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Conserved domains on  [gi|1222444026|ref|WP_090495440|]
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SpoIIE family protein phosphatase [Pseudoalteromonas sp. DSM 26666]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RsbU COG2208
Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
 295-485 1.19e-28

Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, Transcription];


:

Pssm-ID: 441810 [Multi-domain]  Cd Length: 435  Bit Score: 117.85  E-value: 1.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 295 GGDFF--MPINDEGTAFILGDMMGHGLQA--LkeSFAIKGFISGFLATGLAYQEMLAALNNALYkQQLCKSSLVTLVICF 370
Cdd:COG2208   234 GGDFYdvFPLDDGRLAVVIGDVSGHGVPAalL--MAMLRSALRALAREGLDPAEVLERLNRALY-EDLGGGRFVTAFLGV 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 371 L--ENNKLYWLNAGHPAPVIISKNGDLSQLNGTGPLLGLSNDHQYTLYETELDNVEHIILYTDGWTDnRFTDKDEM---T 445
Cdd:COG2208   311 LdpETGRLTYANAGHPPPLLLRADGEVEELDGGGLPLGLLPDAEYEEHEIPLEPGDRLLLYTDGLTE-ARNGDGELfgeE 389

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1222444026 446 ELKKII-PTQSTSAEDFAHSL------WKNSQVAlskeVDDASLIII 485
Cdd:COG2208   390 RLLELLaENADLPAEELLDALlealeeFRGGGPQ----EDDITLLAL 432
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 136-256 4.43e-18

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: 82.91  E-value: 4.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 136 NIDKRPSIIYVDDDVTQLALMSAYLKD-KFNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNLKSQL 214
Cdd:COG3437     2 RTGQAPTVLIVDDDPENLELLRQLLRTlGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDI 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1222444026 215 SVVMLTGDDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERV 256
Cdd:COG3437    82 PVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNA 123
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
16-128 7.31e-10

Histidine kinase-like ATPase domain;


:

Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 56.91  E-value: 7.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026  16 LTEIRQVLKHVLGALSVTRDEADAAGLVATEYLTNLIRH--NEGDEQLIMLRIsQINNDTYQLTFVDELKPYNLFKQNNS 93
Cdd:pfam13581   8 LRAARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHayREGPEGPVEVRL-TSDGGGLVVTVADSGPPFDPLTLPPP 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1222444026  94 SWTLASDELVEGGMGVELIRHYFADAIYDTRAGKN 128
Cdd:pfam13581  87 DLEEPDEDRKEGGRGLALIRGLMDDVEYTRGGEGN 121
 
Name Accession Description Interval E-value
RsbU COG2208
Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
 295-485 1.19e-28

Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, Transcription];


Pssm-ID: 441810 [Multi-domain]  Cd Length: 435  Bit Score: 117.85  E-value: 1.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 295 GGDFF--MPINDEGTAFILGDMMGHGLQA--LkeSFAIKGFISGFLATGLAYQEMLAALNNALYkQQLCKSSLVTLVICF 370
Cdd:COG2208   234 GGDFYdvFPLDDGRLAVVIGDVSGHGVPAalL--MAMLRSALRALAREGLDPAEVLERLNRALY-EDLGGGRFVTAFLGV 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 371 L--ENNKLYWLNAGHPAPVIISKNGDLSQLNGTGPLLGLSNDHQYTLYETELDNVEHIILYTDGWTDnRFTDKDEM---T 445
Cdd:COG2208   311 LdpETGRLTYANAGHPPPLLLRADGEVEELDGGGLPLGLLPDAEYEEHEIPLEPGDRLLLYTDGLTE-ARNGDGELfgeE 389

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1222444026 446 ELKKII-PTQSTSAEDFAHSL------WKNSQVAlskeVDDASLIII 485
Cdd:COG2208   390 RLLELLaENADLPAEELLDALlealeeFRGGGPQ----EDDITLLAL 432
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
 303-485 6.21e-26

Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.


Pssm-ID: 462119 [Multi-domain]  Cd Length: 192  Bit Score: 104.27  E-value: 6.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 303 NDEGTAFILGDMMGHGLQALKESFAIKGFISGFLATGLAYQEMLAALNNALYkQQLCKSSLVTLVICFL--ENNKLYWLN 380
Cdd:pfam07228   1 PDGRLALVIGDVMGHGLPAALLMGLLRTALRALAAEGLDPAEVLKRLNRLLQ-RNLEEDMFATAVLAVYdpETGTLEYAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 381 AGHPAPVIISKNGD-LSQLNGTGPLLGLSNDHQYTLYETELDNVEHIILYTDGWTDNRFTD---KDEMTELKKIIPTQST 456
Cdd:pfam07228  80 AGHPPPLLLRPDGGvVELLESPGLPLGILPDAPYEVVELELEPGDTLLLYTDGLTEARDPDgelFGLERLLALLAERHGL 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1222444026 457 SAEDFAHSLWKNSQVALSKEV-DDASLIII 485
Cdd:pfam07228 160 PPEELLDALLEALLRLGGGELeDDITLLVL 189
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
295-463 1.27e-18

