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Conserved domains on  [gi|898527763|ref|WP_049594865|]
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sigma-54 dependent transcriptional regulator [Acinetobacter baumannii]

Protein Classification

sigma-54-dependent transcriptional regulator( domain architecture ID 11454220)

sigma-54 factor interaction domain-containing protein with a domain similar to that found in the response regulator FleR from Pseudomonas aeruginosa

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
4-464 0e+00

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: 525.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   4 QQPLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVL 83
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  84 TAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKVEHDAAENALenklLIGRSLPIQQLRIAIKKIARSQAP 163
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSG----LIGRSPAMQEVRRLIEKVAPSDAT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 164 VFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQDKQGLILSAHGGSLFLDEIAE 243
Cdd:COG2204  157 VLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 244 LPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGEDVLLLAN 323
Cdd:COG2204  237 MPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLAR 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 324 HFIQKICMEWETPSKqLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDATIDISHlhpaplranisnpfvsatqniqt 403
Cdd:COG2204  317 HFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAED----------------------- 372
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 898527763 404 tvaapqvvkklpsegLERYLENIEKDILINALNMTHWNRTLAAKKLGMTFRSLRYRLKKFG 464
Cdd:COG2204  373 ---------------LPEALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
4-464 0e+00

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: 525.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   4 QQPLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVL 83
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  84 TAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKVEHDAAENALenklLIGRSLPIQQLRIAIKKIARSQAP 163
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSG----LIGRSPAMQEVRRLIEKVAPSDAT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 164 VFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQDKQGLILSAHGGSLFLDEIAE 243
Cdd:COG2204  157 VLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 244 LPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGEDVLLLAN 323
Cdd:COG2204  237 MPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLAR 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 324 HFIQKICMEWETPSKqLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDATIDISHlhpaplranisnpfvsatqniqt 403
Cdd:COG2204  317 HFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAED----------------------- 372
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 898527763 404 tvaapqvvkklpsegLERYLENIEKDILINALNMTHWNRTLAAKKLGMTFRSLRYRLKKFG 464
Cdd:COG2204  373 ---------------LPEALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
8-466 4.47e-129

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 381.89  E-value: 4.47e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAYA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  88 NMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKVEHD--AAENALENKLLIGRSLP----IQQLRIAIKKIARSQ 161
Cdd:PRK11361  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEirHLHQALSTSWQWGHILTnspaMMDICKDTAKIALSQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 162 APVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQDKQGLILSAHGGSLFLDEI 241
Cdd:PRK11361 167 ASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDEI 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 242 AELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGEDVLLL 321
Cdd:PRK11361 247 GEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLL 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 322 ANHFIQKICMEWETPSKQLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDATIDISHLhPAPLRANISNPFVSatqni 401
Cdd:PRK11361 327 ANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDL-PPQIRQPVCNAGEV----- 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 898527763 402 qttvaapqvvKKLPS--EGLERYLENIEKDILINALNMTHWNRTLAAKKLGMTFRSLRYRLKKFGLD 466
Cdd:PRK11361 401 ----------KTAPVgeRNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
8-461 7.03e-120

nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response regulator that is phosphorylated by NtrB and interacts with sigma-54. NtrC usually controls the expression of glutamine synthase, GlnA, and may be called GlnL, GlnG, etc. [Central intermediary metabolism, Nitrogen metabolism, Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 273818 [Multi-domain]  Cd Length: 463  Bit Score: 358.67  E-value: 7.03e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763    8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   88 NMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALN----RQKVEHDAAENAlENKLLIGRSLPIQQLRIAIKKIARSQAP 163
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAhaqeQVALPADAGEAE-DSAELIGEAPAMQEVFRAIGRLSRSDIT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  164 VFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQDKQGLILSAHGGSLFLDEIAE 243
Cdd:TIGR01818 160 VLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEIGD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  244 LPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGEDVLLLAN 323
Cdd:TIGR01818 240 MPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRLAR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  324 HFIQKICMEWETPSKQLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDATIDISHLHP--APLRANISNPFVSATQNI 401
Cdd:TIGR01818 320 HFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAelALTGRPASAPDSDGQDSW 399
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 898527763  402 QTTVA--APQVVKKLPSEGLERYLENIEKDILINALNMTHWNRTLAAKKLGMTFRSLRYRLK 461
Cdd:TIGR01818 400 DEALEawAKQALSRGEQGLLDRALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKLK 461
Sigma54_activat pfam00158
Sigma-54 interaction domain;
140-306 3.38e-98

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 292.38  E-value: 3.38e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  140 LIGRSLPIQQLRIAIKKIARSQAPVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTG 219
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  220 ATQDKQGLILSAHGGSLFLDEIAELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFF 299
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*..
gi 898527763  300 RIHVMDL 306
Cdd:pfam00158 161 RLNVIPI 167
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
8-107 2.19e-38

phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR and similar proteins; Pseudomonas aeruginosa PilR is the response regulator of the PilS/PilR two-component regulatory system (PilSR TCS) that acts in conjunction with sigma-54 to regulate the expression of type 4 pilus (T4P) major subunit PilA. In addition, the PilSR TCS regulates flagellum-dependent swimming motility and pilus-dependent twitching motility. PilR contains an N-terminal REC domain, a central sigma-54 interaction domain, and a C-terminal Fis-type helix-turn-helix DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 134.97  E-value: 2.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                         90       100
                 ....*....|....*....|
gi 898527763  88 NMDIAIAALKAGAFDFVSKP 107
Cdd:cd19926   81 SLDTAIEALKAGAFDFLTKP 100
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
163-287 1.29e-08

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 53.92  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   163 PVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMES---ELFGHKKGSFTGATQDKQG--LILSAHGGSLF 237
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPDVLI 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 898527763   238 LDEIAELPLSMQVKLLRAVQEKKirpVGSDQEIDVDFRVISASHQDLDLL 287
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEELR---LLLLLKSEKNLTVILTTNDEKDLG 130
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
4-464 0e+00

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: 525.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   4 QQPLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVL 83
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  84 TAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKVEHDAAENALenklLIGRSLPIQQLRIAIKKIARSQAP 163
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSG----LIGRSPAMQEVRRLIEKVAPSDAT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 164 VFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQDKQGLILSAHGGSLFLDEIAE 243
Cdd:COG2204  157 VLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 244 LPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGEDVLLLAN 323
Cdd:COG2204  237 MPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLAR 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 324 HFIQKICMEWETPSKqLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDATIDISHlhpaplranisnpfvsatqniqt 403
Cdd:COG2204  317 HFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAED----------------------- 372
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 898527763 404 tvaapqvvkklpsegLERYLENIEKDILINALNMTHWNRTLAAKKLGMTFRSLRYRLKKFG 464
Cdd:COG2204  373 ---------------LPEALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
112-466 1.50e-153

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 443.83  E-value: 1.50e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 112 HLDQLLQKALNRQKVEHDAAENALENklLIGRSLPIQQLRIAIKKIARSQAPVFVTGESGTGKEVVANLVHRLSNRSEGP 191
Cdd:COG3829  114 ELKRLERKLREEELERGLSAKYTFDD--IIGKSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPRRDGP 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 192 FIAINCGAIPTELMESELFGHKKGSFTGATQ-DKQGLILSAHGGSLFLDEIAELPLSMQVKLLRAVQEKKIRPVGSDQEI 270
Cdd:COG3829  192 FVAVNCAAIPENLLESELFGYEKGAFTGAKKgGKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGGTKPI 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 271 DVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGEDVLLLANHFIQKICMEWETPSKQLTEAAKTYLLQ 350
Cdd:COG3829  272 PVDVRIIAATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGISPEALELLLA 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 351 QHFPGNVRELRNMIERAITLSEDATIDISHLhPAPLRANISNPFVSATQNIQTTvaapqvvkklpsegleryLENIEKDI 430
Cdd:COG3829  352 YDWPGNVRELENVIERAVVLSEGDVITPEHL-PEYLLEEAEAASAAEEGSLKEA------------------LEEVEKEL 412
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 898527763 431 LINALNMTHWNRTLAAKKLGMTFRSLRYRLKKFGLD 466
Cdd:COG3829  413 IEEALEKTGGNKSKAAKALGISRSTLYRKLKKYGIK 448
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
8-466 4.47e-129

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 381.89  E-value: 4.47e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAYA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  88 NMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKVEHD--AAENALENKLLIGRSLP----IQQLRIAIKKIARSQ 161
Cdd:PRK11361  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEirHLHQALSTSWQWGHILTnspaMMDICKDTAKIALSQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 162 APVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQDKQGLILSAHGGSLFLDEI 241
Cdd:PRK11361 167 ASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTLLLDEI 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 242 AELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGEDVLLL 321
Cdd:PRK11361 247 GEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLL 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 322 ANHFIQKICMEWETPSKQLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDATIDISHLhPAPLRANISNPFVSatqni 401
Cdd:PRK11361 327 ANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDL-PPQIRQPVCNAGEV----- 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 898527763 402 qttvaapqvvKKLPS--EGLERYLENIEKDILINALNMTHWNRTLAAKKLGMTFRSLRYRLKKFGLD 466
Cdd:PRK11361 401 ----------KTAPVgeRNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
8-461 7.03e-120

nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response regulator that is phosphorylated by NtrB and interacts with sigma-54. NtrC usually controls the expression of glutamine synthase, GlnA, and may be called GlnL, GlnG, etc. [Central intermediary metabolism, Nitrogen metabolism, Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 273818 [Multi-domain]  Cd Length: 463  Bit Score: 358.67  E-value: 7.03e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763    8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   88 NMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALN----RQKVEHDAAENAlENKLLIGRSLPIQQLRIAIKKIARSQAP 163
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERALAhaqeQVALPADAGEAE-DSAELIGEAPAMQEVFRAIGRLSRSDIT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  164 VFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQDKQGLILSAHGGSLFLDEIAE 243
Cdd:TIGR01818 160 VLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEIGD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  244 LPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGEDVLLLAN 323
Cdd:TIGR01818 240 MPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRLAR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  324 HFIQKICMEWETPSKQLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDATIDISHLHP--APLRANISNPFVSATQNI 401
Cdd:TIGR01818 320 HFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAelALTGRPASAPDSDGQDSW 399
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 898527763  402 QTTVA--APQVVKKLPSEGLERYLENIEKDILINALNMTHWNRTLAAKKLGMTFRSLRYRLK 461
Cdd:TIGR01818 400 DEALEawAKQALSRGEQGLLDRALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKLK 461
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
140-464 5.40e-110

Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 338.41  E-value: 5.40e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 140 LIGRSLPIQQLRIAIKKIARSQAPVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTG 219
Cdd:COG3284  323 LAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESELFGYEPGAFTG 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 220 A-TQDKQGLILSAHGGSLFLDEIAELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLF 298
Cdd:COG3284  403 ArRKGRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRDLRELVAAGRFREDLY 482
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 299 FRIHVMDLILPPLRERgEDVLLLANHFIQKICMEWETPSkqLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDATIDI 378
Cdd:COG3284  483 YRLNGLTLTLPPLRER-EDLPALIEHLLRELAAGRGPLR--LSPEALALLAAYPWPGNVRELRNVLRTALALADGGVITV 559
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 379 SHLhPAPLRAnisnpfvsatqniQTTVAAPQVVKKLPSegleryLENIEKDILINALNMTHWNRTLAAKKLGMTfRSLRY 458
Cdd:COG3284  560 EDL-PDELRA-------------ELAAAAPAAAAPLTS------LEEAERDAILRALRACGGNVSAAARALGIS-RSTLY 618

                 ....*..
gi 898527763 459 R-LKKFG 464
Cdd:COG3284  619 RkLKRYG 625
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1-462 2.78e-106

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 323.14  E-value: 2.78e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   1 MAEQQPLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPI 80
Cdd:PRK10365   1 MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  81 AVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKAL-NRQKVEHDAAENALENKLLIGRSLPIQQLRIAIKKIAR 159
Cdd:PRK10365  81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALaHTHSIDAETPAVTASQFGMVGKSPAMQHLLSEIALVAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 160 SQAPVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQDKQGLILSAHGGSLFLD 239
Cdd:PRK10365 161 SEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 240 EIAELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGEDVL 319
Cdd:PRK10365 241 EIGDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 320 LLANHFIQKICMEWETPSKQLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDATIDISHLhpaPLranisnpfvsatq 399
Cdd:PRK10365 321 LLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISEREL---PL------------- 384
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 898527763 400 niqttVAAPQVVKKLPSEGLERYLEnIEKDILINALNMTHWNRTLAAKKLGMTFRSLRYRLKK 462
Cdd:PRK10365 385 -----AIASTPIPLGQSQDIQPLVE-VEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
8-465 4.07e-103

PEP-CTERM-box response regulator transcription factor; Members of this protein family share full-length homology with (but do not include) the acetoacetate metabolism regulatory protein AtoC (see SP|Q06065). These proteins have a Fis family DNA binding sequence (pfam02954), a response regulator receiver domain (pfam00072), and sigma-54 interaction domain (pfam00158). [Regulatory functions, DNA interactions]


Pssm-ID: 274348 [Multi-domain]  Cd Length: 445  Bit Score: 315.15  E-value: 4.07e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763    8 VLLVDDeeDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLP---DGS--GLDLVKHVSQNYPNTPIAV 82
Cdd:TIGR02915   1 LLIVED--DLGLQKQLKWSFADYELAVAADRESAIALVRRHEPAVVTLDLGLPpdaDGAseGLAALQQILAIAPDTKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   83 LTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKVEHD-----AAENALENKLLIGRSLPIQQLRIAIKKI 157
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETEnrrlqSALGGTALRGLITSSPGMQKICRTIEKI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  158 ARSQAPVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQDKQGLILSAHGGSLF 237
Cdd:TIGR02915 159 APSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTLF 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  238 LDEIAELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGED 317
Cdd:TIGR02915 239 LDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDGD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  318 VLLLANHFIQKICMEWETPSKQLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDATIDISHLHpAPLRANISNPFvsa 397
Cdd:TIGR02915 319 AVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAEDLG-LDARERAETPL--- 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 898527763  398 tqniqttvaapqvvkklpSEGLERYLENIEKDILINALNMTHWNRTLAAKKLGMTFRSLRYRLKKFGL 465
Cdd:TIGR02915 395 ------------------EVNLREVRERAEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGI 444
PRK15115 PRK15115
response regulator GlrR; Provisional
1-376 8.28e-100

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 306.38  E-value: 8.28e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   1 MAEQQPLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPI 80
Cdd:PRK15115   1 MSRKPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  81 AVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKVEHDAAENALenklLIGRSLPIQQLRIAIKKIARS 160
Cdd:PRK15115  81 IILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAPATDERWREA----IVTRSPLMLRLLEQARMVAQS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 161 QAPVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQDKQGLILSAHGGSLFLDE 240
Cdd:PRK15115 157 DVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 241 IAELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGEDVLL 320
Cdd:PRK15115 237 IGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPL 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 898527763 321 LANHFIQKICMEWETPSKQLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDATI 376
Cdd:PRK15115 317 LANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVI 372
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
117-466 2.55e-98

Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein for nitrogen fixation. The model produces scores between the trusted and noise cutoffs for a well-described NifA homolog in Aquifex aeolicus (which lacks nitrogenase), for transcriptional activators of alternative nitrogenases (VFe or FeFe instead of MoFe), and truncated forms. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, DNA interactions]


Pssm-ID: 273817 [Multi-domain]  Cd Length: 534  Bit Score: 305.49  E-value: 2.55e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  117 LQKALNRQKVEHDAAENALENkLLIGRSLPIQQLRIAIKKIARSQAPVFVTGESGTGKEVVANLVHRLSNRSEGPFIAIN 196
Cdd:TIGR01817 176 LSKQLRDKAPEIARRRSGKED-GIIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVN 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  197 CGAIPTELMESELFGHKKGSFTGATQDKQGLILSAHGGSLFLDEIAELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRV 276
Cdd:TIGR01817 255 CAALSETLLESELFGHEKGAFTGAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRL 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  277 ISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGEDVLLLANHFIQKICMEWETPSkQLTEAAKTYLLQQHFPGN 356
Cdd:TIGR01817 335 VAATNRDLEEAVAKGEFRADLYYRINVVPIFLPPLRERREDIPLLAEAFLEKFNRENGRPL-TITPSAIRVLMSCKWPGN 413
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  357 VRELRNMIERAITLSEDATIDISHL-------HPAPLRANISNPFVSATQNIQTTVAAPQVVKKLPSEGLERYLENIEKD 429
Cdd:TIGR01817 414 VRELENCLERTATLSRSGTITRSDFscqsgqcLSPMLAKTCPHGHISIDPLAGTTPPHSPASAALPGEPGLSGPTLSERE 493
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 898527763  430 ILINALNMTHWNRTLAAKKLGMTFRSLRYRLKKFGLD 466
Cdd:TIGR01817 494 RLIAALEQAGWVQAKAARLLGMTPRQVGYALRKLNIE 530
Sigma54_activat pfam00158
Sigma-54 interaction domain;
140-306 3.38e-98

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 292.38  E-value: 3.38e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  140 LIGRSLPIQQLRIAIKKIARSQAPVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTG 219
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  220 ATQDKQGLILSAHGGSLFLDEIAELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFF 299
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*..
gi 898527763  300 RIHVMDL 306
Cdd:pfam00158 161 RLNVIPI 167
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
4-466 5.30e-95

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 294.86  E-value: 5.30e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   4 QQPLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVL 83
Cdd:PRK10923   2 QRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  84 TAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALN--RQKVEHDAAENALENKLLIGRSLPIQQLRIAIKKIARSQ 161
Cdd:PRK10923  82 TAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAIShyQEQQQPRNIQVNGPTTDIIGEAPAMQDVFRIIGRLSRSS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 162 APVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQDKQGLILSAHGGSLFLDEI 241
Cdd:PRK10923 162 ISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEI 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 242 AELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGEDVLLL 321
Cdd:PRK10923 242 GDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPRL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 322 ANHFIQKICMEWETPSKQLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDATIDISHLHPAPLRANI-SNPFVSATQN 400
Cdd:PRK10923 322 ARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESTVpESTSQMQPDS 401
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 898527763 401 IQTTVA--APQVVKKLPSEGLERYLENIEKDILINALNMTHWNRTLAAKKLGMTFRSLRYRLKKFGLD 466
Cdd:PRK10923 402 WATLLAqwADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 469
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
140-382 3.74e-94

Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid transport and metabolism];


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 294.02  E-value: 3.74e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 140 LIGRSLPIQQLRIAIKKIARSQAPVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTG 219
Cdd:COG3283  206 IVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAALPDDVAESELFGYAPGAFGN 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 220 ATQDKQGLILSAHGGSLFLDEIAELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFF 299
Cdd:COG3283  286 AREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICATQKDLAELVQEGEFREDLYY 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 300 RIHVMDLILPPLRERGEDVLLLANHFIQKICMEWETPSKQLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDATIDIS 379
Cdd:COG3283  366 RLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLENALYRAVSLLEGDELTPE 445

                 ...
gi 898527763 380 HLH 382
Cdd:COG3283  446 DLQ 448
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
77-465 3.52e-91

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 286.30  E-value: 3.52e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  77 NTPIAVLTaygnmdiaIAALKAGAFDFVSK------------PVNQVHL-DQLLQKALNRQKVEHDAAENALENKLLIGR 143
Cdd:PRK05022 121 GRLIGALT--------LDALDPGQFDAFSDeelralaalaaaTLRNALLiEQLESQAELPQDVAEFLRQEALKEGEMIGQ 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 144 SLPIQQLRIAIKKIARSQAPVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQD 223
Cdd:PRK05022 193 SPAMQQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAESELFGHVKGAFTGAISN 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 224 KQGLILSAHGGSLFLDEIAELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHV 303
Cdd:PRK05022 273 RSGKFELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYHRLSV 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 304 MDLILPPLRERGEDVLLLANHFIQKICMEWETPSKQLTEAAKTYLLQQHFPGNVRELRNMIERAITL------SEDATID 377
Cdd:PRK05022 353 FPLSVPPLRERGDDVLLLAGYFLEQNRARLGLRSLRLSPAAQAALLAYDWPGNVRELEHVISRAALLarargaGRIVTLE 432
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 378 ISHLhpaplraNISNPFVSATQNIQTTVAAPqvvkklPSEGLERYLENIEKDILINALNMTHWNRTLAAKKLGMTfRSLR 457
Cdd:PRK05022 433 AQHL-------DLPAEVALPPPEAAAAPAAV------VSQNLREATEAFQRQLIRQALAQHQGNWAAAARALELD-RANL 498

