634278 103 HIRII 107
Cdd:cd17548    73 DIPVI 77
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
 24-111 7.56e-05

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: 42.39  E-value: 7.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFEFqnkrlEFISAYSGAEAKELIKEHPdAAIVLLDVVM-ETDdaGLQVAKFIREEAKNN 102
Cdd:cd17569     2 TILLVDDEPNILKALKRLLRREGY-----EVLTATSGEEALEILKQEP-VDVVISDQRMpGMD--GAELLKRVRERYPDT 73


                  ....*....
gi 1889634278 103 hIRIILrTG 111
Cdd:cd17569    74 -VRILL-TG 80
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
 25-98 1.56e-04

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: 41.33  E-value: 1.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1889634278  25 VLIVDDEPEVHAVTKLALSDFEFqnkrlEFISAYSGAEAKELIKEH-PDAaiVLLDVVMETDDaGLQVAKFIREE 98
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGY-----EVDTAADGEEALKLIKERrPDL--VLLDIWLPDMD-GLELLKEIKEK 67
pleD PRK09581
response regulator PleD; Reviewed
 22-110 1.71e-04

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 44.12  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  22 TWKVLIVDDEPevhAVTKLalsdfeFQNKRL----EFISAYSGAEAKELI-KEHPDaaIVLLDVVMETDDaGLQVAKFIR 96
Cdd:PRK09581    2 TARILVVDDIP---ANVKL------LEAKLLaeyyTVLTASSGAEAIAICeREQPD--IILLDVMMPGMD-GFEVCRRLK 69

                          90
                  ....*....|....
gi 1889634278  97 EEAKNNHIRIILRT 110
Cdd:PRK09581   70 SDPATTHIPVVMVT 83
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
 23-110 1.93e-04

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: 41.08  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  23 WKVLIVDDEPEVHAVTKLALSDFE-FQNKrlefISAYSGAEAKELIKEHPdAAIVLLDVVMEtDDAGLQVAKFIReeAKN 101
Cdd:cd19925     1 INVLIVEDDPMVAEIHRAYVEQVPgFTVI----GTAGTGEEALKLLKERQ-PDLILLDIYLP-DGNGLDLLRELR--AAG 72


                  ....*....
gi 1889634278 102 NHIRIILRT 110
Cdd:cd19925    73 HDVDVIVVT 81
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
 24-99 3.25e-04

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: 40.26  E-value: 3.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFEFQnkrleFISAYSGAEAKELIK-EHPDaaIVLLDVVMETDDaGLQVAKFIREEA 99
Cdd:cd17555     2 TILVIDDDEVVRESIAAYLEDSGFQ-----VLQAADGRQGLELFRsEQPD--LVLCDLRMPEMD-GLEVLKQITKES 70
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
 24-97 3.32e-04

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: 40.65  E-value: 3.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFEfqnkRLEFI-SAYSGAEAKELIKEH-PDaaIVLLDVVMETDDaGLQVAKFI---RE 97
Cdd:COG2197     3 RVLIVDDHPLVREGLRALLEAEP----DIEVVgEAADGEEALELLEELrPD--VVLLDIRMPGMD-GLEALRRLltpRE 74
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
 24-119 3.44e-04

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: 40.18  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFEFQnkrleFISAYSGAEAKELIKEHPDAAIVLLDVVMETDDaGLQVAKFIREeaKNNH 103
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYA-----VTEAESGAEALEKLQQGKDIDIVVTDIVMPEMD-GIELAREARK--IDPD 72

                          90
                  ....*....|....*.
gi 1889634278 104 IRIILRTGQPGQAPER 119
Cdd:cd18160    73 VKILFISGGAAAAPEL 88
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
 24-82 4.13e-04

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 40.07  E-value: 4.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSdfefQNKRLEFI-SAYSGAEAKELIKEH-PDaaIVLLDVVM 82
Cdd:cd17541     2 RVLIVDDSAVMRKLLSRILE----SDPDIEVVgTARDGEEALEKIKELkPD--VITLDIEM 56
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
 25-110 5.97e-04

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: 39.67  E-value: 5.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  25 VLIVDDEPEVHAVTK--LALSDFEFQnkrlefiSAYSGAEAKELIKEH-PDAaiVLLDVVMETDDaGLQVAKFIReeAKN 101
Cdd:cd17627     1 ILVVDDDRAVRESLRrsLRFEGYEVE-------TAVDGAEALRVISGNrPDA--VVLDVMMPRLD-GLEVCRRLR--AAG 68


                  ....*....
gi 1889634278 102 NHIRIILRT 110
Cdd:cd17627    69 NDLPILVLT 77
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
 24-98 9.98e-04

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: 38.87  E-value: 9.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889634278  24 KVLIVDDEPEVHAVTKLALsdfEFQNkrLEFISAYSGAEAKELIKE-HPDAaiVLLDvVMETDDAGLQVAKFIREE 98
Cdd:cd17615     1 RVLVVDDEPNITELLSMAL---RYEG--WDVETAADGAEALAAAREfRPDA--VVLD-IMLPDMDGLEVLRRLRAD 68
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
 25-133 1.35e-03

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 38.13  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  25 VLIVDDEPEVHAVTKLALSDFEFqnkrlEFISAYSGAEA-KELIKEHPDaaIVLLDVVMETDDaGLQVAKFIREEAKNNH 103
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGF-----TVIAASNGLEAlDLLNQYIPD--LIISDIIMPGVD-GYSLLGKLRKNADFDT 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1889634278 104 IRIILRTGQpGQAPERqvIINYDI--NDYKSK 133
Cdd:cd19927    73 IPVIFLTAK-GMTSDR--IKGYNAgcDGYLSK 101
PRK10766 PRK10766
two-component system response regulator TorR;
22-111 1.86e-03