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624 [Multi-domain]  Cd Length: 193  Bit Score: 83.94  E-value: 1.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026  295 GGDFF--MPINDEGTAFILGDMMGHGLQALKESFAIKGFISGFLATGLAYQEMLAALNNALYKQQLCkSSLVTLVIC--F 370
Cdd:smart00331  17 GGDFYdvVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRAIYENGED-GMFATLFLAlyD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026  371 LENNKLYWLNAGHPAPVIISKNGDLSQ-LNGTGPLLGLSNDHQYTLYETELDNVEHIILYTDGWTDNRFTDKDEmtelKK 449
Cdd:smart00331  96 FAGGTLSYANAGHSPPYLLRADGGLVEdLDDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTDGLTEARNPERLE----EL 171

                          170
                   ....*....|....
gi 1222444026  450 IIPTQSTSAEDFAH 463
Cdd:smart00331 172 LEELLGSPPAEIAQ 185
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 136-256 4.43e-18

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: 82.91  E-value: 4.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 136 NIDKRPSIIYVDDDVTQLALMSAYLKD-KFNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNLKSQL 214
Cdd:COG3437     2 RTGQAPTVLIVDDDPENLELLRQLLRTlGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDI 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1222444026 215 SVVMLTGDDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERV 256
Cdd:COG3437    82 PVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNA 123
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 146-243 6.77e-13

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: 64.56  E-value: 6.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 146 VDDDVTQLALMSAYLKDK-FNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKsnLKSQLSVVMLTGDDS 224
Cdd:cd00156     3 VDDDPAIRELLKSLLEREgYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRE--LPPDIPVIVLTAKAD 80

                          90
                  ....*....|....*....
gi 1222444026 225 EEVISKINRLGVDDYLIKP 243
Cdd:cd00156    81 EEDAVRALELGADDYLVKP 99
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
16-128 7.31e-10

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 56.91  E-value: 7.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026  16 LTEIRQVLKHVLGALSVTRDEADAAGLVATEYLTNLIRH--NEGDEQLIMLRIsQINNDTYQLTFVDELKPYNLFKQNNS 93
Cdd:pfam13581   8 LRAARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHayREGPEGPVEVRL-TSDGGGLVVTVADSGPPFDPLTLPPP 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1222444026  94 SWTLASDELVEGGMGVELIRHYFADAIYDTRAGKN 128
Cdd:pfam13581  87 DLEEPDEDRKEGGRGLALIRGLMDDVEYTRGGEGN 121
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 143-254 1.03e-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: 56.01  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYL-KDKFNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKsnLKSQLSVVMLTG 221
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLeKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRR--RDPTTPVIILTA 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1222444026 222 DDSEEVISKINRLGVDDYLIKPVKKNKLLQSIE 254
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
16-128 3.00e-09

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 54.92  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026  16 LTEIRQVLKHVLGALSVTRDEADAAGLVATEYLTNLIRH--NEGDEQLIMLRISqINNDTYQLTFVDELKPYNLFKQNNS 93
Cdd:COG2172    11 LGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHayGGDPDGPVEVELE-LDPDGLEIEVRDEGPGFDPEDLPDP 89

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1222444026  94 SWTLAsdelvEGGMGVELIRHYFADAIYDTRAGKN 128
Cdd:COG2172    90 YSTLA-----EGGRGLFLIRRLMDEVEYESDPGGT 119
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
143-277 2.74e-06

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 48.65  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYL-KDKFNVITCENidaGWQAILTSDASI--LLLDHKL--KQGtceplLEKLNKSNLKSQLSVV 217
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLeMEGFNVIVAHD---GEQALDLLDDSIdlLLLDVMMpkKNG-----IDTLKELRQTHQTPVI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222444026 218 MLT--GDDSEEVISKinRLGVDDYLIKPVKKNKLLQSIeRVTHRFAYLSYQSTFGLTPSKVL 277
Cdd:PRK10955   76 MLTarGSELDRVLGL--ELGADDYLPKPFNDRELVARI-RAILRRSHWSEQQQNNDNGSPTL 134
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 42-128 7.42e-03