                 ....*....
gi 898527763 458 YRL-KKFGL 465
Cdd:PRK05022 499 HRLaKRLGL 507
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
90-462 3.37e-88

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 279.30  E-value: 3.37e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  90 DIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKVEHDAAENALENKL----LIGRSLPIQQLRIAIKKIARSQAPVF 165
Cdd:PRK15424 167 DLAEEAGMTGIFIYSAATVRQAFEDALDMTRMTLRHNTHYATRNALRTRYvlgdLLGQSPQMEQVRQTILLYARSSAAVL 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 166 VTGESGTGKEVVANLVHR--------LSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQD-KQGLILSAHGGSL 236
Cdd:PRK15424 247 IQGETGTGKELAAQAIHReyfarhdaRQGKKSHPFVAVNCGAIAESLLEAELFGYEEGAFTGSRRGgRAGLFEIAHGGTL 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 237 FLDEIAELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGE 316
Cdd:PRK15424 327 FLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQPVPVDVRVISATHCDLEEDVRQGRFRRDLFYRLSILRLQLPPLRERVA 406
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 317 DVLLLANHFIQKICMEWETP----SKQLTEAAKTYLLQQHFPGNVRELRNMIER-AITLSEDATIDIShlhPAPLRANIS 391
Cdd:PRK15424 407 DILPLAESFLKQSLAALSAPfsaaLRQGLQQCETLLLHYDWPGNVRELRNLMERlALFLSVEPTPDLT---PQFLQLLLP 483
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 898527763 392 NPFVSATQNIQTTVAAPQVvkklpSEGLERYleniekdilinalnmtHWNRTLAAKKLGMTFRSLRYRLKK 462
Cdd:PRK15424 484 ELARESAKTPAPRLLAATL-----QQALERF----------------NGDKTAAANYLGISRTTLWRRLKA 533
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
90-462 2.63e-87

propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists for the catabolism of propionate by way of propionyl-CoA. Members of this family represent the transcriptional regulatory protein PrpR, whose gene is found in most cases divergently transcribed from an operon for the methylcitric acid cycle of propionate catabolism. 2-methylcitric acid, a catabolite by this pathway, is a coactivator of PrpR. [Regulatory functions, DNA interactions]


Pssm-ID: 274079 [Multi-domain]  Cd Length: 526  Bit Score: 276.74  E-value: 2.63e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   90 DIAIAALKAGAFDFVSKPVNQVhLDQLLQKA----LNRQKVEHDAAENALENKL----LIGRSLPIQQLRIAIKKIARSQ 161
Cdd:TIGR02329 157 DLAEQAGLHGVFLYSADSVRQA-FDDALDVAratrLRQAATLRSATRNQLRTRYrlddLLGASAPMEQVRALVRLYARSD 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  162 APVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQ-DKQGLILSAHGGSLFLDE 240
Cdd:TIGR02329 236 ATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEAELFGYEEGAFTGARRgGRTGLIEAAHRGTLFLDE 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  241 IAELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGEDVLL 320
Cdd:TIGR02329 316 IGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAVQQGRFRRDLFYRLSILRIALPPLRERPGDILP 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  321 LANHFIQKICMEWETP----SKQLTEAAKTYLLQQHFPGNVRELRNMIER-AITLSEDATIDIShlhPAPLRANISNPFV 395
Cdd:TIGR02329 396 LAAEYLVQAAAALRLPdseaAAQVLAGVADPLQRYPWPGNVRELRNLVERlALELSAMPAGALT---PDVLRALAPELAE 472
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  396 SATQNIQTTVAAPQ---VVKKLPSEGLERYleniekdilinalnmtHWNRTLAAKKLGMTFRSLRYRLKK 462
Cdd:TIGR02329 473 ASGKGKTSALSLRErsrVEALAVRAALERF----------------GGDRDAAAKALGISRTTLWRRLKA 526
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
156-465 1.87e-79

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 249.97  E-value: 1.87e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 156 KIARSQAPVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQDKQGLILSAHGGS 235
Cdd:PRK11608  24 RLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTGAQKRHPGRFERADGGT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 236 LFLDEIAELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIhVMDLI-LPPLRER 314
Cdd:PRK11608 104 LFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLDRL-AFDVVqLPPLRER 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 315 GEDVLLLANHFIQKICMEWETP-SKQLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDAtidishlhPAPLRANISNP 393
Cdd:PRK11608 183 QSDIMLMAEHFAIQMCRELGLPlFPGFTERARETLLNYRWPGNIRELKNVVERSVYRHGTS--------EYPLDNIIIDP 254
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 898527763 394 FVSATQNIQTTVAAPQVVKKLPSEgLERYLENIEKDILINALNMTHWNRTLAAKKLGMTFRSLRYRLKKFGL 465
Cdd:PRK11608 255 FKRRPAEEAIAVSETTSLPTLPLD-LREWQHQQEKELLQRSLQQAKFNQKRAAELLGLTYHQLRALLKKHQI 325
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
160-466 3.43e-78

FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 442823 [Multi-domain]  Cd Length: 338  Bit Score: 247.07  E-value: 3.43e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 160 SQAPVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESelfghkkgsftgatqdkqglilsahggslfld 239
Cdd:COG3604  114 SLAAVAILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES-------------------------------- 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 240 eiaelplsmqvkllraVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGEDVL 319
Cdd:COG3604  162 ----------------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDIP 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 320 LLANHFIQKICMEWETPSKQLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDATIDISHLHPAPLRAnisnpfvsatq 399
Cdd:COG3604  226 LLAEHFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDLAPGSREA----------- 294
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 898527763 400 niqttvaapqvvkklpsegleryLENIEKDILINALNMTHWNRTLAAKKLGMTFRSLRYRLKKFGLD 466
Cdd:COG3604  295 -----------------------LEEVEREHILEALERTGGNIAGAARLLGLTPSTLRSRMKKLGIK 338
PRK10820 PRK10820
transcriptional regulator TyrR;
140-372 8.41e-67

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 223.02  E-value: 8.41e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 140 LIGRSLPIQQLRIAIKKIARSQAPVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTG 219
Cdd:PRK10820 206 IVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAPGAYPN 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 220 ATQDKQGLILSAHGGSLFLDEIAELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFF 299
Cdd:PRK10820 286 ALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGEFREDLYY 365
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 898527763 300 RIHVMDLILPPLRERGEDVLLLANHFIQKICMEWETPSKQLTEAAKTYLLQQHFPGNVRELRNMIERAITLSE 372
Cdd:PRK10820 366 RLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNAIYRALTQLE 438
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
140-468 9.00e-61

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 210.46  E-value: 9.00e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 140 LIGRSLPIQQLRIAIKKIARSQAPVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHKKGSFTG 219
Cdd:PRK15429 378 IIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHERGAFTG 457
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 220 ATQDKQGLILSAHGGSLFLDEIAELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFF 299
Cdd:PRK15429 458 ASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREFRSDLYY 537
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 300 RIHVMDLILPPLRERGEDVLLLANHFIQKICMEWETPSKQLTEAAKTYLLQQHFPGNVRELRNMIERAITLSEDATIdis 379
Cdd:PRK15429 538 RLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNVRELENVIERAVLLTRGNVL--- 614
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 380 hlhpaplraNISNPFVSAtqniqTTVAAPQVVKKLPSEGLERYleniekDILINALNMThwNRTL-----AAKKLGMTFR 454
Cdd:PRK15429 615 ---------QLSLPDITL-----PEPETPPAATVVAQEGEDEY------QLIVRVLKET--NGVVagpkgAAQRLGLKRT 672
                        330
                 ....*....|....
gi 898527763 455 SLRYRLKKFGLDTE 468
Cdd:PRK15429 673 TLLSRMKRLGIDKS 686
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
107-466 5.34e-52

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 185.65  E-value: 5.34e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 107 PVNQVHldQLLQKALNRQKVEHDAaenalenklLIGRSLPIQQL-RIAiKKIARSQAPVFVTGESGTGKEVVANLVHRLS 185
Cdd:PRK11388 305 PVEQMR--QLMTSQLGKVSHTFDH---------MPQDSPQMRRLiHFG-RQAAKSSFPVLLCGEEGVGKALLAQAIHNES 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 186 NRSEGPFIAINCGAIPTELMESELFGhkkgsfTGATQDKQGLiLS----AHGGSLFLDEIAELPLSMQVKLLRAVQEKKI 261
Cdd:PRK11388 373 ERAAGPYIAVNCQLYPDEALAEEFLG------SDRTDSENGR-LSkfelAHGGTLFLEKVEYLSPELQSALLQVLKTGVI 445
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 262 RPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIHVMDLILPPLRERGEDVLLLANHFIQKICMEWETpSKQLT 341
Cdd:PRK11388 446 TRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRQLYYALHAFEITIPPLRMRREDIPALVNNKLRSLEKRFST-RLKID 524
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 342 EAAKTYLLQQHFPGNVRELRNMIERAITLSEDATIDISHLhPAPLRanisnpfvsaTQNIQTTVAAPQVVKKLPsegler 421
Cdd:PRK11388 525 DDALARLVSYRWPGNDFELRSVIENLALSSDNGRIRLSDL-PEHLF----------TEQATDDVSATRLSTSLS------ 587
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 898527763 422 yLENIEKDILINALNMTHWNRTLAAKKLGMTFRSLRYRLKKFGLD 466
Cdd:PRK11388 588 -LAELEKEAIINAAQVCGGRIQEMAALLGIGRTTLWRKMKQHGID 631
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
147-378 3.33e-49

Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 443688 [Multi-domain]  Cd Length: 534  Bit Score: 176.18  E-value: 3.33e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 147 IQQL-RIAIkkiaRSQAPVFVTGESGTGKEVVANLVHRLS---NRSEGPFIAINCGAIPTELMESELFGHKKGSFTGATQ 222
Cdd:COG4650  197 IEQIeRVAI----RSRAPILLTGPTGAGKSQLARRIYELKkarHQVSGRFVEVNCATLRGDGAMSALFGHVKGAFTGAVS 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 223 DKQGLILSAHGGSLFLDEIAELPLSMQVKLLRAVQEKKIRPVGSDQEIDVDFRVISASHQDLDLLVRQGKFRQDLFFRIH 302
Cdd:COG4650  273 DRAGLLRSADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARIN 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 303 VMDLILPPLRERGEDV-----LLLANHfiqkicmewetpSKQL-------TEAAKTYLlqqHF--------PGNVRELRN 362
Cdd:COG4650  353 LWTFRLPGLAERREDIepnldYELARF------------AREQgrrvrfnKEARARYL---AFatspealwSGNFRDLNA 417
                        250
                 ....*....|....*.
gi 898527763 363 MIERAITLSEDATIDI 378
Cdd:COG4650  418 SVTRMATLAEGGRITV 433
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
8-107 2.19e-38

phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR and similar proteins; Pseudomonas aeruginosa PilR is the response regulator of the PilS/PilR two-component regulatory system (PilSR TCS) that acts in conjunction with sigma-54 to regulate the expression of type 4 pilus (T4P) major subunit PilA. In addition, the PilSR TCS regulates flagellum-dependent swimming motility and pilus-dependent twitching motility. PilR contains an N-terminal REC domain, a central sigma-54 interaction domain, and a C-terminal Fis-type helix-turn-helix DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 134.97  E-value: 2.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                         90       100
                 ....*....|....*....|
gi 898527763  88 NMDIAIAALKAGAFDFVSKP 107
Cdd:cd19926   81 SLDTAIEALKAGAFDFLTKP 100
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1-125 1.77e-27

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: 106.47  E-value: 1.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   1 MAEQQPLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQN--YPNT 78
Cdd:COG0784    1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALprLPDI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 898527763  79 PIAVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQK 125
Cdd:COG0784   81 PIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
3-132 2.54e-27

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: 107.69  E-value: 2.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   3 EQQPLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAV 82
Cdd:COG4567    2 AEDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVV 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 898527763  83 LTAYGNMDIAIAALKAGAFDFVSKPVNQvhlDQLLQkALNRQKVEHDAAE 132
Cdd:COG4567   82 LTGYASIATAVEAIKLGADDYLAKPADA---DDLLA-ALERAEGDAPAPP 127
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
9-107 6.93e-27

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: 103.85  E-value: 6.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   9 LLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYGN 88
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                         90
                 ....*....|....*....
gi 898527763  89 MDIAIAALKAGAFDFVSKP 107
Cdd:cd00156   81 EEDAVRALELGADDYLVKP 99
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
8-118 9.34e-27

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 103.77  E-value: 9.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763    8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 898527763   88 NMDIAIAALKAGAFDFVSKPVNQVHLDQLLQ 118
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
8-118 2.21e-26

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: 102.91  E-value: 2.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd17563    3 LLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGYA 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 898527763  88 NMDIAIAALKAGAFDFVSKPVNqvhLDQLLQ 118
Cdd:cd17563   83 SIATAVEAIKLGADDYLAKPAD---ADEILA 110
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
5-127 8.49e-26

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: 104.27  E-value: 8.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   5 QPLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLT 84
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 898527763  85 AYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKVE 127
Cdd:COG0745   81 ARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAE 123
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
114-364 1.99e-25

Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 109.81  E-value: 1.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 114 DQLLQKALNRQKVEHDAAENALENklLIG--RSL--PIQQLRIAI----KKIarsqaPVFVTGESGTGKEVVANLVHR-- 183
Cdd:COG1221   82 SEYSFVELLAEKENNEEEEDPFDN--LIGanGSLknAIEQAKAAIlyppKGL-----HTLILGPTGVGKSFFAELMYEya 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 184 LSNR---SEGPFIAINCG--AIPTELMESELFGHKKGSFTGATQDKQGLILSAHGGSLFLDEIAELPLSMQVKLLRAVQE 258
Cdd:COG1221  155 IEIGvlpEDAPFVVFNCAdyANNPQLLMSQLFGYVKGAFTGADKDKEGLIEKADGGILFLDEVHRLPPEGQEMLFTFMDK 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 259 KKIRPVG-SDQEIDVDFRVISASHQDLD--LL---VRqgkfrqdlffRIHVmdLI-LPPLRERG-EDVLLLANHFIQkic 330
Cdd:COG1221  235 GIYRRLGeTEKTRKANVRIIFATTEDPEssLLktfLR----------RIPM--VIkLPSLEERSlEERLELIKHFFK--- 299
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 898527763 331 MEWETPSKQLT---EAAKTyLLQQHFPGNVRELRNMI 364
Cdd:COG1221  300 EEAKRLNKPIKvskEVLKA-LLLYDCPGNIGQLKSDI 335
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
8-128 5.64e-25

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: 99.19  E-value: 5.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 898527763  88 NMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKVEH 128
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKLTK 121
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
5-113 7.78e-24

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: 98.06  E-value: 7.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   5 QPLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQN--YPNTPIAV 82
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADprTADIPIIF 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 898527763  83 LTAYGNMDIAIAALKAGAFDFVSKPVNQVHL 113
Cdd:COG3706   81 LTALDDEEDRARALEAGADDYLTKPFDPEEL 111
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
8-125 1.39e-23

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 95.81  E-value: 1.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGI--KTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTA 85
Cdd:COG4565    6 VLIVEDDPMVAELLRRYLERLPGfeVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVIVITA 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 898527763  86 YGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQK 125
Cdd:COG4565   86 ARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRR 125
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
2-139 4.13e-22

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: 94.46  E-value: 4.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   2 AEQQPLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYP--NTP 79
Cdd:COG3437    3 TGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPStrDIP 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  80 IAVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKVEHDAAENALENKL 139
Cdd:COG3437   83 VIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKL 142
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
141-311 5.54e-22

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 91.64  E-value: 5.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  141 IGRSLPIQQLRIAIKKIARSQAPVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMEselfghkkgsftga 220
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLE-------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  221 tqdkqglilSAHGGSLFLDEIAELPLSMQVKLLRAVQEkkirpvgSDQEidvDFRVISASHQDLDLLVRQGKFRQDLFFR 300
Cdd:pfam14532  67 ---------QAKGGTLYLKDIADLSKALQKGLLLLLAK-------AEGY---RVRLVCTSSKDLPQLAAAGLFDEQLYFE 127
                         170
                  ....*....|.
gi 898527763  301 IHVMDLILPPL 311
Cdd:pfam14532 128 LSALRLHVPPL 138
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
8-140 1.35e-21

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: 90.24  E-value: 1.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAyrvEQAKQLFTQFHYDAC---LTDLNLPDGSGLDLVKHVSQNYPNTPIAVLT 84
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAF---ADAEEALAALSPDFPgvvISDIRMPGMDGLELLAQIRELDPDLPVILIT 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 898527763  85 AYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALN-RQKVehdaaenaLENKLL 140
Cdd:cd17549   78 GHGDVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEkRRLV--------LENRRL 126
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
9-107 1.69e-21

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: 89.00  E-value: 1.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   9 LLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYGN 88
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80
                         90
                 ....*....|....*....
gi 898527763  89 MDIAIAALKAGAFDFVSKP 107
Cdd:cd17574   81 EEDKVLGLELGADDYITKP 99
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
8-107 8.86e-20

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: 84.05  E-value: 8.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARM-GIKT-HLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTA 85
Cdd:COG4753    2 VLIVDDEPLIREGLKRILEWEaGFEVvGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILSG 81
                         90       100
                 ....*....|....*....|..
gi 898527763  86 YGNMDIAIAALKAGAFDFVSKP 107
Cdd:COG4753   82 YSDFEYAQEAIKLGADDYLLKP 103
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
8-121 1.31e-18

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: 81.39  E-value: 1.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 898527763  88 NMDIAIAALKAGAFDFVSKPVNqvhLDQLL---QKAL 121
Cdd:cd17550   81 TIETAVKATKLGAYDFIEKPLS---LDRLLltiERAL 114
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
8-123 2.20e-18

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 80.61  E-value: 2.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 898527763  88 NMDIAIAALKAGAFDFVSKPvnqVHLDQLLQ--KALNR 123
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVKP---FALEELLArlRALLR 115
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
8-123 3.66e-18

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: 80.07  E-value: 3.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEdlcllmqmtLARMGIKTHL------------AYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNY 75
Cdd:cd17536    1 VLIVDDEP---------LIREGLKKLIdweelgfevvgeAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELY 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 898527763  76 PNTPIAVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNR 123
Cdd:cd17536   72 PDIKIIILSGYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKEE 119
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
147-301 5.93e-18

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 80.65  E-value: 5.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 147 IQQLRIAIKkiARSQAPVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMESELFGHkkgsftGATQDKQG 226
Cdd:cd00009    7 IEALREALE--LPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGH------FLVRLLFE 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 898527763 227 LILSAHGGSLFLDEIAELPLSMQVKLLRAVQEKKIRPVGSDqeidvDFRVISASHQDLDllvrqGKFRQDLFFRI 301
Cdd:cd00009   79 LAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRE-----NVRVIGATNRPLL-----GDLDRALYDRL 143
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
8-117 1.57e-17

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 78.28  E-value: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHV---SQNYPNTPIAVLT 84
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIrelEGGGRRTPIIALT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 898527763  85 AYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLL 117
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
6-108 1.90e-16

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: 75.32  E-value: 1.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   6 PLVLLVDDEEdlcllmqmtLARMGIKTHL---AYRVEQAK------QLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYP 76
Cdd:cd17555    1 ATILVIDDDE---------VVRESIAAYLedsGFQVLQAAdgrqglELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESP 71
                         90       100       110
                 ....*....|....*....|....*....|..
gi 898527763  77 NTPIAVLTAYGNMDIAIAALKAGAFDFVSKPV 108
Cdd:cd17555   72 DTPVIVVSGAGVMSDAVEALRLGAWDYLTKPI 103
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
6-121 2.89e-16

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: 74.75  E-value: 2.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   6 PLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTA 85
Cdd:cd17569    1 PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTG 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 898527763  86 YGNMDIAIAALKAGA-FDFVSKPVNQVHLDQLLQKAL 121
Cdd:cd17569   81 YADLDAAIEAINEGEiYRFLTKPWDDEELKETIRQAL 117
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
8-121 3.90e-16

