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Conserved domains on  [gi|501080907|ref|WP_012131530|]
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MULTISPECIES: acetoacetate metabolism transcriptional regulator AtoC [Citrobacter]

Protein Classification

sigma-54-dependent Fis family transcriptional regulator( domain architecture ID 11485325)

sigma-54-dependent Fis family transcriptional regulator containing a REC domain, similar to Escherichia coli transcriptional regulators AtoC and NR(I), which function in the regulation of genes involved in acetoacetate metabolism and nitrogen assimilation, respectively

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1-457 0e+00

acetoacetate metabolism transcriptional regulator AtoC;


:

Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 934.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   1 MKTRYRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPII 80
Cdd:PRK11361   1 MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  81 LMTAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQAMKQEIRSLHQALSTSWQWGHILTNSPGMMDICKDTA 160
Cdd:PRK11361  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 161 KIALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGT 240
Cdd:PRK11361 161 KIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERR 320
Cdd:PRK11361 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 321 EDIPLLANHFLQKFSSENQRDIIEIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIFAEDLPTQFRQSVSHASGI 400
Cdd:PRK11361 321 EDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEV 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501080907 401 KPAQPGERNLKEEIKREERRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Cdd:PRK11361 401 KTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
 
Name Accession Description Interval E-value
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1-457 0e+00

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 934.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   1 MKTRYRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPII 80
Cdd:PRK11361   1 MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  81 LMTAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQAMKQEIRSLHQALSTSWQWGHILTNSPGMMDICKDTA 160
Cdd:PRK11361  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 161 KIALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGT 240
Cdd:PRK11361 161 KIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERR 320
Cdd:PRK11361 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 321 EDIPLLANHFLQKFSSENQRDIIEIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIFAEDLPTQFRQSVSHASGI 400
Cdd:PRK11361 321 EDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEV 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501080907 401 KPAQPGERNLKEEIKREERRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Cdd:PRK11361 401 KTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
3-455 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: 608.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   3 TRYRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILM 82
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  83 TAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQAMKQEIRSLHQalstswqwghILTNSPGMMDICKDTAKI 162
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSG----------LIGRSPAMQEVRRLIEKV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 163 ALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGTLL 242
Cdd:COG2204  151 APSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLF 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 243 LDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERRED 322
Cdd:COG2204  231 LDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERRED 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 323 IPLLANHFLQKFSSENQRDIIeIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIFAEDLPtqfrqsvshasgikp 402
Cdd:COG2204  311 IPLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLP--------------- 374
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501080907 403 aqpgernlkEEIKREERRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYG 455
Cdd:COG2204  375 ---------EALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
7-453 1.66e-157

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: 454.20  E-value: 1.66e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907    7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   87 EVETAVEALRSGAFDYVIKPFDLDELNLLIQRALqlqAMKQEIRSLHQALSTSWQWGHILTNSPGMMDICKDTAKIALSQ 166
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERAL---AHAQEQVALPADAGEAEDSAELIGEAPAMQEVFRAIGRLSRSD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  167 ANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGTLLLDEI 246
Cdd:TIGR01818 158 ITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  247 GEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERREDIPLL 326
Cdd:TIGR01818 238 GDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  327 ANHFLQKFSSENQRDIIEIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIFAEDLPTQFRQSVSHASGIKPAQP- 405
Cdd:TIGR01818 318 ARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELALTGRPASAPDSDGQd 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501080907  406 ----------------GERNLKEEIKREERRIIMEV-LEQQEGNRTRTALMLGISRRALMYKLQE 453
Cdd:TIGR01818 398 swdealeawakqalsrGEQGLLDRALPEFERPLLEAaLQHTRGHKQEAAALLGWGRNTLTRKLKE 462
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
1-457 3.55e-116

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 350.71  E-value: 3.55e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   1 MKTRYRILIVDDED-NVRRM-LATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNgieALKVMRAQHPRVP 78
Cdd:NF038308  24 QKWRPTVALCQQPDlPVDRLeLLHDRRDRALAERVAADIEEVSPETEVRLVPVVLRDPWDFEEV---YGALLDFARAYPF 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  79 IILMTAYAE------------VETAVEALRSGAfDYVIKPFDLDELN---LLIQRALQLQAMKQEIRSLHQALSTSWQWG 143
Cdd:NF038308 101 DTENEDYLVhittgthvaqicWFLLVEARYLPA-RLLQTSPPRDKEEgtyEIIDLDLSRYDALAQRFAREQAEAVSFLKS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 144 HILTNSPGMMDICKDTAKIAL-SQANVLISGESGTGKELIARAIHYNSRRAN---GPFIKINCAALPESLLESELFGHEK 219
Cdd:NF038308 180 GIATRNAAFNRLIEQIERVALrSRAPILLTGPTGAGKSFLARRIYELKKRRHqvsGPFVEVNCATLRGDLAMSELFGHVK 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 220 GAFTGAQTRRQGLFERAHQGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFR 299
Cdd:NF038308 260 GAFTGAQADRAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFR 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 300 EDLFYRLNVIHLTLPPLRERREDIPLLANHFLQKFSSENQRDI-----IEIDPSAMSLLTAWPWPGNIRELSNVIERAVV 374
Cdd:NF038308 340 EDLYARINLWTFRLPGLRERREDIEPNLDYELDRFARELGRQVrfnkeARFRYLAFATSPEALWPGNFRELSASVTRMAT 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 375 MNTGAVIFAEDLPT-------QFRQSVSHASGIKPAQPGERNLKEEI---KREERRIIMEVLEQQEGNRTRTALMLGISR 444
Cdd:NF038308 420 LADGGRITEELVEEeiarlraAWQSAPAAADDDALADLLGGEQLAELdlfDRVQLAAVLRVCRQSRSLSAAGRRLFGVSR 499
                        490
                 ....*....|....*...
gi 501080907 445 RAL-----MYKLQEYGID 457
Cdd:NF038308 500 QQKaspndADRLRKYLAR 517
Sigma54_activat pfam00158
Sigma-54 interaction domain;
145-312 1.19e-113

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 331.29  E-value: 1.19e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  145 ILTNSPGMMDICKDTAKIALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTG 224
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  225 AQTRRQGLFERAHQGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFY 304
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 501080907  305 RLNVIHLT 312
Cdd:pfam00158 161 RLNVIPIE 168
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
6-120 1.76e-37

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: 132.78  E-value: 1.76e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAY 85
Cdd:cd19919    2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAH 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDELNLLIQRAL 120
Cdd:cd19919   82 SDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
resp_reg_YycF NF040534
response regulator YycF;
6-128 7.64e-16

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 76.68  E-value: 7.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHpRVPIILMTAY 85
Cdd:NF040534   2 KILVVDDEKPIADILEFNLKKEGYEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKKY-DMPIIMLTAK 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDEL------NLliqRALQLQAMKQE 128
Cdd:NF040534  81 DSEIDKVLGLELGADDYVTKPFSTRELiarvkaNL---RRHQQQNTEEE 126
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
5-59 8.28e-15

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: 68.36  E-value: 8.28e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 501080907     5 YRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMP 59
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1-457 0e+00

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 934.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   1 MKTRYRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPII 80
Cdd:PRK11361   1 MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  81 LMTAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQAMKQEIRSLHQALSTSWQWGHILTNSPGMMDICKDTA 160
Cdd:PRK11361  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQWGHILTNSPAMMDICKDTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 161 KIALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGT 240
Cdd:PRK11361 161 KIALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERR 320
Cdd:PRK11361 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 321 EDIPLLANHFLQKFSSENQRDIIEIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIFAEDLPTQFRQSVSHASGI 400
Cdd:PRK11361 321 EDISLLANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVCNAGEV 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501080907 401 KPAQPGERNLKEEIKREERRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Cdd:PRK11361 401 KTAPVGERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
3-455 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: 608.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   3 TRYRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILM 82
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  83 TAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQAMKQEIRSLHQalstswqwghILTNSPGMMDICKDTAKI 162
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSG----------LIGRSPAMQEVRRLIEKV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 163 ALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGTLL 242
Cdd:COG2204  151 APSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLF 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 243 LDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERRED 322
Cdd:COG2204  231 LDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERRED 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 323 IPLLANHFLQKFSSENQRDIIeIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIFAEDLPtqfrqsvshasgikp 402
Cdd:COG2204  311 IPLLARHFLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLP--------------- 374
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501080907 403 aqpgernlkEEIKREERRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYG 455
Cdd:COG2204  375 ---------EALEEVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
108-457 0e+00

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: 519.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 108 DLDELNLLIQRAlqlqaMKQEIRSLHQALSTSwqwGHILTNSPGMMDIcKDTA-KIALSQANVLISGESGTGKELIARAI 186
Cdd:COG3829  111 DITELKRLERKL-----REEELERGLSAKYTF---DDIIGKSPAMKEL-LELAkRVAKSDSTVLILGESGTGKELFARAI 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 187 HYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGA-QTRRQGLFERAHQGTLLLDEIGEMPLVLQAKLLRILQERE 265
Cdd:COG3829  182 HNASPRRDGPFVAVNCAAIPENLLESELFGYEKGAFTGAkKGGKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKE 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 266 FERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERREDIPLLANHFLQKFSSENQRDIIEI 345
Cdd:COG3829  262 VRRVGGTKPIPVDVRIIAATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFNKKYGKNIKGI 341
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 346 DPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIFAEDLPTQFRQSVSHASgikpaQPGERNLKEEIKREERRIIMEV 425
Cdd:COG3829  342 SPEALELLLAYDWPGNVRELENVIERAVVLSEGDVITPEHLPEYLLEEAEAAS-----AAEEGSLKEALEEVEKELIEEA 416
                        330       340       350
                 ....*....|....*....|....*....|..
gi 501080907 426 LEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Cdd:COG3829  417 LEKTGGNKSKAAKALGISRSTLYRKLKKYGIK 448
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
7-453 1.66e-157

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: 454.20  E-value: 1.66e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907    7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:TIGR01818   1 VWVVDDDRSIRWVLEKALSRAGYEVRTFGNAASVLRALARGQPDLLITDVRMPGEDGLDLLPQIKKRHPQLPVIVMTAHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   87 EVETAVEALRSGAFDYVIKPFDLDELNLLIQRALqlqAMKQEIRSLHQALSTSWQWGHILTNSPGMMDICKDTAKIALSQ 166
Cdd:TIGR01818  81 DLDTAVAAYQRGAFEYLPKPFDLDEAVTLVERAL---AHAQEQVALPADAGEAEDSAELIGEAPAMQEVFRAIGRLSRSD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  167 ANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGTLLLDEI 246
Cdd:TIGR01818 158 ITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTLFLDEI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  247 GEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERREDIPLL 326
Cdd:TIGR01818 238 GDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERREDIPRL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  327 ANHFLQKFSSENQRDIIEIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIFAEDLPTQFRQSVSHASGIKPAQP- 405
Cdd:TIGR01818 318 ARHFLALAARELDVEPKLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPAELALTGRPASAPDSDGQd 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501080907  406 ----------------GERNLKEEIKREERRIIMEV-LEQQEGNRTRTALMLGISRRALMYKLQE 453
Cdd:TIGR01818 398 swdealeawakqalsrGEQGLLDRALPEFERPLLEAaLQHTRGHKQEAAALLGWGRNTLTRKLKE 462
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
7-451 1.07e-152

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 441.01  E-value: 1.07e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDELNLLIQRALqlqAMKQEIRSLHQALSTSwQWGHIlTNSPGMMDICKDTAKIALSQ 166
Cdd:PRK10365  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKAL---AHTHSIDAETPAVTAS-QFGMV-GKSPAMQHLLSEIALVAPSE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 167 ANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGTLLLDEI 246
Cdd:PRK10365 163 ATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEI 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 247 GEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERREDIPLL 326
Cdd:PRK10365 243 GDISPMMQVRLLRAIQEREVQRVGSNQTISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLL 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 327 ANHFLQKFSSENQRDIIEIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIFAEDLPTQFRQSVSHASGIKPAQPg 406
Cdd:PRK10365 323 AGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAVVLLTGEYISERELPLAIASTPIPLGQSQDIQP- 401
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 501080907 407 ernlkeeIKREERRIIMEVLEQQEGNRTRTALMLGISRRALMYKL 451
Cdd:PRK10365 402 -------LVEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKL 439
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
7-456 3.63e-147