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


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 35.71  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026  42 LVATEYLTNLIRHNEGDEQLIMLRIS-QINNDTYQLTFVDELKPYNLFKQNNSSWTLAsdelvEGGMGVELIRHyFADA- 119
Cdd:cd16936     3 LAVSEAVTNAVRHAYRHDGPGPVRLElDLDPDRLRVEVTDSGPGFDPLRPADPDAGLR-----EGGRGLALIRA-LMDEv 76

                          90
                  ....*....|
gi 1222444026 120 -IYDTRAGKN 128
Cdd:cd16936    77 gYRRTPGGKT 86
 
Name Accession Description Interval E-value
RsbU COG2208
Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
 295-485 1.19e-28

Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, Transcription];


Pssm-ID: 441810 [Multi-domain]  Cd Length: 435  Bit Score: 117.85  E-value: 1.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 295 GGDFF--MPINDEGTAFILGDMMGHGLQA--LkeSFAIKGFISGFLATGLAYQEMLAALNNALYkQQLCKSSLVTLVICF 370
Cdd:COG2208   234 GGDFYdvFPLDDGRLAVVIGDVSGHGVPAalL--MAMLRSALRALAREGLDPAEVLERLNRALY-EDLGGGRFVTAFLGV 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 371 L--ENNKLYWLNAGHPAPVIISKNGDLSQLNGTGPLLGLSNDHQYTLYETELDNVEHIILYTDGWTDnRFTDKDEM---T 445
Cdd:COG2208   311 LdpETGRLTYANAGHPPPLLLRADGEVEELDGGGLPLGLLPDAEYEEHEIPLEPGDRLLLYTDGLTE-ARNGDGELfgeE 389

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1222444026 446 ELKKII-PTQSTSAEDFAHSL------WKNSQVAlskeVDDASLIII 485
Cdd:COG2208   390 RLLELLaENADLPAEELLDALlealeeFRGGGPQ----EDDITLLAL 432
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
 303-485 6.21e-26

Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.


Pssm-ID: 462119 [Multi-domain]  Cd Length: 192  Bit Score: 104.27  E-value: 6.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 303 NDEGTAFILGDMMGHGLQALKESFAIKGFISGFLATGLAYQEMLAALNNALYkQQLCKSSLVTLVICFL--ENNKLYWLN 380
Cdd:pfam07228   1 PDGRLALVIGDVMGHGLPAALLMGLLRTALRALAAEGLDPAEVLKRLNRLLQ-RNLEEDMFATAVLAVYdpETGTLEYAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 381 AGHPAPVIISKNGD-LSQLNGTGPLLGLSNDHQYTLYETELDNVEHIILYTDGWTDNRFTD---KDEMTELKKIIPTQST 456
Cdd:pfam07228  80 AGHPPPLLLRPDGGvVELLESPGLPLGILPDAPYEVVELELEPGDTLLLYTDGLTEARDPDgelFGLERLLALLAERHGL 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1222444026 457 SAEDFAHSLWKNSQVALSKEV-DDASLIII 485
Cdd:pfam07228 160 PPEELLDALLEALLRLGGGELeDDITLLVL 189
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
295-463 1.27e-18

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624 [Multi-domain]  Cd Length: 193  Bit Score: 83.94  E-value: 1.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026  295 GGDFF--MPINDEGTAFILGDMMGHGLQALKESFAIKGFISGFLATGLAYQEMLAALNNALYKQQLCkSSLVTLVIC--F 370
Cdd:smart00331  17 GGDFYdvVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRAIYENGED-GMFATLFLAlyD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026  371 LENNKLYWLNAGHPAPVIISKNGDLSQ-LNGTGPLLGLSNDHQYTLYETELDNVEHIILYTDGWTDNRFTDKDEmtelKK 449
Cdd:smart00331  96 FAGGTLSYANAGHSPPYLLRADGGLVEdLDDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTDGLTEARNPERLE----EL 171

                          170
                   ....*....|....
gi 1222444026  450 IIPTQSTSAEDFAH 463
Cdd:smart00331 172 LEELLGSPPAEIAQ 185
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 136-256 4.43e-18

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: 82.91  E-value: 4.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 136 NIDKRPSIIYVDDDVTQLALMSAYLKD-KFNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNLKSQL 214
Cdd:COG3437     2 RTGQAPTVLIVDDDPENLELLRQLLRTlGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDI 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1222444026 215 SVVMLTGDDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERV 256
Cdd:COG3437    82 PVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNA 123
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 139-261 1.31e-17

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: 84.63  E-value: 1.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 139 KRPSIIYVDDDVTQLALMSAYLKDK-FNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNlkSQLSVV 217
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAgYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALD--PDLPVI 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1222444026 218 MLTGDDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERVTHRFA 261
Cdd:COG2204    79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRR 122
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 139-264 3.11e-17