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


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 74.23  E-value: 3.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd19919    3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAHS 82
                         90       100       110
                 ....*....|....*....|....*....|....
gi 898527763  88 NMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKAL 121
Cdd:cd19919   83 DLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
8-138 5.65e-16

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 77.16  E-value: 5.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEdlcllmqmtLARMGIKTHL-----------AYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYP 76
Cdd:COG3279    4 ILIVDDEP---------LARERLERLLekypdlevvgeASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDP 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 898527763  77 NTPIAVLTAYGNMdiAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKVEHDAAENALENK 138
Cdd:COG3279   75 PPPIIFTTAYDEY--ALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEAKAAAEASPEEKD 134
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
7-139 1.37e-15

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: 75.14  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   7 LVLLVDDEEDLCLLMQMTLARMGikthlaYRVE---QAKQLFTQFHYD--ACL-TDLNLPDGSGLDLVKHVSQNYPNTPI 80
Cdd:COG4566    1 TVYIVDDDEAVRDSLAFLLESAG------LRVEtfaSAEAFLAALDPDrpGCLlLDVRMPGMSGLELQEELAARGSPLPV 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 898527763  81 AVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKAL--NRQKVEHDAAENALENKL 139
Cdd:COG4566   75 IFLTGHGDVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALarDRARRAERARRAELRARL 135
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
8-117 3.34e-15

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: 71.34  E-value: 3.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYP--NTPIAVLTA 85
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWlaNTPAIALTG 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 898527763  86 YGNMDIAIAALKAGaFDF-VSKPVNQVHLDQLL 117
Cdd:cd17580   81 YGQPEDRERALEAG-FDAhLVKPVDPDELIELI 112
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
8-122 4.46e-15

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: 71.39  E-value: 4.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEdlcllmqmtLARMGIKTHLAYR-----------VEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYP 76
Cdd:cd17535    1 VLIVDDHP---------LVREGLRRLLESEpdievvgeaadGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYP 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 898527763  77 NTPIAVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALN 122
Cdd:cd17535   72 DLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
6-121 6.00e-15

phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response regulators contain an N-terminal receiver domain (REC) and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. The Sinorhizobium meliloti two-component system FixL/FixJ regulates nitrogen fixation in response to oxygen during symbiosis. Under microaerobic conditions, the kinase FixL phosphorylates the response regulator FixJ resulting in the regulation of nitrogen fixation genes such as nifA and fixK. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 71.09  E-value: 6.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   6 PLVLLVDDEEDLC-----LLMQMTLArmgIKTHlayrvEQAKQLFTQFHYD--ACL-TDLNLPDGSGLDLVKHVSQNYPN 77
Cdd:cd17537    1 ATVYVVDDDEAVRdslafLLRSVGLA---VKTF-----TSASAFLAAAPPDqpGCLvLDVRMPGMSGLELQDELLARGSN 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 898527763  78 TPIAVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKAL 121
Cdd:cd17537   73 IPIIFITGHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
8-107 8.86e-15

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 70.46  E-value: 8.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd17615    2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKD 81
                         90       100
                 ....*....|....*....|
gi 898527763  88 NMDIAIAALKAGAFDFVSKP 107
Cdd:cd17615   82 SVEDRIAGLTAGGDDYVTKP 101
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
8-107 1.74e-13

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 66.03  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYpNTPIAVLTAYG 87
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWS-AVPVIVLSARD 79
                         90       100
                 ....*....|....*....|
gi 898527763  88 NMDIAIAALKAGAFDFVSKP 107
Cdd:cd17620   80 EESDKIAALDAGADDYLTKP 99
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
8-109 2.25e-13

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: 66.56  E-value: 2.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNyPNTPIAVLTAYG 87
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKT-SQVPVLMLTARG 79
                         90       100
                 ....*....|....*....|..
gi 898527763  88 NMDIAIAALKAGAFDFVSKPVN 109
Cdd:cd17623   80 DDIDRILGLELGADDYLPKPFN 101
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
8-111 3.89e-13

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 65.93  E-value: 3.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAY-RVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQ--NYPNTPIAVLT 84
Cdd:cd17551    3 ILIVDDNPTNLLLLEALLRSAGYLEVVSFtDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRAlpGLEDVPIVMIT 82
                         90       100
                 ....*....|....*....|....*..
gi 898527763  85 AYGNMDIAIAALKAGAFDFVSKPVNQV 111
Cdd:cd17551   83 ADTDREVRLRALEAGATDFLTKPFDPV 109
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
8-123 7.20e-13

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 65.00  E-value: 7.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 898527763  88 NMDIAIAALKAGAFDFVSKPvnqVHLDQLLQ--KALNR 123
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTKP---FHIEELLArlRALIR 115
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
8-143 2.38e-12

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: 65.75  E-value: 2.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIK-THLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPnTPIAVLTAY 86
Cdd:COG3707    6 VLVVDDEPLRRADLREGLREAGYEvVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP-APVILLTAY 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 898527763  87 GNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNR------QKVEHDAAENALENKLLIGR 143
Cdd:COG3707   85 SDPELIERALEAGVSAYLVKPLDPEDLLPALELALARfrelraLRRELAKLREALEERKLIER 147
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
8-107 4.54e-12

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 62.45  E-value: 4.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80
                         90       100
                 ....*....|....*....|
gi 898527763  88 NMDIAIAALKAGAFDFVSKP 107
Cdd:cd17573   81 KTEQEIEAFKEGADDYIAKP 100
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
423-462 2.03e-11

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 58.56  E-value: 2.03e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 898527763  423 LENIEKDILINALNMTHWNRTLAAKKLGMTFRSLRYRLKK 462
Cdd:pfam02954   1 LEEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
8-107 2.27e-11

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 60.15  E-value: 2.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80
                         90       100
                 ....*....|....*....|
gi 898527763  88 NMDIAIAALKAGAFDFVSKP 107
Cdd:cd19935   81 SVEDRVKGLDLGADDYLVKP 100
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
8-107 2.63e-11

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 60.21  E-value: 2.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                         90       100
                 ....*....|....*....|
gi 898527763  88 NMDIAIAALKAGAFDFVSKP 107
Cdd:cd19928   81 TLMTAVKAAERGAFEYLPKP 100
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
8-108 4.15e-11

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 59.93  E-value: 4.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd17554    3 ILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAYS 82
                         90       100
                 ....*....|....*....|.
gi 898527763  88 NMDIAIAALKAGAFDFVSKPV 108
Cdd:cd17554   83 EYKSDFSSWAADAYVVKSSDL 103
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
8-121 5.98e-11

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: 59.66  E-value: 5.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIK-THLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHV--SQNYPNTPIAVLT 84
Cdd:cd19923    3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIraDGALSHLPVLMVT 82
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 898527763  85 AYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKAL 121
Cdd:cd19923   83 AEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
9-124 9.03e-11

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: 58.77  E-value: 9.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   9 LLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYGN 88
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 898527763  89 MDIAIAALKAGAFDFVSKPvnqVHLDQLLQ--KALNRQ 124
Cdd:cd17625   81 VEDRVKGLDLGADDYLPKP---FSLAELLAriRALLRR 115
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
9-107 1.00e-10

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: 58.82  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   9 LLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQN--YPNTPIAVLTAY 86
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDpkTSSIPIIMLTAK 80
                         90       100
                 ....*....|....*....|.
gi 898527763  87 GNMDIAIAALKAGAFDFVSKP 107
Cdd:cd19937   81 GEEFDKVLGLELGADDYITKP 101
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
8-113 1.17e-10

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 58.57  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                         90       100
                 ....*....|....*....|....*.
gi 898527763  88 NMDIAIAALKAGAFDFVSKPVNQVHL 113
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKPFHKDEL 106
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
8-140 1.33e-10

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 61.36  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQfHYDACLTDLNLPDGSGLDLVKHVSQNYpNTPIAVLTAYG 87
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD-SIDLLLLDVMMPKKNGIDTLKELRQTH-QTPVIMLTARG 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 898527763  88 NMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNR-----QKVEHDAAENALENKLL 140
Cdd:PRK10955  82 SELDRVLGLELGADDYLPKPFNDRELVARIRAILRRshwseQQQNNDNGSPTLEVDAL 139
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
8-107 1.43e-10

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


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 58.41  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHV--SQNYPNTPIAVLTA 85
Cdd:cd17618    3 ILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLkrDEMTRDIPIIMLTA 82
                         90       100
                 ....*....|....*....|..
gi 898527763  86 YGNMDIAIAALKAGAFDFVSKP 107
Cdd:cd17618   83 RGEEEDKVRGLEAGADDYITKP 104
ompR PRK09468
osmolarity response regulator; Provisional
1-131 2.35e-10

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 60.76  E-value: 2.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   1 MAEQQPLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPI 80
Cdd:PRK09468   1 MMQENYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPI 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 898527763  81 AVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKVEHDAA 131
Cdd:PRK09468  81 IMLTAKGEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVLRRQAPELPGA 131
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
8-121 3.61e-10

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 57.31  E-value: 3.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGikthlaYRVEQA--------KQLFTQFhyDACLTDLNLPDGSGLDLVKHVSQN--YPN 77
Cdd:cd17562    3 ILAVDDSASIRQMVSFTLRGAG------YEVVEAadgrdalsKAQSKKF--DLIITDQNMPNMDGIELIKELRKLpaYKF 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 898527763  78 TPIAVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKAL 121
Cdd:cd17562   75 TPILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
8-107 3.86e-10

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: 57.05  E-value: 3.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYpNTPIAVLTAYG 87
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTAKD 79
                         90       100
                 ....*....|....*....|
gi 898527763  88 NMDIAIAALKAGAFDFVSKP 107
Cdd:cd17614   80 SEVDKVLGLELGADDYVTKP 99
fixJ PRK09390
response regulator FixJ; Provisional
6-132 3.98e-10

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 59.25  E-value: 3.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   6 PLVLLVDDEEDlcllMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDA---CL-TDLNLPDGSGLDLVKHVSQNYPNTPIA 81
Cdd:PRK09390   4 GVVHVVDDDEA----MRDSLAFLLDSAGFEVRLFESAQAFLDALPGLrfgCVvTDVRMPGIDGIELLRRLKARGSPLPVI 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 898527763  82 VLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNR----QKVEHDAAE 132
Cdd:PRK09390  80 VMTGHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQapeaAKSEAVAAD 134
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
8-119 6.85e-10