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: 427.24  E-value: 3.63e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907    7 ILIVDDEDNVRRMLAtaFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMP-----EMNGIEALKVMRAQHPRVPIIL 81
Cdd:TIGR02915   1 LLIVEDDLGLQKQLK--WSFADYELAVAADRESAIALVRRHEPAVVTLDLGLPpdadgASEGLAALQQILAIAPDTKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   82 MTAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQAMKQEIRSLHQALSTSWQWGhILTNSPGMMDICKDTAK 161
Cdd:TIGR02915  79 ITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSALGGTALRG-LITSSPGMQKICRTIEK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  162 IALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGTL 241
Cdd:TIGR02915 158 IAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  242 LLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERRE 321
Cdd:TIGR02915 238 FLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  322 DIPLLANHFLQKFSSENQRDIIEIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIFAEDLPTQFRQSvshasgik 401
Cdd:TIGR02915 318 DAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAEDLGLDARER-------- 389
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 501080907  402 PAQPGERNLKEEIKREERRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
Cdd:TIGR02915 390 AETPLEVNLREVRERAEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGI 444
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
4-457 3.29e-138

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 405.41  E-value: 3.29e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   4 RYRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMT 83
Cdd:PRK10923   3 RGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  84 AYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQAMKQEIRSLHQALSTSwqwgHILTNSPGMMDICKDTAKIA 163
Cdd:PRK10923  83 AHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNIQVNGPTT----DIIGEAPAMQDVFRIIGRLS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 164 LSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGTLLL 243
Cdd:PRK10923 159 RSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 244 DEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERREDI 323
Cdd:PRK10923 239 DEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDI 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 324 PLLANHFLQKFSSENQRDIIEIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIFAEDLPTQFRQSVSHASGIKPA 403
Cdd:PRK10923 319 PRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESTVPESTSQMQ 398
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501080907 404 ----------------QPGERNLKEEIKRE-ERRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Cdd:PRK10923 399 pdswatllaqwadralRSGHQNLLSEAQPElERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 469
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
89-455 7.17e-130

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 389.26  E-value: 7.17e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  89 ETAVEALRSGAFDYVIKPFDL-DELNLLIQRALQLQAMKQEIRSLHQALSTSWQWGHILTNSPGMMDICKDTAKIALSQA 167
Cdd:COG3284  266 GLDLEALPDGARRAPASPRPLrLRDGRRLGALLRLRPARRAARAAPAGAPAPAALAALAGGDPAMRRALRRARRLADRDI 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 168 NVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQTR-RQGLFERAHQGTLLLDEI 246
Cdd:COG3284  346 PVLILGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESELFGYEPGAFTGARRKgRPGKIEQADGGTLFLDEI 425
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 247 GEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRErREDIPLL 326
Cdd:COG3284  426 GDMPLALQARLLRVLQEREVTPLGGTKPIPVDVRLIAATHRDLRELVAAGRFREDLYYRLNGLTLTLPPLRE-REDLPAL 504
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 327 ANHFLQKFSSEnqRDIIEIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIFAEDLPTQFRQSVShasgikPAQPG 406
Cdd:COG3284  505 IEHLLRELAAG--RGPLRLSPEALALLAAYPWPGNVRELRNVLRTALALADGGVITVEDLPDELRAELA------AAAPA 576
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 501080907 407 ERNLKEEIKREERRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYG 455
Cdd:COG3284  577 AAAPLTSLEEAERDAILRALRACGGNVSAAARALGISRSTLYRKLKRYG 625
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
145-457 1.76e-125

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: 374.82  E-value: 1.76e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  145 ILTNSPGMMDICKDTAKIALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTG 224
Cdd:TIGR01817 198 IIGKSPAMRQVVDQARVVARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVNCAALSETLLESELFGHEKGAFTG 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  225 AQTRRQGLFERAHQGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFY 304
Cdd:TIGR01817 278 AIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRLVAATNRDLEEAVAKGEFRADLYY 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  305 RLNVIHLTLPPLRERREDIPLLANHFLQKFSSENQRDiIEIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIFAE 384
Cdd:TIGR01817 358 RINVVPIFLPPLRERREDIPLLAEAFLEKFNRENGRP-LTITPSAIRVLMSCKWPGNVRELENCLERTATLSRSGTITRS 436
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  385 DLPTQFRQSVS---HASGikPAQPGERNLKEEIKR--------------------EERRIIMEVLEQQEGNRTRTALMLG 441
Cdd:TIGR01817 437 DFSCQSGQCLSpmlAKTC--PHGHISIDPLAGTTPphspasaalpgepglsgptlSERERLIAALEQAGWVQAKAARLLG 514
                         330
                  ....*....|....*.
gi 501080907  442 ISRRALMYKLQEYGID 457
Cdd:TIGR01817 515 MTPRQVGYALRKLNIE 530
PRK15115 PRK15115
response regulator GlrR; Provisional
6-459 1.37e-121

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 361.85  E-value: 1.37e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAY 85
Cdd:PRK15115   7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQAmkqeirslhQALSTSWQwGHILTNSPGMMDICKDTAKIALS 165
Cdd:PRK15115  87 GSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSA---------PATDERWR-EAIVTRSPLMLRLLEQARMVAQS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 166 QANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGTLLLDE 245
Cdd:PRK15115 157 DVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 246 IGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERREDIPL 325
Cdd:PRK15115 237 IGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPL 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 326 LANHFLQKFSSENQRDIIEIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIfAEDLPTQfrqsvsHASGIKPAQP 405
Cdd:PRK15115 317 LANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVI-SDALVEQ------ALEGENTALP 389
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501080907 406 gerNLKEEIKREERRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGIDPA 459
Cdd:PRK15115 390 ---TFVEARNQFELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELDAN 440
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
94-444 3.60e-120

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 360.26  E-value: 3.60e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  94 ALRSGAFDyvikPFDLDEL------------NLLIQRALQLQAMKQeiRSLHQAL-STSWQWGHILTNSPGMMDICKDTA 160
Cdd:PRK05022 131 ALDPGQFD----AFSDEELralaalaaatlrNALLIEQLESQAELP--QDVAEFLrQEALKEGEMIGQSPAMQQLKKEIE 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 161 KIALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGT 240
Cdd:PRK05022 205 VVAASDLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAESELFGHVKGAFTGAISNRSGKFELADGGT 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERR 320
Cdd:PRK05022 285 LFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRERG 364
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 321 EDIPLLANHFLQkfssENQRDI----IEIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGA------VIFAEDLPTQF 390
Cdd:PRK05022 365 DDVLLLAGYFLE----QNRARLglrsLRLSPAAQAALLAYDWPGNVRELEHVISRAALLARARgagrivTLEAQHLDLPA 440
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 501080907 391 RQSV-SHASGIKPAQPGERNLKEEIKREERRIIMEVLEQQEGNRTRTALMLGISR 444
Cdd:PRK05022 441 EVALpPPEAAAAPAAVVSQNLREATEAFQRQLIRQALAQHQGNWAAAARALELDR 495
RNA_repair_RtcR NF038308
RNA repair transcriptional activator RtcR;
1-457 3.55e-116

RNA repair transcriptional activator RtcR;


Pssm-ID: 468466 [Multi-domain]  Cd Length: 527  Bit Score: 350.71  E-value: 3.55e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   1 MKTRYRILIVDDED-NVRRM-LATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNgieALKVMRAQHPRVP 78
Cdd:NF038308  24 QKWRPTVALCQQPDlPVDRLeLLHDRRDRALAERVAADIEEVSPETEVRLVPVVLRDPWDFEEV---YGALLDFARAYPF 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  79 IILMTAYAE------------VETAVEALRSGAfDYVIKPFDLDELN---LLIQRALQLQAMKQEIRSLHQALSTSWQWG 143
Cdd:NF038308 101 DTENEDYLVhittgthvaqicWFLLVEARYLPA-RLLQTSPPRDKEEgtyEIIDLDLSRYDALAQRFAREQAEAVSFLKS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 144 HILTNSPGMMDICKDTAKIAL-SQANVLISGESGTGKELIARAIHYNSRRAN---GPFIKINCAALPESLLESELFGHEK 219
Cdd:NF038308 180 GIATRNAAFNRLIEQIERVALrSRAPILLTGPTGAGKSFLARRIYELKKRRHqvsGPFVEVNCATLRGDLAMSELFGHVK 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 220 GAFTGAQTRRQGLFERAHQGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFR 299
Cdd:NF038308 260 GAFTGAQADRAGLLRAADGGTLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFR 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 300 EDLFYRLNVIHLTLPPLRERREDIPLLANHFLQKFSSENQRDI-----IEIDPSAMSLLTAWPWPGNIRELSNVIERAVV 374
Cdd:NF038308 340 EDLYARINLWTFRLPGLRERREDIEPNLDYELDRFARELGRQVrfnkeARFRYLAFATSPEALWPGNFRELSASVTRMAT 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 375 MNTGAVIFAEDLPT-------QFRQSVSHASGIKPAQPGERNLKEEI---KREERRIIMEVLEQQEGNRTRTALMLGISR 444
Cdd:NF038308 420 LADGGRITEELVEEeiarlraAWQSAPAAADDDALADLLGGEQLAELdlfDRVQLAAVLRVCRQSRSLSAAGRRLFGVSR 499
                        490
                 ....*....|....*...
gi 501080907 445 RAL-----MYKLQEYGID 457
Cdd:NF038308 500 QQKaspndADRLRKYLAR 517
Sigma54_activat pfam00158
Sigma-54 interaction domain;
145-312 1.19e-113

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 331.29  E-value: 1.19e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  145 ILTNSPGMMDICKDTAKIALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTG 224
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  225 AQTRRQGLFERAHQGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFY 304
Cdd:pfam00158  81 ADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYY 160

                  ....*...
gi 501080907  305 RLNVIHLT 312
Cdd:pfam00158 161 RLNVIPIE 168
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
125-456 2.81e-112

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 340.24  E-value: 2.81e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 125 MKQEIRSLHQALSTSWqwGHILTNSPGMMDICKDTAKIALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAA 204
Cdd:COG3283  188 LGEQLQALQVNDDSGF--DHIVASSPKMRQVIRQAKKMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLALNCAA 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 205 LPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAA 284
Cdd:COG3283  266 LPDDVAESELFGYAPGAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVDVRVICA 345
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 285 TNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERREDIPLLANHFLQKFSSENQRDIIEIDPSAMSLLTAWPWPGNIRE 364
Cdd:COG3283  346 TQKDLAELVQEGEFREDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQ 425
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 365 LSNVIERAVVMNTGAVIFAEDLptQFRQSVSHASGIKPAQPGerNLKEEIKREERriimEVLEQ--QEGNRTRT-ALMLG 441
Cdd:COG3283  426 LENALYRAVSLLEGDELTPEDL--QLPEYAASAGLLDDLLEG--SLDEIVKRFER----SLLRRlyPSYPSTRKlAKRLG 497
                        330
                 ....*....|....*
gi 501080907 442 ISRRALMYKLQEYGI 456
Cdd:COG3283  498 VSHTAIANKLREYGI 512
phageshock_pspF TIGR02974
psp operon transcriptional activator PspF; Members of this protein family are PspF, the ...
169-450 6.76e-104

psp operon transcriptional activator PspF; Members of this protein family are PspF, the sigma-54-dependent transcriptional activator of the phage shock protein (psp) operon, in Escherichia coli and numerous other species. The psp operon is induced by a number of stress conditions, including heat shock, ethanol, and filamentous phage infection. Changed com_name to adhere to TIGR role notes conventions. 09/15/06 - DMH [Regulatory functions, DNA interactions]


Pssm-ID: 274371 [Multi-domain]  Cd Length: 329  Bit Score: 312.31  E-value: 6.76e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  169 VLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGTLLLDEIGE 248
Cdd:TIGR02974  25 VLIIGERGTGKELIAARLHYLSKRWQGPLVKLNCAALSENLLDSELFGHEAGAFTGAQKRHQGRFERADGGTLFLDELAT 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  249 MPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERREDIPLLAN 328
Cdd:TIGR02974 105 ASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCATNADLPALAAEGRFRADLLDRLAFDVITLPPLRERQEDIMLLAE 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  329 HFLQKFSSENQRDII-EIDPSAMSLLTAWPWPGNIRELSNVIERAVV-MNTGAVIF-------------------AEDLP 387
Cdd:TIGR02974 185 HFAIRMARELGLPLFpGFTPQAREQLLEYHWPGNVRELKNVVERSVYrHGLEEAPIdeiiidpfaspwrpkqaapAVDEV 264
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501080907  388 TQFRQSVSHASGIKPAQPgeRNLKEEIKREERRIIMEVLEQQEGNRTRTALMLGISR---RALMYK 450
Cdd:TIGR02974 265 NSTPTDLPSPSSIAAAFP--LDLKQAQQDYEIELLQQALAEAQFNQRKAAELLGLTYhqlRGLLRK 328
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
114-458 1.33e-97