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 78.09  E-value: 3.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 139 KRPSIIYVDDDVTQLALMSAYLKDKF---NVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNlkSQLS 215
Cdd:COG4565     2 KMIRVLIVEDDPMVAELLRRYLERLPgfeVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARG--PDVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1222444026 216 VVMLTGDDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERVTHRFAYLS 264
Cdd:COG4565    80 VIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLR 128
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 139-259 1.76e-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: 72.96  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 139 KRPSIIYVDDDVTQLALMSAYLKDK-FNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNLKSQLSVV 217
Cdd:COG0784     4 GGKRILVVDDNPDNRELLRRLLERLgYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPII 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1222444026 218 MLTGDDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERVTHR 259
Cdd:COG0784    84 ALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLAR 125
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 140-258 1.14e-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: 71.86  E-value: 1.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 140 RPSIIYVDDDVTQLALMSAYLKDK-FNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNLKSQLSVVM 218
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAgYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIF 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1222444026 219 LTGDDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERVTH 258
Cdd:COG3706    81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVAR 120
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
 138-259 1.59e-13

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 68.79  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 138 DKRPSIIYVDDDVTQLALMSAYLKDK-FNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLnkSNLKSQLSV 216
Cdd:COG4567     2 AEDRSLLLVDDDEAFARVLARALERRgFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEAL--RERDPDARI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1222444026 217 VMLTGDDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERVTHR 259
Cdd:COG4567    80 VVLTGYASIATAVEAIKLGADDYLAKPADADDLLAALERAEGD 122
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 146-243 6.77e-13

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: 64.56  E-value: 6.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 146 VDDDVTQLALMSAYLKDK-FNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKsnLKSQLSVVMLTGDDS 224
Cdd:cd00156     3 VDDDPAIRELLKSLLEREgYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRE--LPPDIPVIVLTAKAD 80

                          90
                  ....*....|....*....
gi 1222444026 225 EEVISKINRLGVDDYLIKP 243
Cdd:cd00156    81 EEDAVRALELGADDYLVKP 99
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
 140-259 1.20e-12

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: 66.90  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 140 RPSIIYVDDDVTQLALMSAYLKDK-FNVITCENIDAGWQAILTSDASILLLDHKLkqgtceP------LLEKLNKSNlkS 212
Cdd:COG0745     1 MPRILVVEDDPDIRELLADALEREgYEVDTAADGEEALELLEEERPDLILLDLML------PgmdgleVCRRLRARP--S 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1222444026 213 QLSVVMLTGDDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERVTHR 259
Cdd:COG0745    73 DIPIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRR 119
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
 143-259 4.04e-11

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 60.01  E-value: 4.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYLK-DKFNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSnlkSQLSVVMLT- 220
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEmEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKT---SQVPVLMLTa 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1222444026 221 -GDDSEEVISKinRLGVDDYLIKPVKKNKLLQSIERVTHR 259
Cdd:cd17623    78 rGDDIDRILGL--ELGADDYLPKPFNPRELVARIRAILRR 115
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
16-128 7.31e-10

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 56.91  E-value: 7.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026  16 LTEIRQVLKHVLGALSVTRDEADAAGLVATEYLTNLIRH--NEGDEQLIMLRIsQINNDTYQLTFVDELKPYNLFKQNNS 93
Cdd:pfam13581   8 LRAARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHayREGPEGPVEVRL-TSDGGGLVVTVADSGPPFDPLTLPPP 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1222444026  94 SWTLASDELVEGGMGVELIRHYFADAIYDTRAGKN 128
Cdd:pfam13581  87 DLEEPDEDRKEGGRGLALIRGLMDDVEYTRGGEGN 121
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 143-254 1.03e-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: 56.01  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYL-KDKFNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKsnLKSQLSVVMLTG 221
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLeKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRR--RDPTTPVIILTA 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1222444026 222 DDSEEVISKINRLGVDDYLIKPVKKNKLLQSIE 254
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
16-128 3.00e-09

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 54.92  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026  16 LTEIRQVLKHVLGALSVTRDEADAAGLVATEYLTNLIRH--NEGDEQLIMLRISqINNDTYQLTFVDELKPYNLFKQNNS 93
Cdd:COG2172    11 LGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHayGGDPDGPVEVELE-LDPDGLEIEVRDEGPGFDPEDLPDP 89

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1222444026  94 SWTLAsdelvEGGMGVELIRHYFADAIYDTRAGKN 128
Cdd:COG2172    90 YSTLA-----EGGRGLFLIRRLMDEVEYESDPGGT 119
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
 146-243 2.06e-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: 51.64  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 146 VDDDVTQLALMSAYL-KDKFNVITCENIDAGWQAILTSDASILLLDHKLkqgtceP------LLEKLNKSNlkSQLSVVM 218
Cdd:cd17574     3 VEDDEEIAELLSDYLeKEGYEVDTAADGEEALELAREEQPDLIILDVML------PgmdgfeVCRRLREKG--SDIPIIM 74