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: 56.48  E-value: 6.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEdlcllMQMTLARMGIKTHLAYRV-------EQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPI 80
Cdd:cd19925    3 VLIVEDDP-----MVAEIHRAYVEQVPGFTVigtagtgEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDV 77
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 898527763  81 AVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQK 119
Cdd:cd19925   78 IVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLER 116
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
8-121 9.09e-10

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: 56.13  E-value: 9.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEdlclLMQMTLARmgIKTHLAYRV-------EQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPI 80
Cdd:cd17542    3 VLIVDDAA----FMRMMLKD--ILTKAGYEVvgeaangEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKV 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 898527763  81 AVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKAL 121
Cdd:cd17542   77 IMCSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
8-119 1.50e-09

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: 55.86  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEedlcLLMQMTLARMgIKTHLAYRV-------EQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPnTPI 80
Cdd:cd17541    3 VLIVDDS----AVMRKLLSRI-LESDPDIEVvgtardgEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERP-TPV 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 898527763  81 AVLTAY--GNMDIAIAALKAGAFDFVSKPVNQVHLD------QLLQK 119
Cdd:cd17541   77 VMVSSLteEGAEITLEALELGAVDFIAKPSGGISLDleeiaeELIEK 123
dpiA PRK10046
two-component response regulator DpiA; Provisional
5-126 1.74e-09

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 57.72  E-value: 1.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   5 QPLVLLVDDEEDLCLLMQMTLARM--GI-KTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQ-NYPNTpI 80
Cdd:PRK10046   3 APLTLLIVEDETPLAEMHAEYIRHipGFsQILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQaHYPGD-V 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 898527763  81 AVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKV 126
Cdd:PRK10046  82 VFTTAASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRFRQRKHM 127
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
6-122 6.06e-09

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 53.54  E-value: 6.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   6 PLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNyPNTPIAVLTA 85
Cdd:cd17619    1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQ-SEVGIILVTG 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 898527763  86 YGNMDIAIAALKAGAFDFVSKPVNqvhLDQLLQKALN 122
Cdd:cd17619   80 RDDEVDRIVGLEIGADDYVTKPFN---PRELLVRAKN 113
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
163-287 1.29e-08

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 53.92  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   163 PVFVTGESGTGKEVVANLVHRLSNRSEGPFIAINCGAIPTELMES---ELFGHKKGSFTGATQDKQG--LILSAHGGSLF 237
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRLAlaLARKLKPDVLI 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 898527763   238 LDEIAELPLSMQVKLLRAVQEKKirpVGSDQEIDVDFRVISASHQDLDLL 287
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEELR---LLLLLKSEKNLTVILTTNDEKDLG 130
PRK10643 PRK10643
two-component system response regulator PmrA;
8-136 1.37e-08

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 55.04  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:PRK10643   3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTARD 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 898527763  88 NMDIAIAALKAGAFDFVSKPVNqvhLDQLLQ--KALNRQKVEHdaAENALE 136
Cdd:PRK10643  83 TLEDRVAGLDVGADDYLVKPFA---LEELHAriRALIRRHQGQ--GENELQ 128
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
8-123 1.50e-08

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 55.20  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQnYPNTPIAVLTAYG 87
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQ-WSAIPVIVLSARS 82
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 898527763  88 NMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNR 123
Cdd:PRK10529  83 EESDKIAALDAGADDYLSKPFGIGELQARLRVALRR 118
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
8-107 1.64e-08

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 52.56  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYG 82
                         90       100
                 ....*....|....*....|
gi 898527763  88 NMDIAIAALKAGAFDFVSKP 107
Cdd:cd17553   83 ELDMIQESKELGALTHFAKP 102
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
8-119 1.95e-08

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 52.28  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGL---DLVKHVSqnypNTPIAVLT 84
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFywcREIRQIS----NVPIIFIS 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 898527763  85 AY-GNMDIaIAALKAGAFDFVSKPvnqVHLDQLLQK 119
Cdd:cd18159   77 SRdDNMDQ-VMAINMGGDDYITKP---FDLDVLLAK 108
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
8-60 2.12e-08

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: 50.26  E-value: 2.12e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 898527763     8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLP 60
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
8-121 2.57e-08

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: 52.02  E-value: 2.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIK-THLAYRVEQAKQLFTQFHYDACLTDLNLPDG-SGLDLVKHVSQNYpNTPIAVLTA 85
Cdd:cd17534    3 ILIVEDEAIIALDLKEILESLGYEvVGIADSGEEAIELAEENKPDLILMDINLKGDmDGIEAAREIREKF-DIPVIFLTA 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 898527763  86 YGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKAL 121
Cdd:cd17534   82 YSDEETLERAKETNPYGYLVKPFNERELKAAIELAL 117
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
8-110 2.63e-08

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: 52.14  E-value: 2.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQfHYDACL--TDLNLPDGSGLDLVKHVSQNYPNTPIAV--L 83
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQ-HPDIKLviTDYNMPEMDGFELVREIRKKYSRDQLAIigI 81
                         90       100
                 ....*....|....*....|....*..
gi 898527763  84 TAYGNMDIAIAALKAGAFDFVSKPVNQ 110
Cdd:cd17544   82 SASGDNALSARFIKAGANDFLTKPFLP 108
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
8-108 3.90e-08

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: 51.61  E-value: 3.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYpNTPIAVLTAYG 87
Cdd:cd17622    3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKY-QGPILLLTALD 81
                         90       100
                 ....*....|....*....|.
gi 898527763  88 NMDIAIAALKAGAFDFVSKPV 108
Cdd:cd17622   82 SDIDHILGLELGADDYVVKPV 102
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
8-108 5.76e-08

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 50.57  E-value: 5.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNyPNT---PIAVLT 84
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKED-PETrhiPVIMIT 80
                         90       100
                 ....*....|....*....|....
gi 898527763  85 AYGNMDIAIAALKAGAFDFVSKPV 108
Cdd:cd17538   81 ALDDREDRIRGLEAGADDFLSKPI 104
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
8-107 5.78e-08

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: 50.45  E-value: 5.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQN--YPNTPIAVLTA 85
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNadFDTIPVIFLTA 80
                         90       100
                 ....*....|....*....|..
gi 898527763  86 YGNMDIAIAALKAGAFDFVSKP 107
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
8-109 7.34e-08

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: 50.55  E-value: 7.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNyPNTPIAVLTAYG 87
Cdd:cd17626    3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAE-SGVPIVMLTAKS 81
                         90       100
                 ....*....|....*....|..
gi 898527763  88 NMDIAIAALKAGAFDFVSKPVN 109
Cdd:cd17626   82 DTVDVVLGLESGADDYVAKPFK 103
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
8-108 8.56e-08

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: 50.20  E-value: 8.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNyPNT---PIAVLT 84
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKAD-PATrhiPVIFLT 79
                         90       100
                 ....*....|....*....|....
gi 898527763  85 AYGNMDIAIAALKAGAFDFVSKPV 108
Cdd:cd19920   80 ALTDTEDKVKGFELGAVDYITKPF 103
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
8-124 1.01e-07

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: 50.46  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 898527763  88 NMDIAIAALKAGAFDFVSKPVNqvhLDQLLQ--KALNRQ 124
Cdd:cd17627   81 SVSDRVAGLDAGADDYLVKPFA---LEELLArvRALLRR 116
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
8-121 1.40e-07

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: 49.93  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDeeDLCLLMQMT--LARMGIKTHLAYRVEQAKQLFTQF--HYDACLTDLNLPDGSGLDLVKHVsQNYPNTPIAVL 83
Cdd:cd17584    1 VLVVDD--DPTCLAILKrmLLRCGYQVTTCTDAEEALSMLRENkdEFDLVITDVHMPDMDGFEFLELI-RLEMDLPVIMM 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 898527763  84 TAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKAL 121
Cdd:cd17584   78 SADGSTSTVMKGLAHGACDYLLKPVSIEDLKNIWQHVV 115
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
6-135 1.96e-07

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: 50.06  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   6 PLVLLVDDEEDLCLLMQMTLaRMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTA 85
Cdd:cd17596    1 PTILVVDDEVRSLEALRRTL-EEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISG 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 898527763  86 YGNMDIAIAAL-KAGAFDFVSKPvnqVHLDQLLQKALNRQKVEHDAAENAL 135
Cdd:cd17596   80 YTDSEDIIAGInEAGIYQYLTKP---WHPDQLLLTVRNAARLFELQRENER 127
PRK10816 PRK10816
two-component system response regulator PhoP;
8-124 3.33e-07

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 50.89  E-value: 3.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARE 82
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 898527763  88 NMDIAIAALKAGAFDFVSKPvnqVHLDQLLQK--ALNRQ 124
Cdd:PRK10816  83 SWQDKVEVLSAGADDYVTKP---FHIEEVMARmqALMRR 118
PRK13557 PRK13557
histidine kinase; Provisional
8-113 6.58e-07

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 51.60  E-value: 6.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLF-TQFHYDACLTDLNLPDG-SGLDLVKHVSQNYPNTPIAVLTA 85
Cdd:PRK13557 418 ILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILdSHPEVDLLFTDLIMPGGmNGVMLAREARRRQPKIKVLLTTG 497
                         90       100
                 ....*....|....*....|....*...
gi 898527763  86 YGNMDIAIAALKAGAFDFVSKPVNQVHL 113
Cdd:PRK13557 498 YAEASIERTDAGGSEFDILNKPYRRAEL 525
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
8-123 8.76e-07

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 49.72  E-value: 8.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQN--YPNTPIAVLTA 85
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKREsmTRDIPVVMLTA 84
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 898527763  86 YGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNR 123
Cdd:PRK10161  85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRR 122
PRK13435 PRK13435
response regulator; Provisional
1-128 1.12e-06