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 303.56  E-value: 1.33e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 114 LLIQRALQLQAMKQEIRslhQALSTSWQWGHILTNSPGMMDICKDTAKIALSQANVLISGESGTGKELIARAIH------ 187
Cdd:PRK15424 193 LDMTRMTLRHNTHYATR---NALRTRYVLGDLLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHreyfar 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 188 --YNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQtR--RQGLFERAHQGTLLLDEIGEMPLVLQAKLLRILQE 263
Cdd:PRK15424 270 hdARQGKKSHPFVAVNCGAIAESLLEAELFGYEEGAFTGSR-RggRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEE 348
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 264 REFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERREDIPLLANHFLQK--------FS 335
Cdd:PRK15424 349 KEVTRVGGHQPVPVDVRVISATHCDLEEDVRQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQslaalsapFS 428
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 336 SENQRDIIEidpsAMSLLTAWPWPGNIRELSNVIERAVVMntgavIFAEDLPT---QFRQSVSHASGIKPAQPGErnlke 412
Cdd:PRK15424 429 AALRQGLQQ----CETLLLHYDWPGNVRELRNLMERLALF-----LSVEPTPDltpQFLQLLLPELARESAKTPA----- 494
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 501080907 413 eiKREERRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGIDP 458
Cdd:PRK15424 495 --PRLLAATLQQALERFNGDKTAAANYLGISRTTLWRRLKAEAKAQ 538
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
165-457 1.39e-97

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: 296.76  E-value: 1.39e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 165 SQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESelfghekgaftgaqtrrqglferahqgtllld 244
Cdd:COG3604  114 SLAAVAILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES-------------------------------- 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 245 eigemplvlqakllriLQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERREDIP 324
Cdd:COG3604  162 ----------------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDIP 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 325 LLANHFLQKFSSENQRDIIEIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIFAEDLPTQFRqsvshasgikpaq 404
Cdd:COG3604  226 LLAEHFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDLAPGSR------------- 292
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501080907 405 pgernlkEEIKREERRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Cdd:COG3604  293 -------EALEEVEREHILEALERTGGNIAGAARLLGLTPSTLRSRMKKLGIK 338
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
141-457 7.45e-97

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 305.60  E-value: 7.45e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 141 QWGHILTNSPGMMDICKDTAKIALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKG 220
Cdd:PRK15429 374 EFGEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHERG 453
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 221 AFTGAQTRRQGLFERAHQGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFRE 300
Cdd:PRK15429 454 AFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREFRS 533
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 301 DLFYRLNVIHLTLPPLRERREDIPLLANHFLQKFSSENQRDIIEIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAV 380
Cdd:PRK15429 534 DLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNVRELENVIERAVLLTRGNV 613
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 381 IFAEdLPtqfrqSVSHASGIKPAQPGERNLKEEikrEERRIIMEVLEQQEG---NRTRTALMLGISRRALMYKLQEYGID 457
Cdd:PRK15429 614 LQLS-LP-----DITLPEPETPPAATVVAQEGE---DEYQLIVRVLKETNGvvaGPKGAAQRLGLKRTTLLSRMKRLGID 684
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
135-452 2.20e-91

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: 287.14  E-value: 2.20e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  135 ALSTSWQWGHILTNSPGMMDICKDTAKIALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESEL 214
Cdd:TIGR02329 204 QLRTRYRLDDLLGASAPMEQVRALVRLYARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEAEL 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  215 FGHEKGAFTGAQTR-RQGLFERAHQGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMV 293
Cdd:TIGR02329 284 FGYEEGAFTGARRGgRTGLIEAAHRGTLFLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAV 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  294 KEGTFREDLFYRLNVIHLTLPPLRERREDIPLLANHFLQKFSSENQrdiIEIDPSAM-------SLLTAWPWPGNIRELS 366
Cdd:TIGR02329 364 QQGRFRRDLFYRLSILRIALPPLRERPGDILPLAAEYLVQAAAALR---LPDSEAAAqvlagvaDPLQRYPWPGNVRELR 440
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  367 NVIERAVV----MNTGAVIFAED---LPTQFRQSVShaSGIKPAQPGERNLKEEIkreerrIIMEVLEQQEGNRTRTALM 439
Cdd:TIGR02329 441 NLVERLALelsaMPAGALTPDVLralAPELAEASGK--GKTSALSLRERSRVEAL------AVRAALERFGGDRDAAAKA 512
                         330
                  ....*....|...
gi 501080907  440 LGISRRALMYKLQ 452
Cdd:TIGR02329 513 LGISRTTLWRRLK 525
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
163-452 2.18e-88

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 272.70  E-value: 2.18e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 163 ALSQAN--VLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGT 240
Cdd:PRK11608  24 RLAPLDkpVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTGAQKRHPGRFERADGGT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRL--NVIHltLPPLRE 318
Cdd:PRK11608 104 LFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLDRLafDVVQ--LPPLRE 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 319 RREDIPLLANHFLQKFSSENQRDIIE-IDPSAMSLLTAWPWPGNIRELSNVIERAVV------MNTGAVI---FAEDLPT 388
Cdd:PRK11608 182 RQSDIMLMAEHFAIQMCRELGLPLFPgFTERARETLLNYRWPGNIRELKNVVERSVYrhgtseYPLDNIIidpFKRRPAE 261
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501080907 389 QFRQSVSHASGikPAQPgeRNLKEEIKREERRIIMEVLEQQEGNRTRTALMLGISR---RALMYKLQ 452
Cdd:PRK11608 262 EAIAVSETTSL--PTLP--LDLREWQHQQEKELLQRSLQQAKFNQKRAAELLGLTYhqlRALLKKHQ 324
PRK10820 PRK10820
transcriptional regulator TyrR;
144-456 2.66e-84

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 268.48  E-value: 2.66e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 144 HILTNSPGMMDICKDTAKIALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEKGAFT 223
Cdd:PRK10820 205 QIVAVSPKMRQVVEQARKLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAPGAYP 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 224 GAQTRRQGLFERAHQGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLF 303
Cdd:PRK10820 285 NALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGEFREDLY 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 304 YRLNVIHLTLPPLRERREDIPLLANHFLQKFSSENQRDIIEIDPSAMSLLTAWPWPGNIRELSNVIERAVVMNTGAVIFA 383
Cdd:PRK10820 365 YRLNVLTLNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNAIYRALTQLEGYELRP 444
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501080907 384 ED--LPtQFRQSVSHASGIKpaqpgERNLKEEIKREERRIIMEVLEQQEGNRtRTALMLGISRRALMYKLQEYGI 456
Cdd:PRK10820 445 QDilLP-DYDAAVAVGEDAM-----EGSLDEITSRFERSVLTRLYRNYPSTR-KLAKRLGVSHTAIANKLREYGL 512
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
129-459 2.42e-68

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 229.56  E-value: 2.42e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 129 IRSL--HQALSTSWQWGHILTNSPGMMDICKDTAKIALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALP 206
Cdd:PRK11388 309 MRQLmtSQLGKVSHTFDHMPQDSPQMRRLIHFGRQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAVNCQLYP 388
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 207 ESLLESELFGhekGAFTGAQTRRQGLFERAHQGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATN 286
Cdd:PRK11388 389 DEALAEEFLG---SDRTDSENGRLSKFELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPVDVRVIATTT 465
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 287 RNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERREDIPLLANHFLQKFSSENQRDiIEIDPSAMSLLTAWPWPGNIRELS 366
Cdd:PRK11388 466 ADLAMLVEQNRFSRQLYYALHAFEITIPPLRMRREDIPALVNNKLRSLEKRFSTR-LKIDDDALARLVSYRWPGNDFELR 544
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 367 NVIERAVVMNTGAVIFAEDLPTQFRQsvSHASGIKPAQPGERNLK-EEIkreERRIIMEVLEQQEGNRTRTALMLGISRR 445
Cdd:PRK11388 545 SVIENLALSSDNGRIRLSDLPEHLFT--EQATDDVSATRLSTSLSlAEL---EKEAIINAAQVCGGRIQEMAALLGIGRT 619
                        330
                 ....*....|....
gi 501080907 446 ALMYKLQEYGIDPA 459
Cdd:PRK11388 620 TLWRKMKQHGIDAG 633
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
165-371 1.14e-51

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: 182.72  E-value: 1.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 165 SQANVLISGESGTGKELIARAIhYNSRRAN----GPFIKINCAALPESLLESELFGHEKGAFTGAQTRRQGLFERAHQGT 240
Cdd:COG4650  207 SRAPILLTGPTGAGKSQLARRI-YELKKARhqvsGRFVEVNCATLRGDGAMSALFGHVKGAFTGAVSDRAGLLRSADGGV 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIQVDIRIVAATNRNLQEMVKEGTFREDLFYRLNVIHLTLPPLRERR 320
Cdd:COG4650  286 LFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLLARINLWTFRLPGLAERR 365
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501080907 321 EDIPLLANHFLQKFSSENQRDiIEIDPSAMSLLTA------WPWPGNIRELSNVIER 371
Cdd:COG4650  366 EDIEPNLDYELARFAREQGRR-VRFNKEARARYLAfatspeALWSGNFRDLNASVTR 421
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
5-120 5.87e-43

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 147.63  E-value: 5.87e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   5 YRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTA 84
Cdd:COG5803    3 KKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMMTA 82
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 501080907  85 YAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRAL 120
Cdd:COG5803   83 YGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLL 118
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
4-121 1.12e-39

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: 141.63  E-value: 1.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   4 RYRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMT 83
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLT 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 501080907  84 AYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQ 121
Cdd:COG0745   81 ARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLR 118
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
2-124 1.23e-39

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: 138.83  E-value: 1.23e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   2 KTRYRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRA--QHPRVPI 79
Cdd:COG0784    3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRAlpRLPDIPI 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 501080907  80 ILMTAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQA 124
Cdd:COG0784   83 IALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
6-120 1.76e-37

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: 132.78  E-value: 1.76e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAY 85
Cdd:cd19919    2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAH 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDELNLLIQRAL 120
Cdd:cd19919   82 SDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
7-121 2.78e-37

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: 132.46  E-value: 2.78e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAF---SLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMT 83
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIdweELGFEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 501080907  84 AYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQ 121
Cdd:cd17536   81 GYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKE 118
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
7-136 6.20e-37

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: 131.84  E-value: 6.20e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQAMKQEIRSLHQAL 136
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQL 130
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
8-106 1.28e-36

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: 130.04  E-value: 1.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   8 LIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYAE 87
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                         90
                 ....*....|....*....
gi 501080907  88 VETAVEALRSGAFDYVIKP 106
Cdd:cd00156   81 EEDAVRALELGADDYLVKP 99
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
7-121 1.78e-36

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: 129.92  E-value: 1.78e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQ 121
Cdd:cd17550   81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
6-106 1.96e-36

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: 129.51  E-value: 1.96e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAF-SLQGHET-QCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMT 83
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILeWEAGFEVvGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILS 80
                         90       100
                 ....*....|....*....|...
gi 501080907  84 AYAEVETAVEALRSGAFDYVIKP 106
Cdd:COG4753   81 GYSDFEYAQEAIKLGADDYLLKP 103
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
4-112 2.55e-36

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: 131.95  E-value: 2.55e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   4 RYRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRA--QHPRVPIIL 81
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRAdpRTADIPIIF 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 501080907  82 MTAYAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:COG3706   81 LTALDDEEDRARALEAGADDYLTKPFDPEEL 111
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1-136 1.46e-35

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: 131.44  E-value: 1.46e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   1 MKT--RYRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHP--R 76
Cdd:COG3437    1 MRTgqAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPStrD 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  77 VPIILMTAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQAMKQEIRSLHQAL 136
Cdd:COG3437   81 IPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYL 140
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
7-141 2.21e-35