                          90       100
                  ....*....|....*....|....*..
gi 1222444026 219 LTGDDSEEviSKIN--RLGVDDYLIKP 243
Cdd:cd17574    75 LTAKDEEE--DKVLglELGADDYITKP 99
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
 142-243 1.50e-07

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: 49.39  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 142 SIIYVDDDVTQLALMSAYLKDKFN---VITCENIDAGWQAILTSDASILLLDHKLkqgtceP------LLEKLNKSNLKS 212
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEAGfevVGEAENGEEALELLEEHKPDLVITDINM------PgmdgleLLEAIRELDPDT 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1222444026 213 QlsVVMLTGDDSEEVISKINRLGVDDYLIKP 243
Cdd:COG4753    75 K--IIILSGYSDFEYAQEAIKLGADDYLLKP 103
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
 146-255 2.47e-07

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: 49.17  E-value: 2.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 146 VDDDVTQLALMSAYLK--DKFNVI-TCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNLKSQlsVVMLTGD 222
Cdd:cd19925     6 VEDDPMVAEIHRAYVEqvPGFTVIgTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVD--VIVVTAA 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1222444026 223 DSEEVISKINRLGVDDYLIKPVKKNKLLQSIER 255
Cdd:cd19925    84 NDVETVREALRLGVVDYLIKPFTFERLRQRLER 116
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
 143-261 3.99e-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: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYLK--DKFNVI-TCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNLKSQlsVVML 219
Cdd:COG3279     4 ILIVDDEPLARERLERLLEkyPDLEVVgEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPP--IIFT 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1222444026 220 TGDDSEEVISKinRLGVDDYLIKPVKKNKLLQSIERVTHRFA 261
Cdd:COG3279    82 TAYDEYALEAF--EVNAVDYLLKPIDEERLAKALEKAKERLE 121
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
 142-260 5.86e-07

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 49.96  E-value: 5.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 142 SIIYVDDDVTQLALMSAYLKDK-FNVIT-CENIDAGWQAILTSDASILLLDHKLkqgTCEPLLEKLNKSNLKSQLSVVML 219
Cdd:COG3707     5 RVLVVDDEPLRRADLREGLREAgYEVVAeAADGEDAVELVRELKPDLVIVDIDM---PDRDGLEAARQISEERPAPVILL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1222444026 220 TGDDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERVTHRF 260
Cdd:COG3707    82 TAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARF 122
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
 141-244 2.32e-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: 46.28  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 141 PSIIYVDDDVTQLALMSAYLKDK-FNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLnkSNLKSQLSVVML 219
Cdd:cd17563     1 KSLLLVDDDEVFAERLARALERRgFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPL--RALQPDARIVVL 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1222444026 220 TGDDS-----EEViskinRLGVDDYLIKPV 244
Cdd:cd17563    79 TGYASiatavEAI-----KLGADDYLAKPA 103
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
143-277 2.74e-06

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 48.65  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYL-KDKFNVITCENidaGWQAILTSDASI--LLLDHKL--KQGtceplLEKLNKSNLKSQLSVV 217
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLeMEGFNVIVAHD---GEQALDLLDDSIdlLLLDVMMpkKNG-----IDTLKELRQTHQTPVI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222444026 218 MLT--GDDSEEVISKinRLGVDDYLIKPVKKNKLLQSIeRVTHRFAYLSYQSTFGLTPSKVL 277
Cdd:PRK10955   76 MLTarGSELDRVLGL--ELGADDYLPKPFNDRELVARI-RAILRRSHWSEQQQNNDNGSPTL 134
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
 143-256 3.68e-06

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: 46.09  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYLKDK-FNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNLKSQLSVVMLTG 221
Cdd:cd17618     3 ILIVEDEPAIREMIAFNLERAgFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIMLTA 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1222444026 222 DDSEEviSKINRL--GVDDYLIKPVKKNKLLQSIERV 256
Cdd:cd17618    83 RGEEE--DKVRGLeaGADDYITKPFSPRELVARIKAV 117
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
 143-253 5.13e-06

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


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 45.65  E-value: 5.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYLKDK-FNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNLKSqlSVVMLTG 221
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEgYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPT--SVIVITA 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1222444026 222 DDSEEVISKINRLGVDDYLIKPVKKNKLLQSI 253
Cdd:cd17572    79 HGSVDIAVEAMRLGAYDFLEKPFDADRLRVTV 110
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
 143-253 8.22e-06