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 48.12  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   1 MAEQQPLVLLVDDEEDLCLLMQMTLARMGIKT-HLAYRVEQAKQLFTQFHYDACLTDLNLPDG-SGLDLVKHVSQNYpnt 78
Cdd:PRK13435   1 MFLRQLKVLIVEDEALIALELEKLVEEAGHEVvGIAMSSEQAIALGRRRQPDVALVDVHLADGpTGVEVARRLSADG--- 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 898527763  79 PIAVLTAYGNMDIaIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKVEH 128
Cdd:PRK13435  78 GVEVVFMTGNPER-VPHDFAGALGVIAKPYSPRGVARALSYLSARRVGDR 126
PRK10336 PRK10336
two-component system response regulator QseB;
8-123 2.01e-06

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 48.74  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:PRK10336   3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTARD 82
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 898527763  88 NMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNR 123
Cdd:PRK10336  83 ALAERVEGLRLGADDYLCKPFALIEVAARLEALMRR 118
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
8-107 2.10e-06

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 46.04  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNyPNTPIAVLTAYG 87
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRAR-SNVPVIMVTAKD 79
                         90       100
                 ....*....|....*....|
gi 898527763  88 NMDIAIAALKAGAFDFVSKP 107
Cdd:cd17621   80 SEIDKVVGLELGADDYVTKP 99
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
8-123 3.31e-06

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: 45.87  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEedlcllmqmTLARMGIKTHL---AYRV-------EQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPn 77
Cdd:cd19932    3 VLIAEDE---------ALIRMDLREMLeeaGYEVvgeasdgEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENI- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 898527763  78 TPIAVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNR 123
Cdd:cd19932   73 APIVLLTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIAR 118
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
8-108 3.85e-06

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: 45.42  E-value: 3.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQ-FHYDACLTDLNLPDG-SGLDLVKHVSQNYPNTPIAVLTA 85
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESgPDIDLLVTDVIMPGGmNGSQLAEEARRRRPDLKVLLTSG 80
                         90       100
                 ....*....|....*....|...
gi 898527763  86 YGNMDIAIAALKAGaFDFVSKPV 108
Cdd:cd18161   81 YAENAIEGGDLAPG-VDVLSKPF 102
PRK15479 PRK15479
transcriptional regulator TctD;
8-123 3.95e-06

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 47.79  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:PRK15479   3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTARS 82
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 898527763  88 NMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNR 123
Cdd:PRK15479  83 AVADRVKGLNVGADDYLPKPFELEELDARLRALLRR 118
PRK10693 PRK10693
two-component system response regulator RssB;
33-108 4.14e-06

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 48.45  E-value: 4.14e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 898527763  33 HLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYGNM-DIAiAALKAGAFDFVSKPV 108
Cdd:PRK10693   1 VLAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMaDIA-KALRLGVQDVLLKPV 76
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
8-107 6.40e-06

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: 44.80  E-value: 6.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIK-THLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAY 86
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAvTEAESGAEALEKLQQGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISGG 81
                         90       100
                 ....*....|....*....|.
gi 898527763  87 GNMDIAIAALKAGAFDFVSKP 107
Cdd:cd18160   82 AAAAPELLSDAVGDNATLKKP 102
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
8-108 7.36e-06

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: 45.06  E-value: 7.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYpNTPIAVLTAYG 87
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHS-HVPILMLTART 80
                         90       100
                 ....*....|....*....|.
gi 898527763  88 NMDIAIAALKAGAFDFVSKPV 108
Cdd:cd19939   81 EEMDRVLGLEMGADDYLCKPF 101
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
140-197 7.63e-06

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 45.96  E-value: 7.63e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 898527763  140 LIGRSLPIQQLRIAIKKIARSQAP-VFVTGESGTGKEVVANLVHRLSNRSEGPFIAINC 197
Cdd:pfam13191   2 LVGREEELEQLLDALDRVRSGRPPsVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKC 60
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
163-281 8.20e-06

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 45.36  E-value: 8.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  163 PVFVTGESGTGK-EVVANLVHRLSNRsegPFIAINCGAIPTelmESELFG----------HKKGSFTGATQdkqglilsa 231
Cdd:pfam07728   1 GVLLVGPPGTGKtELAERLAAALSNR---PVFYVQLTRDTT---EEDLFGrrnidpggasWVDGPLVRAAR--------- 65
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 898527763  232 HGGSLFLDEIAELPLSMQVKLLRAVQEKKIRPVGSDQEIDV---DFRVISASH 281
Cdd:pfam07728  66 EGEIAVLDEINRANPDVLNSLLSLLDERRLLLPDGGELVKAapdGFRLIATMN 118
orf27 CHL00148
Ycf27; Reviewed
1-168 9.02e-06

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 47.02  E-value: 9.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   1 MAEQQPLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLP--DGSGldlVKHVSQNYPNT 78
Cdd:CHL00148   2 MENSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPklDGYG---VCQEIRKESDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  79 PIAVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRqkVEHDAAENALENKLLIGrslpIQQLRIAIKK-- 156
Cdd:CHL00148  79 PIIMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLRR--TNKKSFSSKIPNSSIIR----IGFLKIDLNKkq 152
                        170
                 ....*....|..
gi 898527763 157 IARSQAPVFVTG 168
Cdd:CHL00148 153 VYKNNERIRLTG 164
PRK10610 PRK10610
chemotaxis protein CheY;
1-123 9.86e-06

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 44.97  E-value: 9.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   1 MAEQQPLVLLVDDEEDLCLLMQMTLARMGIKThlayrVEQAKQLFTQFH------YDACLTDLNLPDGSGLDLVKHVSQN 74
Cdd:PRK10610   1 MADKELKFLVVDDFSTMRRIVRNLLKELGFNN-----VEEAEDGVDALNklqaggFGFVISDWNMPNMDGLELLKTIRAD 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 898527763  75 --YPNTPIAVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNR 123
Cdd:PRK10610  76 gaMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEK 126
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
8-113 1.15e-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: 44.45  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNyPNT---PIAVLT 84
Cdd:cd17548    2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKED-PATrdiPVIALT 80
                         90       100
                 ....*....|....*....|....*....
gi 898527763  85 AYGNMDIAIAALKAGAFDFVSKPVNQVHL 113
Cdd:cd17548   81 AYAMKGDREKILEAGCDGYISKPIDTREF 109
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
3-141 1.38e-05

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 46.22  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   3 EQQPLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQnYPNTPIAV 82
Cdd:PRK10710   8 ENTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRR-FSDIPIVM 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 898527763  83 LTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNRQKVEHDAAENALENKLLI 141
Cdd:PRK10710  87 VTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTILRRCKPQRELQQQDAESPLII 145
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
8-118 1.75e-05

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 44.33  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLaYRVEQAKQ----LFTQFHYDAC------LTDLNLPDGSGLDLVKHVSQNyPN 77
Cdd:cd17557    2 ILLVEDNPGDAELIQEAFKEAGVPNEL-HVVRDGEEaldfLRGEGEYADAprpdliLLDLNMPRMDGFEVLREIKAD-PD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 898527763  78 T---PIAVLTAYGN-MDIaIAALKAGAFDFVSKPVNqvhLDQLLQ 118
Cdd:cd17557   80 LrriPVVVLTTSDAeEDI-ERAYELGANSYIVKPVD---FEEFVE 120
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
8-123 1.76e-05

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: 44.07  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEedlcllmqmTLARmgikTHLAYRVEQ---------------AKQLFTQFHYDACLTDLNLPDGSGLDLVKHVS 72
Cdd:cd17532    1 ALIVDDE---------PLAR----EELRYLLEEhpdieivgeaengeeALEAIEELKPDVVFLDIQMPGLDGLELAKKLS 67
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 898527763  73 QnYPNTPIAV-LTAYGnmDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALNR 123
Cdd:cd17532   68 K-LAKPPLIVfVTAYD--EYAVEAFELNAVDYLLKPFSEERLAEALAKLRKR 116
PRK15369 PRK15369
two component system response regulator;
8-127 2.72e-05

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 45.07  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEdlcllmqmtLARMGIKTHLA----YR-VEQAK------QLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYP 76
Cdd:PRK15369   6 ILLVDDHE---------LIINGIKNMLApyprYKiVGQVDnglevyNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWP 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 898527763  77 NTPIAVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQK----------ALNRQKVE 127
Cdd:PRK15369  77 AMNILVLTARQEEHMASRTLAAGALGYVLKKSPQQILLAAIQTvavgkryidpALNREAIL 137
REC_1_GGDEF cd19921
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
8-106 2.74e-05

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: 43.32  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLC-LLMQMTLARMGIKTHLAYRVEQAKQLFTQFH-YDACLTDLNLPDGSGLDLVKHVSQNypNTPIAVLTA 85
Cdd:cd19921    2 VLIVEDSKTFSkVLKHLIAQELGLEVDVAETLAEAKALLEEGDdYFAALVDLNLPDAPNGEAVDLVLEK--GIPVIVLTG 79
                         90       100
                 ....*....|....*....|.
gi 898527763  86 YGNMDIAIAALKAGAFDFVSK 106
Cdd:cd19921   80 SFDEDKRETLLSKGVVDYVLK 100
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
3-107 3.98e-05

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 44.95  E-value: 3.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   3 EQQPLVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAV 82
Cdd:PRK11083   1 MQQPTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIF 80
                         90       100
                 ....*....|....*....|....*
gi 898527763  83 LTAYGNMDIAIAALKAGAFDFVSKP 107
Cdd:PRK11083  81 LTARSDEVDRLVGLEIGADDYVAKP 105
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
8-139 4.85e-05

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 45.88  E-value: 4.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763    8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:PRK09959  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 898527763   88 NMDIAIAALKAGAFDFVSKPVN----QVHLDQLLQKALNRQKVEH---DAAENALENKL 139
Cdd:PRK09959 1041 QANEREKGLSCGMNLCLFKPLTldvlKTHLSQLHQVAHIAPQYRHldiEALKNNTANDL 1099
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
8-107 5.48e-05

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 44.53  E-value: 5.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYG 87
Cdd:PRK09836   3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTALG 82
                         90       100
                 ....*....|....*....|
gi 898527763  88 NMDIAIAALKAGAFDFVSKP 107
Cdd:PRK09836  83 TIEHRVKGLELGADDYLVKP 102
PRK15347 PRK15347
two component system sensor kinase;
8-203 8.11e-05