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 40.02  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  22 TWKVLIVDDEPevhaVTKLALSDFeFQNKRLEFISAYSGAEAKE-LIKEHPDaaIVLLDVVMETDDaGLQVAKFIREEAk 100
Cdd:PRK10766    2 SYHILVVEDEP----VTRARLQGY-FEQEGYTVSEAASGAGMREiMQNQHVD--LILLDINLPGED-GLMLTRELRSRS- 72

                          90
                  ....*....|.
gi 1889634278 101 nnHIRIILRTG 111
Cdd:PRK10766   73 --TVGIILVTG 81
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
24-97 2.10e-03

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 40.60  E-value: 2.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSdfefqNKRLEFISAYSGAEAKELIKEHPdAAIVLLDVVMETDDaGLQVAKFIRE 97
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFA-----LQGFETHCANNGRTALHLFADIH-PDVVLMDIRMPEMD-GIKALKEMRS 72
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
 24-110 2.43e-03

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: 38.09  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSDFEFQNkrleFISAYSGAEAKELIKeHPDAAIVLLDVVMETDDaGLQVAKFIREEAKNNH 103
Cdd:cd19923     2 KVLVVDDFSTMRRIIKNLLKELGFNN----VEEAEDGVDALEKLK-AGGFDFVITDWNMPNMD-GLELLKTIRADGALSH 75


                  ....*..
gi 1889634278 104 IRIILRT 110
Cdd:cd19923    76 LPVLMVT 82
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
 24-116 3.41e-03

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: 37.42  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEP-EVHAVTKLaLSDFEFqnkrLEFISAYSGAEAKELIKEH-PDaaIVLLDVVMETDDaGLQVAKFIREEAKN 101
Cdd:cd17551     2 RILIVDDNPtNLLLLEAL-LRSAGY----LEVVSFTDPREALAWCRENpPD--LILLDYMMPGMD-GLEFIRRLRALPGL 73

                          90
                  ....*....|....*
gi 1889634278 102 NHIRIILRTGQPGQA 116
Cdd:cd17551    74 EDVPIVMITADTDRE 88
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 25-112 4.48e-03

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: 37.47  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  25 VLIVDDEPEV-HAVTK-LALSDFEFQnkrlefiSAYSGAEAKELIKEHPdAAIVLLDVVMETDDaGLQVAKFIREeaKNN 102
Cdd:cd17549     1 VLLVDDDADVrEALQQtLELAGFRVR-------AFADAEEALAALSPDF-PGVVISDIRMPGMD-GLELLAQIRE--LDP 69

                          90
                  ....*....|
gi 1889634278 103 HIRIILRTGQ 112
Cdd:cd17549    70 DLPVILITGH 79
REC_1_GGDEF cd19921
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
 24-81 4.76e-03

first 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 contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the first REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381148 [Multi-domain]  Cd Length: 115  Bit Score: 37.16  E-value: 4.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1889634278  24 KVLIVDDEPEVHAVTKLALSdfefQNKRLEFISAYSGAEAKELIKEHPDAAIVLLDVV 81
Cdd:cd19921     1 KVLIVEDSKTFSKVLKHLIA----QELGLEVDVAETLAEAKALLEEGDDYFAALVDLN 54
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
 56-114 5.35e-03

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 36.87  E-value: 5.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  56 SAYSGAEAKELIKEH-PDAAIvlLDVVMETDDaGLQVAKFIREEAKNNHIRIILRTGQPG 114
Cdd:cd19930    29 QASNGQEALRLVLKHsPDVAI--LDIEMPGRT-GLEVAAELREELPDTKVLIVTTFGRPG 85
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
 25-104 5.38e-03

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: 36.75  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  25 VLIVDDEPevhavtkLA---LSDFEFQNKRLEFI-SAYSGAEAKELIKEH-PDaaIVLLDVVMETDDaGLQVAKFIREEA 99
Cdd:cd17532     1 ALIVDDEP-------LAreeLRYLLEEHPDIEIVgEAENGEEALEAIEELkPD--VVFLDIQMPGLD-GLELAKKLSKLA 70


                  ....*
gi 1889634278 100 KNNHI 104
Cdd:cd17532    71 KPPLI 75
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
 25-112 8.52e-03

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: 36.21  E-value: 8.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  25 VLIVDDEPevhaVTKLALSDFeFQNKRLEFISAYSGAEAKELIKEHpDAAIVLLDVVMETDDaGLQVAKFIREEAknnHI 104
Cdd:cd17619     3 ILIVEDEP----VTRATLKSY-FEQEGYDVSEAGDGEEMRQILARQ-DIDLVLLDINLPGKD-GLSLTRELREQS---EV 72


                  ....*...
gi 1889634278 105 RIILRTGQ 112
Cdd:cd17619    73 GIILVTGR 80
orf27 CHL00148
Ycf27; Reviewed
 24-111 8.94e-03

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 37.77  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889634278  24 KVLIVDDEPEVHAV--TKLALSDFefqnkrlEFISAYSGAEA-KELIKEHPDaaIVLLDVVMETDDaGLQVAKFIREEAK 100
Cdd:CHL00148    8 KILVVDDEAYIRKIleTRLSIIGY-------EVITASDGEEAlKLFRKEQPD--LVILDVMMPKLD-GYGVCQEIRKESD 77

                          90
                  ....*....|.
gi 1889634278 101 nnhIRIILRTG 111
Cdd:CHL00148   78 ---VPIIMLTA 85
 
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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