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 44.74  E-value: 8.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYLKDKFNVITCENIDAGWQAILTSDA-SILLLDHKLKQgtcEPLLEKLNKSNLKSQLSVVMLTG 221
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRvDLVLLDLRLGQ---ESGLDLLRTIRARSDVPIIIISG 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1222444026 222 DDSEEVISKIN-RLGVDDYLIKPVKKNKLLQSI 253
Cdd:cd17594    79 DRRDEIDRVVGlELGADDYLAKPFGLRELLARV 111
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
 143-243 8.39e-06

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 44.36  E-value: 8.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYLK-DKFNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKsnlKSQLSVVMLTG 221
Cdd:cd19936     1 IALVDDDRNILTSVSMALEaEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQ---KSTLPVIFLTS 77

                          90       100
                  ....*....|....*....|....
gi 1222444026 222 DDSE--EVISKinRLGVDDYLIKP 243
Cdd:cd19936    78 KDDEidEVFGL--RMGADDYITKP 99
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
 146-253 9.87e-06

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: 44.38  E-value: 9.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 146 VDDDVTQLALMSAYL-KDKFNVITCENidaGWQAI--LTSDA-SILLLD------------HKLKQgtceplLEKLNKsn 209
Cdd:cd17546     4 VDDNPVNRKVLKKLLeKLGYEVDVAEN---GQEALelLKEEPfDLVLMDlqmpvmdgleatRRIRE------LEGGGR-- 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1222444026 210 lksQLSVVMLTGDDSEEVISKINRLGVDDYLIKPVKKNKLLQSI 253
Cdd:cd17546    73 ---RTPIIALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
 201-259 1.61e-05

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: 44.25  E-value: 1.61e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222444026 201 LLEKLNKSNLKSQlsVVMLTG-DDSE---EVIskinRLGVDDYLIKPVKKNKLLQSIERVTHR 259
Cdd:cd17536    63 LIEKIRELYPDIK--IIILSGyDDFEyaqKAI----RLGVVDYLLKPVDEEELEEALEKAKEE 119
ompR PRK09468
osmolarity response regulator; Provisional
 143-259 1.68e-05

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 46.12  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYLKDK-FNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNlkSQLSVVMLT- 220
Cdd:PRK09468    8 ILVVDDDMRLRALLERYLTEQgFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQN--NPTPIIMLTa 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1222444026 221 -GDDSEEVISKinRLGVDDYLIKPVKKNKLLQSIERVTHR 259
Cdd:PRK09468   86 kGEEVDRIVGL--EIGADDYLPKPFNPRELLARIRAVLRR 123
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
 141-250 2.03e-05

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: 43.53  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 141 PSIIYVDDDVTQLALMSAYL-KDKFNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKsnlKSQLSVVML 219
Cdd:cd17619     1 PHILIVEDEPVTRATLKSYFeQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELRE---QSEVGIILV 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1222444026 220 TGDDSEevISKINRL--GVDDYLIKPVKKNKLL 250
Cdd:cd17619    78 TGRDDE--VDRIVGLeiGADDYVTKPFNPRELL 108
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
 143-250 2.42e-05

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 43.52  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYLKD-KFNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKsnlKSQLSVVMLTG 221
Cdd:cd17622     3 ILLVEDDPKLARLIADFLEShGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRP---KYQGPILLLTA 79

                          90       100
                  ....*....|....*....|....*....
gi 1222444026 222 DDSEEVISKINRLGVDDYLIKPVKKNKLL 250
Cdd:cd17622    80 LDSDIDHILGLELGADDYVVKPVEPAVLL 108
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
143-281 2.92e-05

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 45.48  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYL-KDKFNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNLKSQLSVVMLTG 221
Cdd:PRK10161    5 ILVVEDEAPIREMVCFVLeQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTA 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222444026 222 DDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERVTHRFAYLSYQSTFGL-------TPSKVLLGHN 281
Cdd:PRK10161   85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRRISPMAVEEVIEMqglsldpTSHRVMAGEE 151
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
 141-254 3.46e-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: 43.16  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 141 PSIIYVDDDVTQL-ALMSAYLKDKFNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKsnlKSQLSV-VM 218
Cdd:cd17569     1 PTILLVDDEPNILkALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRE---RYPDTVrIL 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1222444026 219 LTGD-DSEEVISKINRLGVDDYLIKPVKKNKLLQSIE 254
Cdd:cd17569    78 LTGYaDLDAAIEAINEGEIYRFLTKPWDDEELKETIR 114
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
 216-256 3.72e-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: 43.04  E-value: 3.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1222444026 216 VVMLTGDDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERV 256
Cdd:cd17542    76 VIMCSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKV 116
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
 143-256 4.04e-05