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: 129.84  E-value: 2.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHG 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQAMKQEIRSLHQALSTSWQ 141
Cdd:COG4566   82 DVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAERARRAELRARLA 136
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
6-119 2.94e-34

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: 124.26  E-value: 2.94e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAY 85
Cdd:cd17554    2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAY 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 501080907  86 AEVETAVEALRSGAfdYVIKPFDLDELNLLIQRA 119
Cdd:cd17554   82 SEYKSDFSSWAADA--YVVKSSDLTELKETIKRL 113
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
3-128 6.03e-34

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 124.31  E-value: 6.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   3 TRYRILIVDDEDNVRRMLATAFS-LQGHET-QCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPII 80
Cdd:COG4565    2 KMIRVLIVEDDPMVAELLRRYLErLPGFEVvGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVI 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 501080907  81 LMTAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQAMKQE 128
Cdd:COG4565   82 VITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLRE 129
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
7-112 1.77e-33

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 121.87  E-value: 1.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907    7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100
                  ....*....|....*....|....*.
gi 501080907   87 EVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDEL 106
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
7-127 4.29e-33

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: 121.15  E-value: 4.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQAMKQ 127
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKLTK 121
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
8-106 1.19e-32

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: 119.43  E-value: 1.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   8 LIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYAE 87
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80
                         90
                 ....*....|....*....
gi 501080907  88 VETAVEALRSGAFDYVIKP 106
Cdd:cd17574   81 EEDKVLGLELGADDYITKP 99
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
6-119 1.05e-30

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: 114.61  E-value: 1.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAY 85
Cdd:cd17555    2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGA 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501080907  86 AEVETAVEALRSGAFDYVIKPF-DLDELNLLIQRA 119
Cdd:cd17555   82 GVMSDAVEALRLGAWDYLTKPIeDLAVLEHAVRRA 116
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
6-145 4.30e-30

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: 115.01  E-value: 4.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAY 85
Cdd:COG4567    6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLTGY 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDEL-NLLIQRALQLQAMKQEIRSLHQAlstswQWGHI 145
Cdd:COG4567   86 ASIATAVEAIKLGADDYLAKPADADDLlAALERAEGDAPAPPENPMSLDRL-----EWEHI 141
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
5-137 5.68e-30

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 116.45  E-value: 5.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   5 YRILIVDDEDNVRRMLATAfsLQGHE----TQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPII 80
Cdd:COG3279    2 MKILIVDDEPLARERLERL--LEKYPdlevVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPII 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501080907  81 LMTAYAEVetAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQAMKQEIRSLHQALS 137
Cdd:COG3279   80 FTTAYDEY--ALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEAKAAAEASPEEKD 134
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
161-369 8.43e-30

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: 122.91  E-value: 8.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 161 KIALSQA-----------NVLISGESGTGKELIARAIH----YNSRRA-NGPFIKINCAAL---PEsLLESELFGHEKGA 221
Cdd:COG1221  114 KNAIEQAkaailyppkglHTLILGPTGVGKSFFAELMYeyaiEIGVLPeDAPFVVFNCADYannPQ-LLMSQLFGYVKGA 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 222 FTGAQTRRQGLFERAHQGTLLLDEIGEMPLVLQAKLLRILQEREFERIG-GHQTIQVDIRIVAATNRNLQE-MVKegTFR 299
Cdd:COG1221  193 FTGADKDKEGLIEKADGGILFLDEVHRLPPEGQEMLFTFMDKGIYRRLGeTEKTRKANVRIIFATTEDPESsLLK--TFL 270
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501080907 300 EdlfyRLNVIhLTLPPLRER----REDiplLANHFLQKFSSENQRDIIeIDPSAMSLLTAWPWPGNIRELSNVI 369
Cdd:COG1221  271 R----RIPMV-IKLPSLEERsleeRLE---LIKHFFKEEAKRLNKPIK-VSKEVLKALLLYDCPGNIGQLKSDI 335
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
6-112 2.07e-29

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 111.00  E-value: 2.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAY 85
Cdd:cd17563    2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGY 81
                         90       100
                 ....*....|....*....|....*..
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17563   82 ASIATAVEAIKLGADDYLAKPADADEI 108
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
7-112 9.73e-29

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: 109.10  E-value: 9.73e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQ---HPRVPIILMT 83
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELeggGRRTPIIALT 80
                         90       100
                 ....*....|....*....|....*....
gi 501080907  84 AYAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQL 109
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
5-121 3.91e-28

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: 107.87  E-value: 3.91e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   5 YRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTA 84
Cdd:cd17569    1 PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTG 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 501080907  85 YAEVETAVEALRSGA-FDYVIKPFDLDELNLLIQRALQ 121
Cdd:cd17569   81 YADLDAAIEAINEGEiYRFLTKPWDDEELKETIRQALE 118
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
6-112 1.56e-27

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: 106.28  E-value: 1.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAY 85
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAK 80
                         90       100
                 ....*....|....*....|....*..
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17615   81 DSVEDRIAGLTAGGDDYVTKPFSLEEV 107
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
7-112 1.57e-26

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: 103.36  E-value: 1.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQC--ASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTA 84
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEPDIEVVgeAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80
                         90       100
                 ....*....|....*....|....*...
gi 501080907  85 YAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17535   81 HDDPEYVLRALKAGAAGYLLKDSSPEEL 108
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
7-107 2.63e-26

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: 102.20  E-value: 2.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQhPR---VPIILMT 83
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKAD-PAtrhIPVIFLT 79
                         90       100
                 ....*....|....*....|....
gi 501080907  84 AYAEVETAVEALRSGAFDYVIKPF 107
Cdd:cd19920   80 ALTDTEDKVKGFELGAVDYITKPF 103
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
7-112 3.30e-26

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: 102.46  E-value: 3.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                         90       100
                 ....*....|....*....|....*.
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17627   81 SVSDRVAGLDAGADDYLVKPFALEEL 106
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
7-116 8.01e-26

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: 101.00  E-value: 8.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHP--RVPIILMTA 84
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWlaNTPAIALTG 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 501080907  85 YAEVETAVEALRSGaFD-YVIKPFDLDELNLLI 116
Cdd:cd17580   81 YGQPEDRERALEAG-FDaHLVKPVDPDELIELI 112
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
6-112 8.97e-26

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: 101.36  E-value: 8.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDED-NVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQ--HPRVPIILM 82
Cdd:cd17551    2 RILIVDDNPtNLLLLEALLRSAGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALpgLEDVPIVMI 81
                         90       100       110
                 ....*....|....*....|....*....|
gi 501080907  83 TAYAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17551   82 TADTDREVRLRALEAGATDFLTKPFDPVEL 111
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
151-315 1.18e-25

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: 102.22  E-value: 1.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 151 GMMDICKDTAKIAL---SQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESELFGHEkgaftgAQT 227
Cdd:cd00009    1 VGQEEAIEALREALelpPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LVR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 228 RRQGLFERAHQGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHqtiqvDIRIVAATNRNLqemvkEGTFREDLFYRLN 307
Cdd:cd00009   75 LLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRE-----NVRVIGATNRPL-----LGDLDRALYDRLD 144

                 ....*...
gi 501080907 308 vIHLTLPP 315
Cdd:cd00009  145 -IRIVIPL 151
fixJ PRK09390
response regulator FixJ; Provisional
3-137 1.19e-25

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 103.54  E-value: 1.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   3 TRYRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILM 82
Cdd:PRK09390   2 DKGVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVM 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501080907  83 TAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQL-------QAMKQEIRSLHQALS 137
Cdd:PRK09390  82 TGHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQapeaaksEAVAADIRARIASLS 143
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
5-114 1.64e-25

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: 100.93  E-value: 1.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   5 YRILIVDDEDNVRRMLATAFSLQ-GHE---TqcASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPrVPII 80
Cdd:cd17541    1 IRVLIVDDSAVMRKLLSRILESDpDIEvvgT--ARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERP-TPVV 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 501080907  81 LMTAYAE--VETAVEALRSGAFDYVIKPFDLDELNL 114
Cdd:cd17541   78 MVSSLTEegAEITLEALELGAVDFIAKPSGGISLDL 113
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
4-138 1.99e-25

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: 102.73  E-value: 1.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   4 RYRILIVDDEDNVRRMLATAFSLQGHE-TQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRvPIILM 82
Cdd:COG3707    3 GLRVLVVDDEPLRRADLREGLREAGYEvVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPA-PVILL 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  83 TAYAEVETAVEALRSGAFDYVIKPFDLDEL----NLLIQRALQLQAMKQEIRSLHQALST 138
Cdd:COG3707   82 TAYSDPELIERALEAGVSAYLVKPLDPEDLlpalELALARFRELRALRRELAKLREALEE 141
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
7-120 2.55e-25

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: 99.98  E-value: 2.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:cd17537    3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHG 82
                         90       100       110
                 ....*....|....*....|....*....|....
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDELNLLIQRAL 120
Cdd:cd17537   83 DVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
6-107 3.99e-25

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: 99.11  E-value: 3.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQH--PRVPIILMT 83
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPetRHIPVIMIT 80
                         90       100
                 ....*....|....*....|....
gi 501080907  84 AYAEVETAVEALRSGAFDYVIKPF 107
Cdd:cd17538   81 ALDDREDRIRGLEAGADDFLSKPI 104
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
6-121 5.10e-25

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: 99.17  E-value: 5.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAY 85
Cdd:cd17553    2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAY 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQ 121
Cdd:cd17553   82 GELDMIQESKELGALTHFAKPFDIDEIRDAVKKYLP 117
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
7-112 8.49e-25

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: 98.33  E-value: 8.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                         90       100
                 ....*....|....*....|....*.
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVKPFALEEL 106
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
6-120 1.02e-24

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: 98.25  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHE-TQCASNGQTALQHFADAPPDVVLMDIRMP-EMNGIEALKVMRAQHPrVPIILMT 83
Cdd:cd17534    2 KILIVEDEAIIALDLKEILESLGYEvVGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKFD-IPVIFLT 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 501080907  84 AYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRAL 120
Cdd:cd17534   81 AYSDEETLERAKETNPYGYLVKPFNERELKAAIELAL 117
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
6-117 1.43e-24

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: 98.09  E-value: 1.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQ--HPRVPIILMT 83
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDemTRDIPIIMLT 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 501080907  84 AYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQ 117
Cdd:cd17618   82 ARGEEEDKVRGLEAGADDYITKPFSPRELVARIK 115
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
8-117 2.47e-24

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: 97.29  E-value: 2.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   8 LIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYAE 87
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 501080907  88 VETAVEALRSGAFDYVIKPFDLDELNLLIQ 117
Cdd:cd17625   81 VEDRVKGLDLGADDYLPKPFSLAELLARIR 110
orf27 CHL00148
Ycf27; Reviewed
2-121 4.31e-24

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 100.56  E-value: 4.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   2 KTRYRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQhPRVPIIL 81
Cdd:CHL00148   4 NSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKE-SDVPIIM 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 501080907  82 MTAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQ 121
Cdd:CHL00148  83 LTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLR 122
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
5-112 1.21e-23

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: 95.39  E-value: 1.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   5 YRILIVDDEDNVRRMLATAFSLQGHETQC--ASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILM 82
Cdd:cd19925    1 INVLIVEDDPMVAEIHRAYVEQVPGFTVIgtAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVV 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 501080907  83 TAYAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd19925   81 TAANDVETVREALRLGVVDYLIKPFTFERL 110
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
7-106 1.22e-23

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: 94.54  E-value: 1.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRaQHPRVPIILMTAYA 86
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR-EWSAVPVIVLSARD 79
                         90       100
                 ....*....|....*....|
gi 501080907  87 EVETAVEALRSGAFDYVIKP 106
Cdd:cd17620   80 EESDKIAALDAGADDYLTKP 99
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
6-120 3.68e-23

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: 94.02  E-value: 3.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQC-ASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPrVPIILMTA 84
Cdd:cd19932    2 RVLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENI-APIVLLTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 501080907  85 YAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRAL 120
Cdd:cd19932   81 YSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAI 116
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
5-120 4.22e-23