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 45.40  E-value: 8.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLD---LVKHVSQNY-PNTPIAVL 83
Cdd:PRK15347 693 ILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLEttqLWRDDPNNLdPDCMIVAL 772
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  84 TAYGNMDIAIAALKAGAFDFVSKPVN--------------QVHLDQLLQKALNRQKVEHDAAENALENKLLIGRSLPIQQ 149
Cdd:PRK15347 773 TANAAPEEIHRCKKAGMNHYLTKPVTlaqlaralelaaeyQLLRGIELSPQDSSCSPLLDTDDMALNSKLYQSLLLLLAQ 852
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 898527763 150 LRIAIKKIAR-SQAPVFVTGESG-TGKEVVANLVHRLSNrsegpfiAINCGAIPTE 203
Cdd:PRK15347 853 IEQAVENQEVlSQLLHTLKGCAGqAGLTELQCAVIDLEN-------ALETGEILSL 901
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
38-126 1.50e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 43.99  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  38 VEQAKQLftqfHYDACLTDLNLPDGSGLDLVKHVSQNYPnTPIAV---LTAYGNmDIAIAALKAGAFDFVSKPVNQVHLD 114
Cdd:PRK00742  42 REKIKKL----NPDVITLDVEMPVMDGLDALEKIMRLRP-TPVVMvssLTERGA-EITLRALELGAVDFVTKPFLGISLG 115
                         90
                 ....*....|..
gi 898527763 115 QLLQKALNRQKV 126
Cdd:PRK00742 116 MDEYKEELAEKV 127
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
7-108 1.56e-04

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: 41.28  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   7 LVLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNyPNTPIAVLTAY 86
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRAR-SDVPIIIISGD 79
                         90       100
                 ....*....|....*....|...
gi 898527763  87 GNMDIA-IAALKAGAFDFVSKPV 108
Cdd:cd17594   80 RRDEIDrVVGLELGADDYLAKPF 102
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1-100 3.20e-04

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 41.94  E-value: 3.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   1 MAEQQPLVLLVDDEedlcllmqmTLARMGIKTHLA----YRV-------EQAKQLFTQFHYDACLTDLNLPDGSGLDLVK 69
Cdd:PRK10651   2 SNQEPATILLIDDH---------PMLRTGVKQLISmapdITVvgeasngEQGIELAESLDPDLILLDLNMPGMNGLETLD 72
                         90       100       110
                 ....*....|....*....|....*....|.
gi 898527763  70 HVSQNYPNTPIAVLTAYGNMDIAIAALKAGA 100
Cdd:PRK10651  73 KLREKSLSGRIVVFSVSNHEEDVVTALKRGA 103
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
8-122 3.24e-04

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: 40.23  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARM-GIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNyPNT---PIAVL 83
Cdd:cd17552    4 ILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQAN-PETqsiPVILL 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 898527763  84 TA---------YGNMDIAIAalkagafdfVSKPVNQVHLDQLLQKALN 122
Cdd:cd17552   83 TAkaqpsdrqrFASLGVAGV---------IAKPFDPLTLAEQIAKLLG 121
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
8-71 3.55e-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: 3.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 898527763   8 VLLVDDEEDLCLLMQMTLARM-GIK-THLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHV 71
Cdd:COG2197    4 VLIVDDHPLVREGLRALLEAEpDIEvVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
29-119 4.29e-04

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 39.83  E-value: 4.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  29 GIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAygnmDIAIAA----LKAGAFDFV 104
Cdd:cd17593   25 DVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVSG----DVQPEAkervLELGALAFL 100
                         90
                 ....*....|....*
gi 898527763 105 SKPVNQVHLDQLLQK 119
Cdd:cd17593  101 KKPFDPEKLAQLLEE 115
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
1-122 5.23e-04

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 39.56  E-value: 5.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   1 MAEQQP-----LVLLVDDEEDLCLLMQmtlarmgikthlAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNY 75
Cdd:cd19930    3 IAEDQEmvrgaLAALLELEDDLEVVAQ------------ASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREEL 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 898527763  76 PNTPIAVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQKALN 122
Cdd:cd19930   71 PDTKVLIVTTFGRPGYFRRALAAGVDGYVLKDRPIEELADAIRTVHA 117
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
8-106 5.24e-04

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


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 40.08  E-value: 5.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLA-RMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQN--YPNTPIAVLT 84
Cdd:cd17575    3 VLLVDDQAIIGEAVRRALAdEEDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANpaTRDIPIIVLS 82
                         90       100
                 ....*....|....*....|..
gi 898527763  85 AYGNMDIAIAALKAGAFDFVSK 106
Cdd:cd17575   83 TKEEPEVKSEAFALGANDYLVK 104
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
8-122 5.51e-04

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


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 39.73  E-value: 5.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRV-EQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAY 86
Cdd:cd17530    3 VLVLDDDPFQCMMAATILEDLGPGNVDEADDgREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMSGL 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 898527763  87 GNMDIAIAALKAGAFDF-----VSKPVNQVHLDQLLQKALN 122
Cdd:cd17530   83 DGGILESAETLAGANGLnllgtLSKPFSPEELTELLTKYTA 123
PRK10766 PRK10766
two-component system response regulator TorR;
8-133 5.83e-04

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 41.18  E-value: 5.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEedlcllmQMTLARM-GIKTHLAYRV------EQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVsQNYPNTPI 80
Cdd:PRK10766   5 ILVVEDE-------PVTRARLqGYFEQEGYTVseaasgAGMREIMQNQHVDLILLDINLPGEDGLMLTREL-RSRSTVGI 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 898527763  81 AVLTAYGNMDIAIAALKAGAFDFVSKPVN----QVHLDQLLQK-ALNRQKVEHDAAEN 133
Cdd:PRK10766  77 ILVTGRTDSIDRIVGLEMGADDYVTKPLElrelLVRVKNLLWRiSLARQAQPHAQEED 134
PRK09483 PRK09483
response regulator; Provisional
8-106 8.16e-04

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 40.86  E-value: 8.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEdlcllmqmtLARMGIKTHL-----------AYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYP 76
Cdd:PRK09483   4 VLLVDDHE---------LVRAGIRRILedikgikvvgeACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTP 74
                         90       100       110
                 ....*....|....*....|....*....|
gi 898527763  77 NTPIAVLTAYGNMDIAIAALKAGAFDFVSK 106
Cdd:PRK09483  75 DVKIIMLTVHTENPLPAKVMQAGAAGYLSK 104
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
3-135 8.20e-04

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 41.85  E-value: 8.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   3 EQQPL----VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNYPN- 77
Cdd:PRK11091 519 DDMPLpalnILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPRe 598
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 898527763  78 --TPIAVLTA--------YgnmdiaiaaLKAGAFDFVSKPVNQVHLDQLLQK--------ALNRQKVEHDAAENAL 135
Cdd:PRK11091 599 dlPPLVALTAnvlkdkkeY---------LDAGMDDVLSKPLSVPALTAMIKKfwdtqddeESTVTTEESSKANEAL 665
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
8-113 1.10e-03

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 38.85  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQN--YPNTPIAVLTA 85
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDpdLKDIPVILLTT 80
                         90       100
                 ....*....|....*....|....*...
gi 898527763  86 YGNMDIAIAALKAGAFDFVSKPVNQVHL 113
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITKPYDEKYL 108
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
1-138 2.46e-03

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 40.60  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   1 MAEQQPL-VLLVDDEE-DLCLlmqmtlarmgIKTHLAYRVE---------QAKQLFTQFHYDACLTDLNLP--DG-SGLD 66
Cdd:PRK11107 662 DESRLPLtVMAVDDNPaNLKL----------IGALLEEQVEhvvlcdsghQAVEQAKQRPFDLILMDIQMPgmDGiRACE 731
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 898527763  67 LVKHVSQNYpNTPIAVLTAYgnmdiAIAA-----LKAGAFDFVSKPVNQVHLDQLLQKALNRQKVEHDAAENALENK 138
Cdd:PRK11107 732 LIRQLPHNQ-NTPIIAVTAH-----AMAGererlLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFTSRVVAPEPPEP 802
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
54-119 4.13e-03

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 37.32  E-value: 4.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 898527763  54 LTDLNLPDGSGLDLVKHVSQNYPNTPIAVLTAYGNMDIAIAAlkagafdfvskpVNQVHLDQLLQK 119
Cdd:cd17595   57 LVDQRMPEMDGVEFLEKAMELFPEAKRVLLTAYADTDAAIRA------------INDVQLDYYLLK 110
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
8-107 6.64e-03

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 36.27  E-value: 6.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763   8 VLLVDDEEDLCLLMQMTLARMGIKTHLAYRVEQAKQLFTQFHYDACLTDLNLPDGSGLDLVKHVSQNyPNTPIAVLTAYG 87
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQK-STLPVIFLTSKD 79
                         90       100
                 ....*....|....*....|
gi 898527763  88 NMDIAIAALKAGAFDFVSKP 107
Cdd:cd19936   80 DEIDEVFGLRMGADDYITKP 99
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
147-244 8.10e-03

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 38.29  E-value: 8.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763 147 IQQLRIAIKKIARSQAP--VFVTGESGTGKEVVANLV-HRLSNRSEGP-----FIAINCGAIPTE------LMESELFGH 212
Cdd:COG1474   35 IEELASALRPALRGERPsnVLIYGPTGTGKTAVAKYVlEELEEEAEERgvdvrVVYVNCRQASTRyrvlsrILEELGSGE 114
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 898527763 213 KKgSFTG-ATQDKQGLI---LSAHGGSLF--LDEIAEL 244
Cdd:COG1474  115 DI-PSTGlSTDELFDRLyeaLDERDGVLVvvLDEIDYL 151
PRK14084 PRK14084
DNA-binding response regulator;
50-148 8.35e-03

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 37.81  E-value: 8.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 898527763  50 YDACLTDLNLPDGSGLDLVKHVsqNYPNTPIAVLTAYGNMDIAIAALKAGAFDFVSKPVNQVHLDQLLQK-ALNRQKVEH 128
Cdd:PRK14084  47 YDIIFLDINLMDESGIELAAKI--QKMKEPPAIIFATAHDQFAVKAFELNATDYILKPFEQKRIEQAVNKvRATKAKDDN 124
                         90       100
                 ....*....|....*....|
gi 898527763 129 DAAENALENKLLIGRSLPIQ 148
Cdd:PRK14084 125 NASAIANDMSANFDQSLPIE 144
 
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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