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: 42.87  E-value: 4.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYLKD-KFNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNlkSQLSVVMLTG 221
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDeGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKY--PDLPVIMISG 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1222444026 222 DDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERV 256
Cdd:cd17550    79 HGTIETAVKATKLGAYDFIEKPLSLDRLLLTIERA 113
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
 146-259 4.25e-05

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 42.98  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 146 VDDDVTQLALMSAYLKDK-FNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNLksQLSVVMLTGDDS 224
Cdd:cd17625     3 VEDEKDLSEAITKHLKKEgYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGI--ETPVLLLTALDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1222444026 225 EEviSKIN--RLGVDDYLIKPVKKNKLLQSIERVTHR 259
Cdd:cd17625    81 VE--DRVKglDLGADDYLPKPFSLAELLARIRALLRR 115
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
 141-260 5.20e-05

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of this subfamily are response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It belongs to the nitrogen regulatory protein C (NtrC) family of response regulators, which activate transcription by RNA polymerase (RNAP) in response to a change in the environment. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Proteins in this subfamily contain an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 43.12  E-value: 5.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 141 PSIIYVDDDVTQLALMSAYLKDKFNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSnlKSQLSVVMLT 220
Cdd:cd17596     1 PTILVVDDEVRSLEALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRER--WPEVVRIIIS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1222444026 221 G-DDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERVTHRF 260
Cdd:cd17596    79 GyTDSEDIIAGINEAGIYQYLTKPWHPDQLLLTVRNAARLF 119
dpiA PRK10046
two-component response regulator DpiA; Provisional
 141-259 9.68e-05

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 43.85  E-value: 9.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 141 PSIIYVDDDVTQLALMSA-YLKD--KFNVI-TCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNLKSqlSV 216
Cdd:PRK10046    4 PLTLLIVEDETPLAEMHAeYIRHipGFSQIlLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPG--DV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1222444026 217 VMLTGDDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERVTHR 259
Cdd:PRK10046   82 VFTTAASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRFRQR 124
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
 143-243 1.75e-04

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 40.67  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYL--KDKFNVI-TCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNLKSQLSVVML 219
Cdd:cd17561     4 VLIADDNREFVQLLEEYLnsQPDMEVVgVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIML 83

                          90       100
                  ....*....|....*....|....
gi 1222444026 220 TGDDSEEVISKINRLGVDDYLIKP 243
Cdd:cd17561    84 TAFGQEDITQRAVELGASYYILKP 107
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
 141-255 4.16e-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: 39.88  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 141 PSIIYVDDDVTQLALMSAYLKDK-FNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNlkSQLSVVML 219
Cdd:cd17555     1 ATILVIDDDEVVRESIAAYLEDSgFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKES--PDTPVIVV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1222444026 220 TG----DDSEEVIskinRLGVDDYLIKPVKK-NKLLQSIER 255
Cdd:cd17555    79 SGagvmSDAVEAL----RLGAWDYLTKPIEDlAVLEHAVRR 115
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 143-255 6.66e-04

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 39.78  E-value: 6.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYLKDK-FNVITCEN-------IDAGWQAILTSDasILL-----LDhklkqgtcepLLEKLNKsn 209
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAgFRVRAFADaeealaaLSPDFPGVVISD--IRMpgmdgLE----------LLAQIRE-- 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1222444026 210 LKSQLSVVMLT--GDDSEEVisKINRLGVDDYLIKPVKKNKLLQSIER 255
Cdd:cd17549    67 LDPDLPVILITghGDVPMAV--EAMRAGAYDFLEKPFDPERLLDVVRR 112
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
 146-249 1.14e-03

phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains; Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 38.76  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 146 VDDDVTQLALMSA-YLKDKFNVITCENIDAGWQAILTSDASI--LLLDHKLKQGTCEPLLEKLNksnLKSQLSVVMLTGD 222
Cdd:cd17584     4 VDDDPTCLAILKRmLLRCGYQVTTCTDAEEALSMLRENKDEFdlVITDVHMPDMDGFEFLELIR---LEMDLPVIMMSAD 80

                          90       100
                  ....*....|....*....|....*..
gi 1222444026 223 DSEEVISKINRLGVDDYLIKPVKKNKL 249
Cdd:cd17584    81 GSTSTVMKGLAHGACDYLLKPVSIEDL 107
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
 143-253 1.40e-03

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 38.60  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYLK-DKFNVITCENIDAGWQAILTSDASILLLDHKL--KQGtceplLEKLNKSNLKSQLSVVML 219
Cdd:cd17626     3 ILVVDDDAALAEMIGIVLRgEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLpgIDG-----IEVCRQIRAESGVPIVML 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1222444026 220 TG-DDSEEVISKINRlGVDDYLIKPVKKNKLLQSI 253
Cdd:cd17626    78 TAkSDTVDVVLGLES-GADDYVAKPFKPKELVARI 111
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
 146-245 1.53e-03