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 93.88  E-value: 4.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   5 YRILIVDDEDNVRRMLATAFSLQGHETQC-ASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMT 83
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCS 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 501080907  84 AYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRAL 120
Cdd:cd17542   81 AMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
6-112 1.42e-21

phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response regulator protein acting with PhoR in a 2-component system responding to phosphate ion. PhoB acts as a positive regulator of gene expression for phosphate-related genes such as phoA, phoS, phoE and ugpAB as well as itself. It is often found proximal to genes for the high-affinity phosphate ABC transporter (pstSCAB; GenProp0190) and presumably regulates these as well. [Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 92.78  E-value: 1.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907    6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQhPR---VPIILM 82
Cdd:TIGR02154   4 RILVVEDEPAIRELIAYNLEKAGYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRR-PEtraIPIIML 82
                          90       100       110
                  ....*....|....*....|....*....|
gi 501080907   83 TAYAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:TIGR02154  83 TARGEEEDRVRGLETGADDYITKPFSPREL 112
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
7-106 6.51e-21

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: 87.11  E-value: 6.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80
                         90       100
                 ....*....|....*....|
gi 501080907  87 EVETAVEALRSGAFDYVIKP 106
Cdd:cd19935   81 SVEDRVKGLDLGADDYLVKP 100
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
8-120 6.68e-21

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: 87.71  E-value: 6.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   8 LIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQ--HPRVPIILMTAY 85
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDpkTSSIPIIMLTAK 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDELNLLIQRAL 120
Cdd:cd19937   81 GEEFDKVLGLELGADDYITKPFSPRELLARVKAVL 115
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
146-316 1.62e-20

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 87.40  E-value: 1.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  146 LTNSPGMMDICKDTAKIALSQANVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLESelfghekgaftga 225
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLEQ------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  226 qtrrqglferAHQGTLLLDEIGEMPLVLQAKLLRILQEREferigghqtiQVDIRIVAATNRNLQEMVKEGTFREDLFYR 305
Cdd:pfam14532  68 ----------AKGGTLYLKDIADLSKALQKGLLLLLAKAE----------GYRVRLVCTSSKDLPQLAAAGLFDEQLYFE 127
                         170
                  ....*....|.
gi 501080907  306 LNVIHLTLPPL 316
Cdd:pfam14532 128 LSALRLHVPPL 138
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
6-112 2.09e-20

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: 86.37  E-value: 2.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPrVPIILMTAY 85
Cdd:cd17626    2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAESG-VPIVMLTAK 80
                         90       100
                 ....*....|....*....|....*..
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17626   81 SDTVDVVLGLESGADDYVAKPFKPKEL 107
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
7-112 3.55e-20

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: 85.43  E-value: 3.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRaQHPRVPIILMTAYA 86
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELR-KTSQVPVLMLTARG 79
                         90       100
                 ....*....|....*....|....*.
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17623   80 DDIDRILGLELGADDYLPKPFNPREL 105
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
6-112 3.72e-20

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 88.87  E-value: 3.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTA- 84
Cdd:PRK11083   5 TILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTAr 84
                         90       100
                 ....*....|....*....|....*...
gi 501080907  85 YAEVETAVeALRSGAFDYVIKPFDLDEL 112
Cdd:PRK11083  85 SDEVDRLV-GLEIGADDYVAKPFSPREV 111
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
6-118 2.49e-19

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: 83.62  E-value: 2.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQG--HETQCASNGQTALQH------FADAP-PDVVLMDIRMPEMNGIEALKVMRaQHP- 75
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDFlrgegeYADAPrPDLILLDLNMPRMDGFEVLREIK-ADPd 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 501080907  76 --RVPIILMTAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQR 118
Cdd:cd17557   80 lrRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRS 124
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
6-112 3.45e-19

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: 82.97  E-value: 3.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQhP---RVPIILM 82
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKED-PatrDIPVIAL 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 501080907  83 TAYAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17548   80 TAYAMKGDREKILEAGCDGYISKPIDTREF 109
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
5-112 3.73e-19

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: 82.82  E-value: 3.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   5 YRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRaQHPRVPIILMTA 84
Cdd:cd17619    1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELR-EQSEVGIILVTG 79
                         90       100
                 ....*....|....*....|....*...
gi 501080907  85 YAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17619   80 RDDEVDRIVGLEIGADDYVTKPFNPREL 107
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
7-112 4.41e-19

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: 82.47  E-value: 4.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHpRVPIILMTAYA 86
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTAKD 79
                         90       100
                 ....*....|....*....|....*.
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17614   80 SEVDKVLGLELGADDYVTKPFSNREL 105
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
7-119 9.27e-19

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: 81.56  E-value: 9.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDEL----NLLIQRA 119
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTKPFHIEELlarlRALIRRA 117
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
7-106 1.11e-18

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: 81.05  E-value: 1.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                         90       100
                 ....*....|....*....|
gi 501080907  87 EVETAVEALRSGAFDYVIKP 106
Cdd:cd19926   81 SLDTAIEALKAGAFDFLTKP 100
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
6-120 1.82e-18

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: 80.85  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHE-TQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQH--PRVPIILM 82
Cdd:cd19923    2 KVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGalSHLPVLMV 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 501080907  83 TAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRAL 120
Cdd:cd19923   82 TAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
7-122 2.03e-18

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 80.66  E-value: 2.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDE----DNVRRMLATAFSLQghETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILM 82
Cdd:cd17532    1 ALIVDDEplarEELRYLLEEHPDIE--IVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFV 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 501080907  83 TAYAEVetAVEALRSGAFDYVIKPFDLDELNLLIQRALQL 122
Cdd:cd17532   79 TAYDEY--AVEAFELNAVDYLLKPFSEERLAEALAKLRKR 116
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
7-120 2.06e-18

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: 80.40  E-value: 2.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRaQHPRVPIILMTAYA 86
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIR-QISNVPIIFISSRD 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDELNLLIQRAL 120
Cdd:cd18159   80 DNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
6-107 2.11e-18

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 80.24  E-value: 2.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHF-ADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTA 84
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLqQGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80
                         90       100
                 ....*....|....*....|...
gi 501080907  85 YAEVETAVEALRSGAFDYVIKPF 107
Cdd:cd18160   81 GAAAAPELLSDAVGDNATLKKPF 103
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
6-121 2.60e-18

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: 80.67  E-value: 2.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMlaTAFSLQ---GHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAqHP---RVPI 79
Cdd:cd17552    3 RILVIDDEEDIREV--VQACLEklaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQA-NPetqSIPV 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 501080907  80 ILMTAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQ 121
Cdd:cd17552   80 ILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLLG 121
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
6-138 2.61e-18

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: 80.87  E-value: 2.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDE----DNVRRMLATAFslqghETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIIL 81
Cdd:cd17596    2 TILVVDDEvrslEALRRTLEEDF-----DVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRII 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 501080907  82 MTAYAEVETAVEALR-SGAFDYVIKPFDLDELNLLIQRALQLQAMKQEirslHQALST 138
Cdd:cd17596   77 ISGYTDSEDIIAGINeAGIYQYLTKPWHPDQLLLTVRNAARLFELQRE----NERLSL 130
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
5-139 5.01e-18

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 85.20  E-value: 5.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   5 YRILIVDDEDNVRRMLATAFSLQgHETQ---CASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPrVPIIL 81
Cdd:PRK00742   4 IRVLVVDDSAFMRRLISEILNSD-PDIEvvgTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRP-TPVVM 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501080907  82 MTAYAE--VETAVEALRSGAFDYVIKPF-----DLDEL-NLLIQRAlqLQAMKQEIRSLHQALSTS 139
Cdd:PRK00742  82 VSSLTErgAEITLRALELGAVDFVTKPFlgislGMDEYkEELAEKV--RAAARARVRALPPRAAAA 145
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
7-106 7.69e-18

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: 78.70  E-value: 7.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                         90       100
                 ....*....|....*....|
gi 501080907  87 EVETAVEALRSGAFDYVIKP 106
Cdd:cd19928   81 TLMTAVKAAERGAFEYLPKP 100
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
6-120 1.84e-17

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


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 78.11  E-value: 1.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRaQHPR---VPIILM 82
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELR-KLPAykfTPILML 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 501080907  83 TAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRAL 120
Cdd:cd17562   81 TTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
7-106 3.86e-17

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: 76.71  E-value: 3.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHpRVPIILMTAYA 86
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKS-TLPVIFLTSKD 79
                         90       100
                 ....*....|....*....|
gi 501080907  87 EVETAVEALRSGAFDYVIKP 106
Cdd:cd19936   80 DEIDEVFGLRMGADDYITKP 99
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
6-106 7.85e-17

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 81.47  E-value: 7.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQ-GHET-QCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPrVPIILMT 83
Cdd:PRK12555   2 RIGIVNDSPLAVEALRRALARDpDHEVvWVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERP-CPILIVT 80
                         90       100
                 ....*....|....*....|....*
gi 501080907  84 AYAE--VETAVEALRSGAFDYVIKP 106
Cdd:PRK12555  81 SLTErnASRVFEAMGAGALDAVDTP 105
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
6-112 1.35e-16

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 75.49  E-value: 1.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRaQHPRVPIILMTAY 85
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR-RFSDVPIIMVTAR 79
                         90       100
                 ....*....|....*....|....*..
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd19938   80 VEEIDRLLGLELGADDYICKPYSPREV 106
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
7-120 2.08e-16

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: 74.97  E-value: 2.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPP--DVVLMDIRMPEMNGIEALKVMRAQhPRVPIILMTA 84
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDefDLVITDVHMPDMDGFEFLELIRLE-MDLPVIMMSA 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 501080907  85 YAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRAL 120
Cdd:cd17584   80 DGSTSTVMKGLAHGACDYLLKPVSIEDLKNIWQHVV 115
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
7-107 2.90e-16

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: 74.31  E-value: 2.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFA-DAPPDVVLMDIRMP-EMNGIEALKVMRAQHPRVPIILMTA 84
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLEsGPDIDLLVTDVIMPgGMNGSQLAEEARRRRPDLKVLLTSG 80
                         90       100
                 ....*....|....*....|...
gi 501080907  85 YAEVETAVEALRSGaFDYVIKPF 107
Cdd:cd18161   81 YAENAIEGGDLAPG-VDVLSKPF 102
PRK15479 PRK15479
transcriptional regulator TctD;
6-120 4.19e-16

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 77.07  E-value: 4.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAY 85
Cdd:PRK15479   2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTAR 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDELNLLIqRAL 120
Cdd:PRK15479  82 SAVADRVKGLNVGADDYLPKPFELEELDARL-RAL 115
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
6-112 7.07e-16

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: 73.56  E-value: 7.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRaQHPRVPIILMTAY 85
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVR-EHSHVPILMLTAR 79
                         90       100
                 ....*....|....*....|....*..
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd19939   80 TEEMDRVLGLEMGADDYLCKPFSPREL 106
resp_reg_YycF NF040534
response regulator YycF;
6-128 7.64e-16

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 76.68  E-value: 7.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHpRVPIILMTAY 85
Cdd:NF040534   2 KILVVDDEKPIADILEFNLKKEGYEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKKY-DMPIIMLTAK 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDEL------NLliqRALQLQAMKQE 128
Cdd:NF040534  81 DSEIDKVLGLELGADDYVTKPFSTRELiarvkaNL---RRHQQQNTEEE 126
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
6-112 7.78e-16

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 76.77  E-value: 7.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFaDAPPDVVLMDIRMPEMNGIEALKVMRAQHpRVPIILMTAY 85
Cdd:PRK10955   3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLL-DDSIDLLLLDVMMPKKNGIDTLKELRQTH-QTPVIMLTAR 80
                         90       100
                 ....*....|....*....|....*..
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:PRK10955  81 GSELDRVLGLELGADDYLPKPFNDREL 107
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
7-120 1.28e-15

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: 72.74  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQhPR---VPIILMT 83
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSD-PDlkdIPVILLT 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 501080907  84 AYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRAL 120
Cdd:cd17598   80 TLSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
PRK10643 PRK10643
two-component system response regulator PmrA;
6-142 2.48e-15

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 75.07  E-value: 2.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAY 85
Cdd:PRK10643   2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTAR 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDELNLLIqRALqlqamkqeIRSlHQALSTSWQW 142
Cdd:PRK10643  82 DTLEDRVAGLDVGADDYLVKPFALEELHARI-RAL--------IRR-HQGQGENELQ 128
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
6-112 2.94e-15

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: 71.78  E-value: 2.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLAT---AFSLQGHEtqcASNGQTALQHFADAPP-DVVLMDIRMPEMNGIEALKVMRAQHPR--VPI 79
Cdd:cd17544    2 KVLVVDDSATSRNHLRAllrRHNFQVLE---AANGQEALEVLEQHPDiKLVITDYNMPEMDGFELVREIRKKYSRdqLAI 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 501080907  80 ILMTAYAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17544   79 IGISASGDNALSARFIKAGANDFLTKPFLPEEF 111
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
7-112 4.38e-15

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: 70.92  E-value: 4.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80
                         90       100
                 ....*....|....*....|....*.
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17573   81 KTEQEIEAFKEGADDYIAKPFDFKVL 106
pleD PRK09581
response regulator PleD; Reviewed
6-130 4.38e-15

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 77.25  E-value: 4.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDD-EDNVR----RMLATAFslqghETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQhPR---V 77
Cdd:PRK09581   4 RILVVDDiPANVKlleaKLLAEYY-----TVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSD-PAtthI 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 501080907  78 PIILMTAYAEVETAVEALRSGAFDYVIKPfdLDELNLLIQ-RAL-QLQAMKQEIR 130
Cdd:PRK09581  78 PVVMVTALDDPEDRVRGLEAGADDFLTKP--INDVALFARvKSLtRLKMVIDELR 130
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
5-59 8.28e-15

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: 68.36  E-value: 8.28e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 501080907     5 YRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMP 59
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK15347 PRK15347
two component system sensor kinase;
4-123 1.59e-14

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 76.22  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   4 RYRILIVDDEDNVR----RMLATafslQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMR----AQHP 75
Cdd:PRK15347 690 QLQILLVDDVETNRdiigMMLVE----LGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRddpnNLDP 765
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501080907  76 RVPIILMTAYA---EVETAVEAlrsGAFDYVIKPFDLDELNLLIQRALQLQ 123
Cdd:PRK15347 766 DCMIVALTANAapeEIHRCKKA---GMNHYLTKPVTLAQLARALELAAEYQ 813
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
7-106 1.64e-14

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: 69.15  E-value: 1.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQhPRVPIILMTAY- 85
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRAR-SNVPVIMVTAKd 79
                         90       100
                 ....*....|....*....|.
gi 501080907  86 AEVETAVeALRSGAFDYVIKP 106
Cdd:cd17621   80 SEIDKVV-GLELGADDYVTKP 99
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
6-112 2.39e-14

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 72.26  E-value: 2.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAY 85
Cdd:PRK09836   2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTAL 81
                         90       100
                 ....*....|....*....|....*..
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:PRK09836  82 GTIEHRVKGLELGADDYLVKPFAFAEL 108
PRK10816 PRK10816
two-component system response regulator PhoP;
6-117 2.52e-14

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 72.08  E-value: 2.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAY 85
Cdd:PRK10816   2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTAR 81
                         90       100       110
                 ....*....|....*....|....*....|..
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDELNLLIQ 117
Cdd:PRK10816  82 ESWQDKVEVLSAGADDYVTKPFHIEEVMARMQ 113
PRK10693 PRK10693
two-component system response regulator RssB;
33-112 8.77e-14

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 71.95  E-value: 8.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  33 CASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYAEVETAVEALRSGAFDYVIKPF-DLDE 111
Cdd:PRK10693   2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVkDLNR 81

                 .
gi 501080907 112 L 112
Cdd:PRK10693  82 L 82
PRK10610 PRK10610
chemotaxis protein CheY;
6-107 8.93e-14

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 68.08  E-value: 8.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQG-HETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRA--QHPRVPIILM 82
Cdd:PRK10610   7 KFLVVDDFSTMRRIVRNLLKELGfNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRAdgAMSALPVLMV 86
                         90       100
                 ....*....|....*....|....*
gi 501080907  83 TAYAEVETAVEALRSGAFDYVIKPF 107
Cdd:PRK10610  87 TAEAKKENIIAAAQAGASGYVVKPF 111
PRK10336 PRK10336
two-component system response regulator QseB;
6-151 9.38e-14

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 70.31  E-value: 9.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAY 85
Cdd:PRK10336   2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTAR 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFdldelnLLIQRALQLQAMkqeIRSLHQALSTSWQWGHILTNsPG 151
Cdd:PRK10336  82 DALAERVEGLRLGADDYLCKPF------ALIEVAARLEAL---MRRTNGQASNELRHGNVMLD-PG 137
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
4-68 1.19e-13

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: 67.61  E-value: 1.19e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501080907   4 RYRILIVDDEDNVRRMLATAFSLQGHETQC--ASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALK 68
Cdd:COG2197    1 MIRVLIVDDHPLVREGLRALLEAEPDIEVVgeAADGEEALELLEELRPDVVLLDIRMPGMDGLEALR 67
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
6-118 1.51e-13

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: 66.79  E-value: 1.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQ-GHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTA 84
Cdd:cd17593    2 KVLICDDSSMARKQLARALPADwDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVSG 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501080907  85 YAEVEtAVEALRS-GAFDYVIKPFDLDELNLLIQR 118
Cdd:cd17593   82 DVQPE-AKERVLElGALAFLKKPFDPEKLAQLLEE 115
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
7-121 1.69e-13

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 69.45  E-value: 1.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRaQHPRVPIILMTAYA 86
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLR-QWSAIPVIVLSARS 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQ 121
Cdd:PRK10529  83 EESDKIAALDAGADDYLSKPFGIGELQARLRVALR 117
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
7-112 2.02e-13

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: 66.66  E-value: 2.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                         90       100
                 ....*....|....*....|....*.
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKPFHKDEL 106
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
7-121 2.20e-13

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate/nitrite response regulator protein NarL contains an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. Escherichia coli NarL activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons, and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal. Phosphorylation of the NarL REC domain releases the C-terminal HTH output domain that subsequently binds specific DNA promoter sites to repress or activate gene expression. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 66.60  E-value: 2.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDE----DNVRRMLATA--FSLQGHetqcASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPII 80
Cdd:cd19931    1 VLLIDDHpllrKGIKQLIELDpdFTVVGE----ASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIV 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 501080907  81 LMTAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQ 121
Cdd:cd19931   77 ILTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAAS 117
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
6-107 4.08e-13

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 65.32  E-value: 4.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQ-GHE-TQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQ--HPRVPIIL 81
Cdd:cd17561    3 KVLIADDNREFVQLLEEYLNSQpDMEvVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMrlEKRPKIIM 82
                         90       100
                 ....*....|....*....|....*.
gi 501080907  82 MTAYAEVETAVEALRSGAFDYVIKPF 107
Cdd:cd17561   83 LTAFGQEDITQRAVELGASYYILKPF 108
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
168-287 6.24e-13

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: 66.24  E-value: 6.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   168 NVLISGESGTGKELIARAIHYNSRRANGPFIKINCAALPESLLES---ELFGHEKGAFTGAQTRRQgLFERAHQ---GTL 241
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRL-ALALARKlkpDVL 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 501080907   242 LLDEIGEMPLVLQAKLLRILqerEFERIGGHQTIQVDIRIVAATNR 287
Cdd:smart00382  83 ILDEITSLLDAEQEALLLLL---EELRLLLLLKSEKNLTVILTTND 125
ompR PRK09468
osmolarity response regulator; Provisional
1-124 9.49e-13

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 67.69  E-value: 9.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   1 MKTRYRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPII 80
Cdd:PRK09468   2 MQENYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPII 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 501080907  81 LMTAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQA 124
Cdd:PRK09468  82 MLTAKGEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVLRRQA 125
PRK10766 PRK10766
two-component system response regulator TorR;
5-115 1.01e-12

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 67.37  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   5 YRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQhPRVPIILMTA 84
Cdd:PRK10766   3 YHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSR-STVGIILVTG 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 501080907  85 YAEVETAVEALRSGAFDYVIKPFDLDEL-----NLL 115
Cdd:PRK10766  82 RTDSIDRIVGLEMGADDYVTKPLELRELlvrvkNLL 117
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
6-108 1.10e-12

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: 64.32  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHpRVPIILMTAY 85
Cdd:cd17622    2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKY-QGPILLLTAL 80
                         90       100
                 ....*....|....*....|...
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFD 108
Cdd:cd17622   81 DSDIDHILGLELGADDYVVKPVE 103
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
7-112 1.41e-12

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: 64.00  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQhPRVPIILMTAYA 86
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRAR-SDVPIIIISGDR 80
                         90       100
                 ....*....|....*....|....*..
gi 501080907  87 EVETA-VEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17594   81 RDEIDrVVGLELGADDYLAKPFGLREL 107
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
6-121 1.53e-12

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 67.05  E-value: 1.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMR--AQHPRVPIILMT 83
Cdd:PRK10161   4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKreSMTRDIPVVMLT 83
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 501080907  84 AYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQ 121
Cdd:PRK10161  84 ARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMR 121
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
7-106 2.26e-12

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 63.19  E-value: 2.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPP--DVVLMDIRMPEMNGIEAL-KVMRAQH-PRVPIILM 82
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNeiDLILTEVDLPVSSGFKLLsYIMRHKIcKNIPVIMM 80
                         90       100
                 ....*....|....*....|....
gi 501080907  83 TAYAEVETAVEALRSGAFDYVIKP 106
Cdd:cd17582   81 SSQDSVGVVFKCLSKGAADYLVKP 104
PRK15369 PRK15369
two component system response regulator;
5-105 2.35e-12

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 65.87  E-value: 2.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   5 YRILIVDDE----DNVRRMLAT--AFSLQGHetqcASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVP 78
Cdd:PRK15369   4 YKILLVDDHeliiNGIKNMLAPypRYKIVGQ----VDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMN 79
                         90       100
                 ....*....|....*....|....*..
gi 501080907  79 IILMTAYAEVETAVEALRSGAFDYVIK 105
Cdd:PRK15369  80 ILVLTARQEEHMASRTLAAGALGYVLK 106
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
7-118 1.08e-11

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 61.52  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCA--SNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTA 84
Cdd:cd19930    1 VLIAEDQEMVRGALAALLELEDDLEVVAqaSNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 501080907  85 YAEVETAVEALRSGAFDYVIKPFDLDELNLLIQR 118
Cdd:cd19930   81 FGRPGYFRRALAAGVDGYVLKDRPIEELADAIRT 114
PRK11697 PRK11697
two-component system response regulator BtsR;
6-132 1.14e-11

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 64.48  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDE----DNVRRMLATA--FSLQGhetQCaSNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQH-PRvp 78
Cdd:PRK11697   3 KVLIVDDEplarEELRELLQEEgdIEIVG---EC-SNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGMLDPEHmPY-- 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501080907  79 IILMTAYAEVetAVEALRSGAFDYVIKPFDLDELNLLIQRaLQLQAMKQEIRSL 132
Cdd:PRK11697  77 IVFVTAFDEY--AIKAFEEHAFDYLLKPIDPARLAKTLAR-LRQERSPQDVLLP 127
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
6-107 1.51e-11

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 64.32  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRaQHPRVPIILMTAY 85
Cdd:PRK10710  12 RILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIR-RFSDIPIVMVTAK 90
                         90       100
                 ....*....|....*....|..
gi 501080907  86 AEVETAVEALRSGAFDYVIKPF 107
Cdd:PRK10710  91 IEEIDRLLGLEIGADDYICKPY 112
PRK11517 PRK11517
DNA-binding response regulator HprR;
6-112 1.99e-11

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 63.38  E-value: 1.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHpRVPIILMTAY 85
Cdd:PRK11517   2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAK-QTPVICLTAR 80
                         90       100
                 ....*....|....*....|....*..
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:PRK11517  81 DSVDDRVRGLDSGANDYLVKPFSFSEL 107
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
7-106 2.39e-11

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: 60.08  E-value: 2.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMR--AQHPRVPIILMTA 84
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRknADFDTIPVIFLTA 80
                         90       100
                 ....*....|....*....|..
gi 501080907  85 YAEVETAVEALRSGAFDYVIKP 106
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
6-119 3.18e-11

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 62.74  E-value: 3.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRR------MLATAFSLQGHetqcASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPI 79
Cdd:PRK10651   8 TILLIDDHPMLRTgvkqliSMAPDITVVGE----ASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRI 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 501080907  80 ILMTAYAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRA 119
Cdd:PRK10651  84 VVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQA 123
PRK11173 PRK11173
two-component response regulator; Provisional
1-140 6.42e-11