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 38.50  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 146 VDDDVTQLALMSAYLK-DKFNVITcenIDAGWQA--ILTSDASILLLDHKLKQ------GTCEP------LLEKLNKSNL 210
Cdd:cd17581     4 VDDSLVDRKVIERLLRiSSCRVTA---VDSGKRAleFLGLEDEEDSSNFNEPKvnmiitDYCMPgmtgydLLKKVKESSA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1222444026 211 KSQLSVVMLTgddSEEVISKINRL---GVDDYLIKPVK 245
Cdd:cd17581    81 LKEIPVVIMS---SENIPTRISRCleeGAEDFLLKPVK 115
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
 216-259 3.54e-03

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 37.39  E-value: 3.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1222444026 216 VVMLTGDDSEEVISKINRLGVDDYLIKPVKKNKLLQSIERVTHR 259
Cdd:cd19932    75 IVLLTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIAR 118
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
 146-244 4.31e-03

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 36.87  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 146 VDDDVTQLALMSAYLKDKFN---VITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNlkSQLSVVMLTGD 222
Cdd:cd17565     4 VDDDKNIIKILSDIIEDDDLgevVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTG--SNGKFIMISQV 81

                          90       100
                  ....*....|....*....|..
gi 1222444026 223 DSEEVISKINRLGVDDYLIKPV 244
Cdd:cd17565    82 SDKEMIGKAYQAGIEFFINKPI 103
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
 143-243 5.14e-03

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 36.61  E-value: 5.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIYVDDDVTQLALMSAYLKD-KFNVITCENIDAGWQAI--LTSDASILLLDHKLKQGTCEPLLEKLNKSNLKSQLSVVML 219
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKcSYEVTAASDGLQAWDVLedEQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMM 80

                          90       100
                  ....*....|....*....|....
gi 1222444026 220 TGDDSEEVISKINRLGVDDYLIKP 243
Cdd:cd17582    81 SSQDSVGVVFKCLSKGAADYLVKP 104
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
 142-259 5.47e-03

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 36.97  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 142 SIIYVDDDVTQLALMSAYL-KDKFNVITCENIDAGWQAILTSDASILLLDHKL--KQGtceplLEKLNKSNLKSQLSVVM 218
Cdd:cd19939     1 RILIVEDELELARLTRDYLiKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLpgMDG-----LTVCREVREHSHVPILM 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1222444026 219 LTG--DDSEEVISKinRLGVDDYLIKPVKKNKLLQSIERVTHR 259
Cdd:cd19939    76 LTArtEEMDRVLGL--EMGADDYLCKPFSPRELLARVRALLRR 116
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 42-128 7.42e-03

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


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 35.71  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026  42 LVATEYLTNLIRHNEGDEQLIMLRIS-QINNDTYQLTFVDELKPYNLFKQNNSSWTLAsdelvEGGMGVELIRHyFADA- 119
Cdd:cd16936     3 LAVSEAVTNAVRHAYRHDGPGPVRLElDLDPDRLRVEVTDSGPGFDPLRPADPDAGLR-----EGGRGLALIRA-LMDEv 76

                          90
                  ....*....|
gi 1222444026 120 -IYDTRAGKN 128
Cdd:cd16936    77 gYRRTPGGKT 86
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
 143-255 7.96e-03

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 37.77  E-value: 7.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 143 IIY-VDDDVTQLALMSAYLKDK-FNVITCENIDAGWQAILTSDASILLLDHKLkqgtceP------LLEKLNKsnLKSQL 214
Cdd:COG4566     1 TVYiVDDDEAVRDSLAFLLESAgLRVETFASAEAFLAALDPDRPGCLLLDVRM------PgmsgleLQEELAA--RGSPL 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1222444026 215 SVVMLTGD-DSEEVISKInRLGVDDYLIKPVKKNKLLQSIER 255
Cdd:COG4566    73 PVIFLTGHgDVPMAVRAM-KAGAVDFLEKPFDDQALLDAVRR 113
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
 146-256 8.54e-03

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: 36.10  E-value: 8.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222444026 146 VDDDVTQLALMSAYL-KDKFNVITCENIDAGWQAILTSDASILLLDHKLKQGTCEPLLEKLNKSNLKSQLSVVMLTGDDS 224
Cdd:cd19937     3 VDDEEDIVELLKYNLeKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAKGE 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1222444026 225 EevISKIN--RLGVDDYLIKPVKKNKLLQSIERV 256
Cdd:cd19937    83 E--FDKVLglELGADDYITKPFSPRELLARVKAV 114
 
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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