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 62.34  E-value: 6.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   1 MKTrYRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRaQHPRVPII 80
Cdd:PRK11173   1 MQT-PHILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELR-EQANVALM 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501080907  81 LMTAY-AEVETaVEALRSGAFDYVIKPFDLDELNL----LIQRALQLQAMKQEIRSLHQALSTSW 140
Cdd:PRK11173  79 FLTGRdNEVDK-ILGLEIGADDYITKPFNPRELTIrarnLLSRTMNLGTVSEERRSVESYKFNGW 142
PRK13557 PRK13557
histidine kinase; Provisional
6-120 1.74e-10

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 63.15  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFAD-APPDVVLMDIRMP-EMNGIEALKVMRAQHPRVPIILMT 83
Cdd:PRK13557 417 TILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDShPEVDLLFTDLIMPgGMNGVMLAREARRRQPKIKVLLTT 496
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 501080907  84 AYAevETAVEalRSGA----FDYVIKPFDLDELNLLIQRAL 120
Cdd:PRK13557 497 GYA--EASIE--RTDAggseFDILNKPYRRAELARRVRMVL 533
dpiA PRK10046
two-component response regulator DpiA; Provisional
7-134 3.19e-10

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 60.03  E-value: 3.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFS-LQG-HETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTA 84
Cdd:PRK10046   7 LLIVEDETPLAEMHAEYIRhIPGfSQILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPGDVVFTTA 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 501080907  85 YAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQAMKQEIRSLHQ 134
Cdd:PRK10046  87 ASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRFRQRKHMLESIDSASQ 136
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
7-106 4.44e-10

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 56.51  E-value: 4.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQ--GHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTA 84
Cdd:cd17565    1 FYIVDDDKNIIKILSDIIEDDdlGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQ 80
                         90       100
                 ....*....|....*....|..
gi 501080907  85 YAEVETAVEALRSGAFDYVIKP 106
Cdd:cd17565   81 VSDKEMIGKAYQAGIEFFINKP 102
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
7-108 5.89e-10

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: 57.35  E-value: 5.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRmlATAFSLQGH-----ETQCASNGQTALQHFAD-----APPDVVLMDIRMPEMNGIEALKVMRAQHPR 76
Cdd:cd17595    3 ILTVDDDPQVLR--AVARDLRRQygkdyRVLRADSGAEALDALKElklrgEAVALFLVDQRMPEMDGVEFLEKAMELFPE 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 501080907  77 VPIILMTAYAEVETAVEALRSGAFD-YVIKPFD 108
Cdd:cd17595   81 AKRVLLTAYADTDAAIRAINDVQLDyYLLKPWD 113
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
1-145 8.08e-10

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 61.29  E-value: 8.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907    1 MKTRYRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPII 80
Cdd:PRK09959  955 LPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIW 1034
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501080907   81 LMTAYAEVETAVEALRSGafdyvikpfdldeLNLLIQRALQLQAMKQEIRSLHQALSTSWQWGHI 145
Cdd:PRK09959 1035 GLTANAQANEREKGLSCG-------------MNLCLFKPLTLDVLKTHLSQLHQVAHIAPQYRHL 1086
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
7-106 1.06e-09

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 55.45  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMR-AQHPR-VPIILMTA 84
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRkSSALKdTPIIMLTG 80
                         90       100
                 ....*....|....*....|..
gi 501080907  85 YAEVETAVEALRSGAFDYVIKP 106
Cdd:cd17602   81 KDGLVDRIRAKMAGASGYLTKP 102
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
7-106 1.12e-09

phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 55.85  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPP---------DVVLMDIRMPEMNGIEALKVMRaQHPR- 76
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKegndlskelDLIITDIEMPKMDGYELTFELR-DDPRl 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 501080907  77 --VPIILMTAYAEVETAVEALRSGAFDYVIKP 106
Cdd:cd19924   80 anIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
34-158 1.20e-09

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 60.63  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  34 ASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMR--AQHPRVPIILMTAYAEVETAVEALRSGAFDYVIKPFDLDE 111
Cdd:PRK11107 697 CDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRqlPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAM 776
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501080907 112 LNLLIQR-----ALQLQAMKQEIRSLHQALSTSWQWGHILTNSPGMMDICKD 158
Cdd:PRK11107 777 LKQVLLRykpgpKFTSRVVAPEPPEPVHFPNATLDWQLALRQAAGKPDLARD 828
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
418-453 1.94e-09

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 52.78  E-value: 1.94e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 501080907  418 ERRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQE 453
Cdd:pfam02954   5 EKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
6-112 5.06e-09

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 58.83  E-value: 5.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAY 85
Cdd:PRK10841 803 MILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTAN 882
                         90       100
                 ....*....|....*....|....*..
gi 501080907  86 AEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:PRK10841 883 ALAEEKQRCLEAGMDSCLSKPVTLDVL 909
PRK10430 PRK10430
two-component system response regulator DcuR;
7-107 7.92e-09

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 55.88  E-value: 7.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNV----RRMLA--TAFSLQGhetqCASNGQTALQHFADA--PPDVVLMDIRMPEMNGIEALKVMRAQHPRVP 78
Cdd:PRK10430   4 VLIVDDDAMVaelnRRYVAqiPGFQCCG----TASTLEQAKEIIFNSdtPIDLILLDIYMQQENGLDLLPVLHEAGCKSD 79
                         90       100
                 ....*....|....*....|....*....
gi 501080907  79 IILMTAYAEVETAVEALRSGAFDYVIKPF 107
Cdd:PRK10430  80 VIVISSAADAATIKDSLHYGVVDYLIKPF 108
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
6-112 1.03e-08

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: 53.57  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDE----DNVRRMLATAFSLQGHetQCaSNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAqHP---RVP 78
Cdd:cd17575    2 MVLLVDDQaiigEAVRRALADEEDIDFH--YC-SDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRA-NPatrDIP 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 501080907  79 IILMTAYAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17575   78 IIVLSTKEEPEVKSEAFALGANDYLVKLPDKIEL 111
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
6-119 1.15e-08

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: 53.21  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFS--LQGHeTQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMT 83
Cdd:cd17530    2 RVLVLDDDPFQCMMAATILEdlGPGN-VDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMS 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 501080907  84 AY-----AEVETAVEALRSGAFDYVIKPFDLDELNLLIQRA 119
Cdd:cd17530   81 GLdggilESAETLAGANGLNLLGTLSKPFSPEELTELLTKY 121
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
6-112 2.64e-08

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 52.02  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDnVRRMLATAFSLQ-GHETQCASNGQTALQHFADAPPD--VVLMDIRMPEMNGIE-ALKV--MRAQHPRVPI 79
Cdd:cd19933    2 KVLLVDDNA-VNRMVTKGLLEKlGCEVTTVSSGEECLNLLASAEHSfqLVLLDLCMPEMDGFEvALRIrkLFGRRERPLI 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 501080907  80 ILMTAYAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd19933   81 VALTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
PRK09483 PRK09483
response regulator; Provisional
7-105 6.42e-08

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 53.19  E-value: 6.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVR----RML--ATAFSLQGhETQCasnGQTALQHFADAPPDVVLMDIRMPEMNGIEAL-KVMRAQhPRVPI 79
Cdd:PRK09483   4 VLLVDDHELVRagirRILedIKGIKVVG-EACC---GEDAVKWCRTNAVDVVLMDMNMPGIGGLEATrKILRYT-PDVKI 78
                         90       100
                 ....*....|....*....|....*.
gi 501080907  80 ILMTAYAEVETAVEALRSGAFDYVIK 105
Cdd:PRK09483  79 IMLTVHTENPLPAKVMQAGAAGYLSK 104
PRK14084 PRK14084
DNA-binding response regulator;
6-119 4.14e-07

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 50.91  E-value: 4.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGH--ETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIE-ALKVMRAQHPrvP-IIL 81
Cdd:PRK14084   2 KALIVDDEPLARNELTYLLNEIGGfeEINEAENVKETLEALLINQYDIIFLDINLMDESGIElAAKIQKMKEP--PaIIF 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 501080907  82 MTAYAEVetAVEALRSGAFDYVIKPFDLDELNLLIQRA 119
Cdd:PRK14084  80 ATAHDQF--AVKAFELNATDYILKPFEQKRIEQAVNKV 115
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
6-84 4.54e-07

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 52.25  E-value: 4.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDD-EDNVrrMLATAF--SLqGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPR---VPI 79
Cdd:PRK11091 527 NILLVEDiELNV--IVARSVleKL-GNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPRedlPPL 603

                 ....*
gi 501080907  80 ILMTA 84
Cdd:PRK11091 604 VALTA 608
Fis COG2901
DNA-binding protein Fis (factor for inversion stimulation) [Transcription];
418-457 5.89e-07

DNA-binding protein Fis (factor for inversion stimulation) [Transcription];


Pssm-ID: 442146 [Multi-domain]  Cd Length: 83  Bit Score: 47.12  E-value: 5.89e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 501080907 418 ERRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Cdd:COG2901   44 EKPLLETVLEHTRGNQSRAAEMLGINRNTLRKKLKQYGLL 83
PRK13856 PRK13856
two-component response regulator VirG; Provisional
7-124 8.83e-07

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 49.81  E-value: 8.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMrAQHPRVPIILMTAYA 86
Cdd:PRK13856   4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSL-ATKSDVPIIIISGDR 82
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 501080907  87 EVET-AVEALRSGAFDYVIKPFDLDELNLLIQRALQLQA 124
Cdd:PRK13856  83 LEEAdKVVALELGATDFIAKPFGTREFLARIRVALRVRP 121
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
5-105 2.85e-06

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 48.48  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   5 YRILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRvPIILMTA 84
Cdd:PRK10701   2 NKIVFVEDDAEVGSLIAAYLAKHDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQG-PIVLLTS 80
                         90       100
                 ....*....|....*....|.
gi 501080907  85 YAEVETAVEALRSGAFDYVIK 105
Cdd:PRK10701  81 LDSDMNHILALEMGACDYILK 101
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
164-299 8.87e-06

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 47.47  E-value: 8.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 164 LSQANVLISGESGTGKELIARAIhynSRRANGPFIKINCAalpESLLESELFGHE-----KGAFtgaQTRRQGLFerahQ 238
Cdd:COG0714   29 LAGGHLLLEGVPGVGKTTLAKAL---ARALGLPFIRIQFT---PDLLPSDILGTYiydqqTGEF---EFRPGPLF----A 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501080907 239 GTLLLDEIGEMPLVLQAKLLRILQEREFErIGGhQTIQVDIR-IVAATnRNLQEMvkEGTFR 299
Cdd:COG0714   96 NVLLADEINRAPPKTQSALLEAMEERQVT-IPG-GTYKLPEPfLVIAT-QNPIEQ--EGTYP 152
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
169-287 9.29e-06

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 44.89  E-value: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  169 VLISGESGTGKELIARAIhynSRRANGPFIKINCaalpeslleSELFGHEKGAfTGAQTRrqGLFERAHQGT---LLLDE 245
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAV---AKELGAPFIEISG---------SELVSKYVGE-SEKRLR--ELFEAAKKLApcvIFIDE 65
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 501080907  246 I-----------GEMPLVLQAKLLRILQereferigGHQTIQVDIRIVAATNR 287
Cdd:pfam00004  66 IdalagsrgsggDSESRRVVNQLLTELD--------GFTSSNSKVIVIAATNR 110
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
7-112 1.13e-05

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


Pssm-ID: 381149 [Multi-domain]  Cd Length: 110  Bit Score: 44.39  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYA 86
Cdd:cd19922    1 ILLLEKERNLAHFLSLELQKEGYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAEKLSRIKPASVIIVLDHWE 80
                         90       100
                 ....*....|....*....|....*.
gi 501080907  87 EVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd19922   81 DLQEELEEVQRFAVSYVVKPVLISNL 106
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
168-287 1.17e-05

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: 44.98  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  168 NVLISGESGTGKELIARaiHYNSRRANGPFIKINCaalPESLLESELFGHEKGAfTGAQTRRQGLFERAHQ--GTLLLDE 245
Cdd:pfam07728   1 GVLLVGPPGTGKTELAE--RLAAALSNRPVFYVQL---TRDTTEEDLFGRRNID-PGGASWVDGPLVRAARegEIAVLDE 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 501080907  246 IGEMPLVLQAKLLRILQEREFERIGGHQTIQV---DIRIVAATNR 287
Cdd:pfam07728  75 INRANPDVLNSLLSLLDERRLLLPDGGELVKAapdGFRLIATMNP 119
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
6-121 2.08e-05

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


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 43.78  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHE-TQCASNGQTALQHFADAPPDVVLMDIRMPE-MNGIEALKVMRAQHpRVPIILMT 83
Cdd:cd17540    2 RVLIIEDEPLIAMDLEQIVEDLGHQvVGIARTRDEAVALARRERPDLILADIQLADgSSGIDAVNEILTTH-DVPVIFVT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 501080907  84 AYAEvetaveALRSGAF---DYVI-KPFDLDELNLLIQRALQ 121
Cdd:cd17540   81 AYPE------RLLTGERpepTFLItKPFDPEMVKAAISQALF 116
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
169-345 4.13e-05

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 45.38  E-value: 4.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 169 VLISGESGTGKELIARAIhynSRRANGPFIKINcaaLPESLleSELFGhekgafTGAQTRRQgLFERAHQGT---LLLDE 245
Cdd:COG1222  115 VLLYGPPGTGKTLLAKAV---AGELGAPFIRVR---GSELV--SKYIG------EGARNVRE-VFELAREKApsiIFIDE 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 246 I-------------GEM-PLVLQakllrILQE-REFERIGghqtiqvDIRIVAATNRnlQEMVKEGTFREDLFYRlnVIH 310
Cdd:COG1222  180 IdaiaarrtddgtsGEVqRTVNQ-----LLAElDGFESRG-------DVLIIAATNR--PDLLDPALLRPGRFDR--VIE 243
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 501080907 311 LTLPPLRERREdipLLANHfLQKFSSENQRDIIEI 345
Cdd:COG1222  244 VPLPDEEAREE---ILKIH-LRDMPLADDVDLDKL 274
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
168-287 4.65e-05

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 43.43  E-value: 4.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 168 NVLISGESGTGKELIARAIhynSRRANGPFIKINCaalpeslleSELFGHEKGaFTGAQTRRqgLFERAHQ---GTLLLD 244
Cdd:cd19481   28 GILLYGPPGTGKTLLAKAL---AGELGLPLIVVKL---------SSLLSKYVG-ESEKNLRK--IFERARRlapCILFID 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501080907 245 EI---------GEMPLVLQAKLLRILQEreferIGGhQTIQVDIRIVAATNR 287
Cdd:cd19481   93 EIdaigrkrdsSGESGELRRVLNQLLTE-----LDG-VNSRSKVLVIAATNR 138
fis PRK00430
DNA-binding transcriptional regulator Fis;
424-456 5.95e-05

DNA-binding transcriptional regulator Fis;


Pssm-ID: 179020 [Multi-domain]  Cd Length: 95  Bit Score: 41.97  E-value: 5.95e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 501080907 424 EVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
Cdd:PRK00430  62 MVMQYTRGNQTRAALMLGINRGTLRKKLKKYGM 94
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
2-112 6.04e-05

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 44.07  E-value: 6.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   2 KTRYRILIVDDEDNVRR----MLAT--AFSLQGHetqcASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHP 75
Cdd:PRK10403   4 ATPFQVLIVDDHPLMRRgvrqLLELdpGFEVVAE----AGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGV 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 501080907  76 RVPIILMTAYAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:PRK10403  80 TAQIIILTVSDASSDVFALIDAGADGYLLKDSDPEVL 116
PRK13435 PRK13435
response regulator; Provisional
6-120 9.31e-05

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 42.35  E-value: 9.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDE----DNVRRMLATAfslqGHETQ-CASNGQTALQHFADAPPDVVLMDIRMpeMNGIEALKVMR--AQHPRVP 78
Cdd:PRK13435   7 KVLIVEDEaliaLELEKLVEEA----GHEVVgIAMSSEQAIALGRRRQPDVALVDVHL--ADGPTGVEVARrlSADGGVE 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 501080907  79 IILMTAYAEVetaVEALRSGAFDYVIKPFDLDelnlLIQRAL 120
Cdd:PRK13435  81 VVFMTGNPER---VPHDFAGALGVIAKPYSPR----GVARAL 115
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
7-112 1.06e-04

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 41.92  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFSlQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRA-QHPR-VPIILMTA 84
Cdd:cd17539    1 VLLVDDRPSSAERIAAMLS-SEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSlERTRqLPILAVAD 79
                         90       100
                 ....*....|....*....|....*...
gi 501080907  85 YAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17539   80 PGDRGRLIRALEIGVNDYLVRPIDPNEL 107
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
35-119 1.15e-04

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 43.35  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907  35 SNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYAEVETAVEALRSGAFDYVIKPFDLDELNL 114
Cdd:PRK09958  32 TEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSAKNDHFYGKHCADAGANGFVSKKEGMNNIIA 111

                 ....*
gi 501080907 115 LIQRA 119
Cdd:PRK09958 112 AIEAA 116
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
169-386 1.60e-04

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 43.75  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 169 VLISGESGTGKELIARAIhynSRRANGPFIKINCAAlpeslLESELFGHekgafTGAQTRRqgLFERAHQGT---LLLDE 245
Cdd:COG0464  194 LLLYGPPGTGKTLLARAL---AGELGLPLIEVDLSD-----LVSKYVGE-----TEKNLRE--VFDKARGLApcvLFIDE 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907 246 I--------GEMPLVLQ---AKLLRILQEREFERIgghqtiqvdirIVAATNRnlQEMVKEGTFRedlfyRLN-VIHLTL 313
Cdd:COG0464  259 AdalagkrgEVGDGVGRrvvNTLLTEMEELRSDVV-----------VIAATNR--PDLLDPALLR-----RFDeIIFFPL 320
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501080907 314 PPLRERREdipLLANHFLQKFSSEnqrdiiEIDPSAMSLLTAWpwpGNIRELSNVIERAV---VMNTGAVIFAEDL 386
Cdd:COG0464  321 PDAEERLE---IFRIHLRKRPLDE------DVDLEELAEATEG---LSGADIRNVVRRAAlqaLRLGREPVTTEDL 384
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
7-112 1.98e-04

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 40.71  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRML-ATAFSLQGHETQCASNGQTALQHFADAPPDVVLMDIRMPE-MNG---IEALKVMRAQHPRVPIIL 81
Cdd:cd17589    1 FLIVDDQPTFRSMLkSMLRSLGVTRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGqqlLEELRHKKLISPSTVFIM 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 501080907  82 MTAYAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17589   81 VTGESSRAMVLSALELEPDDYLLKPFTVSEL 111
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
8-112 3.21e-04

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 41.79  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   8 LIVDDEDNVRRMLATAFSLQGHETQC---ASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTA 84
Cdd:PRK09935   6 VIIMDTHPIIRMSIEVLLQKNSELQIvlkTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLFLSS 85
                         90       100
                 ....*....|....*....|....*...
gi 501080907  85 YAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:PRK09935  86 KSECFYAGRAIQAGANGFVSKCNDQNDI 113
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
50-112 5.13e-04

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AgrA-like group of LytTR/AlgR family response regulators are Staphylococcus aureus accessory gene regulator protein A (AgrA) and Streptococcus pneumoniae response regulator ComE, which are members of two-component regulatory systems. AgrA is a global regulator that controls the synthesis of virulence factors and other exoproteins. ComE is part of the ComD-ComE system that is part of a quorum-sensing signaling pathway that controls the development of competence, a physiological state required for genetic transformation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381088 [Multi-domain]  Cd Length: 131  Bit Score: 39.91  E-value: 5.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501080907  50 DVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTAYAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:cd17533   55 YFLDIDIKMEEKNGLEVAQKIRKYDPYAIIIFVTTHSEFAPLTFEYKVAALDFILKPLKLEEF 117
PRK09191 PRK09191
two-component response regulator; Provisional
6-120 6.01e-04

two-component response regulator; Provisional


Pssm-ID: 236402 [Multi-domain]  Cd Length: 261  Bit Score: 41.37  E-value: 6.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDE--------DNVRRMlatafslqGHE-TQCASNGQTALQHFADAPPDVVLMDIRM-PEMNGIEALKVMRAQHP 75
Cdd:PRK09191 139 RVLIIEDEpiiamdleQLVESL--------GHRvTGIARTRAEAVALAKKTRPGLILADIQLaDGSSGIDAVNDILKTFD 210
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501080907  76 rVPIILMTAYAE-------VETAvealrsgafdYVI-KPFDLDELNLLIQRAL 120
Cdd:PRK09191 211 -VPVIFITAFPErlltgerPEPA----------FLItKPFQPDTVKAAISQAL 252
PRK01905 PRK01905
Fis family transcriptional regulator;
418-456 6.76e-04

Fis family transcriptional regulator;


Pssm-ID: 179348 [Multi-domain]  Cd Length: 77  Bit Score: 38.25  E-value: 6.76e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 501080907 418 ERRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGI 456
Cdd:PRK01905  38 EKPLLEVVMEQAGGNQSLAAEYLGINRNTLRKKLQQHGL 76
pleD PRK09581
response regulator PleD; Reviewed
6-112 9.55e-04

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 41.42  E-value: 9.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDED----NVRRMLAtafslQGHETQCASNGQTALQHFADAPPDVVLMDIRMPEMNGIEALKVMRAQHP--RVPI 79
Cdd:PRK09581 157 RILLVDDDVsqaeRIANILK-----EEFRVVVVSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERtrYVPI 231
                         90       100       110
                 ....*....|....*....|....*....|...
gi 501080907  80 ILMTAYAEVETAVEALRSGAFDYVIKPFDLDEL 112
Cdd:PRK09581 232 LLLVDEDDDPRLVKALELGVNDYLMRPIDKNEL 264
REC_PFxFATGY cd17586
phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response ...
7-120 1.15e-03

phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response regulators; This subfamily is composed of stand-alone response regulators (RRs) containing the PFxFATG[G/Y] motif; RRs with such a motif are also called ''FAT GUY'' response regulators. Included in this subfamily are Sphingomonas melonis SdrG, Sinorhizobium meliloti Sma0114, and Erythrobacter litoralis EL_LovR. SdrG is involved in the control of the general stress response. Sma0114 is part of the Sma0113/Sma0114 two-component system (TCS) that is involved in catabolite repression and polyhydroxy butyrate synthesis. EL_LovR is involved in a light-regulated TCS. PFxFATG[G/Y] RRs are typically associated with histidine-tryptophan-glutamate (HWE) histidine kinases that constitute a subclass of the larger histidine kinase superfamily characterized by an altered ATP binding site, which lacks the F-box that is normally an integral component of the ATP lid. The PFxFATG[G/Y] motif is involved in conformational changes after phosphorylation that results in the activation of the RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381122 [Multi-domain]  Cd Length: 111  Bit Score: 38.60  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   7 ILIVDDEDNVRRMLATAFS-LQGHETQCASNGQTALQHFADAPPDVVLMDIRM-PEMNGIEALKVMRAQhprVPIILMTA 84
Cdd:cd17586    1 VLVLEDEPLIAMNLEDALEdLGGKEVVTAATCAEALRSLADGPIDIAILDVNLgGETSIPVADALKRRA---IPFIFATG 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 501080907  85 YAevETAVEALRSGAFDYVIKPFDLDELNLLIQRAL 120
Cdd:cd17586   78 YG--DSHGIDSRLIDVPVLRKPFDADSALAALAMLL 111
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
6-123 2.33e-03

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 40.66  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501080907   6 RILIVDDEDNVRRMLATAFSLQGHETQCASNGQTALQHFA-DAPPDVVLMDIRMPEMNGIEALKVMRAQHPRVPIILMTA 84
Cdd:PRK11466 683 RLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQnSEPFAAALVDFDLPDYDGITLARQLAQQYPSLVLIGFSA 762
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 501080907  85 YAEVETAVEALRSGAFDYVIKPFDLDELNLLIQRALQLQ 123
Cdd:PRK11466 763 HVIDETLRQRTSSLFRGIIPKPVPREVLGQLLAHYLQLQ 801
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
50-106 7.76e-03

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 36.58  E-value: 7.76e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 501080907  50 DVVLMDIRMPEMNGIEALKVMRAQHP--RVPIILMTAYAEVETAVEALRSGAFDYVIKP 106
Cdd:cd17581   55 NMIITDYCMPGMTGYDLLKKVKESSAlkEIPVVIMSSENIPTRISRCLEEGAEDFLLKP 113
 
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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