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Conserved domains on  [gi|1589195055|gb|TCU58229|]
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sigma-54 dependent transcriptional regulator of gfr operon [Longicatena caecimuris]

Protein Classification

AAA and PRD domain-containing protein( domain architecture ID 13383482)

AAA and PRD domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PspF super family cl34190
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
34-856 1.48e-156

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


The actual alignment was detected with superfamily member COG1221:

Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 482.30  E-value: 1.48e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055  34 REKLQETLQVECEQLEkdlhwQEERLETLTSSFLSAQFACSRNLISHYMSEFQQKGLVIKTNTRPVYFFWRKSLENRFGV 113
Cdd:COG1221     4 KEKILNYLKELTKNLS-----LEKKSEGFTAEEIAEKLGISRNNVSHELNELVKEGKLIKINGRPVLFLDKEAFEEQFGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 114 ILKAELYETLEDLKNILEKKQQHAFHNLIGANDSLSYVVEQCKAAISYPEHGLPILLQGPTGTGKSLIAQLMYQYGVEME 193
Cdd:COG1221    79 KLKSEYSFVELLAEKENNEEEEDPFDNLIGANGSLKNAIEQAKAAILYPPKGLHTLILGPTGVGKSFFAELMYEYAIEIG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 194 ILSKDSRFMTMNCSEYANNPEMLMTNLFGYKKGSYTGAEKDTQGLLALADGGILFMDEVHGLKPECQEKIFLFMDKGIYH 273
Cdd:COG1221   159 VLPEDAPFVVFNCADYANNPQLLMSQLFGYVKGAFTGADKDKEGLIEKADGGILFLDEVHRLPPEGQEMLFTFMDKGIYR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 274 MVGDNDTWYVSNARLIFATTEQPDEVLLKTLLRRIPLIVKVPSLAERPLQEKRELLQFLIQEEEKHIQRKISMSDLVFRT 353
Cdd:COG1221   239 RLGETEKTRKANVRIIFATTEDPESSLLKTFLRRIPMVIKLPSLEERSLEERLELIKHFFKEEAKRLNKPIKVSKEVLKA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 354 LERHTFTGNIGELKNVIRASVAKAFLRN-QKDMDDVSLHIYDLSSDLLESTGKDVT-------LYDYDDRAMI--HSEDM 423
Cdd:COG1221   319 LLLYDCPGNIGQLKSDIQLACAKAFLNYiTNKKEEIEITLSDLPENVKKGLLKLKEnreeldkLSEYLEEYLIisPDTEK 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 424 FLSIHKDSRLYNFNAY--LIHKFHTLHAY---EKDLNayldsccLKLEQYIDSLFTEHTYHSPKLDMINHLLTNIMNIVI 498
Cdd:COG1221   399 KLISEEDEYELPYNFYeiIEDKYEELKSEglsEEEIN-------KIISKDIESYFKKLIFKLDKSNISEELLLIVVDEVI 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 499 hKYDLEKFSNNEISMIVHFLNDYMQSLSSINQLKIQNRKEAEE----LQNRIHNEYTNEYNVIGDIWQLISDALSFTPGP 574
Cdd:COG1221   472 -VNVVEIFEEAEKKLLRYNSSNLFIALSLHLLSTLLRIKKGKKiinpQLNEIKKKYYEEFILAAEAIKIIEEELKILIPD 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 575 FGYLDLFLFFRYFNREMVASPIP---AVIIAHGYAIASGIAEVANQLLKQRIFDAIDMPIESDFNDTVKKLGEYIKGKEN 651
Cdd:COG1221   551 EEEGFILLLLIELKEEKSLSENVivvVVIAHGGAAASSSMAVVNLLLLEVAVAAIDDPPLEVVDVLIEEKTIVVIINKGK 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 652 YNEVIVMVDMGSLEAIHQKMEGMKRMDIGIINNVTT-----KLALDIGSMILEEMPIQEILKQASHRNQYRYEFVKNRKK 726
Cdd:COG1221   631 GGLLLLLDDGGSLFGIIIIEEEGIIIVTVVIVSTTTvleaaARKKLLELDLDEIIVLEELLKNPLESKKIKISTSKKKKI 710
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 727 QDAILAVCETGIGTAEKISKLMEDSLPKTvsIAMIPYDYDSLVKSGTTSLVFEKYNVLFTVGTKDPKIFDVPFISLEEMI 806
Cdd:COG1221   711 IVTTIAITTGEAGGILILILIIELLDKDL--ILIIIEILLIIIKEEILEKIIEEKKEVIIIVIISIIPLIIPPIILLLAL 788
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|
gi 1589195055 807 EQKSVEKTNSVfesIMRPDQIETFNENMIKNFSMDNLLSYLTILDSDKII 856
Cdd:COG1221   789 KLIILIEILVL---LEILIDKEKIENIIKELLSLLNIIIVLLIIDILILI 835
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
860-943 1.28e-11

PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory domain found in bacterial transcriptional antiterminator such as BglG, SacY and LicT, as well as in activators such as MtlR and LevR. The PRD is phosphorylated on one or two conserved histidine residues. PRD-containing proteins are involved in the regulation of catabolic operons in Gram+ and Gram- bacteria and are often characterized by a short N-terminal effector domain that binds to either RNA (CAT-RBD for antiterminators pfam03123) or DNA (for activators), and a duplicated PRD module which is phosphorylated by the sugar phosphotransferase system (PTS) in response to the availability of carbon source. The phosphorylations modify the conformation and stability of the dimeric proteins and thereby the RNA- or DNA-binding activity of the effector domain. The structure of the LicT PRD domains has been solved in both the active (pdb:1h99) and inactive state (pdb:1tlv), revealing massive structural rearrangements upon activation.


:

Pssm-ID: 459973 [Multi-domain]  Cd Length: 90  Bit Score: 61.50  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 860 EKIIKTIQKELHMKL-SSSVILGLYIHISCLIERLIINKNVTKFEHLETFEKTQTEFiRIVKKAFHDVEQHYNVKIPVSE 938
Cdd:pfam00874   1 EEIIELIEKKLGITFdDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEF-EIAKKILEILEEELGIELPEDE 79

                  ....*
gi 1589195055 939 IGYIY 943
Cdd:pfam00874  80 IGYIA 84
 
Name Accession Description Interval E-value
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
34-856 1.48e-156

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: 482.30  E-value: 1.48e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055  34 REKLQETLQVECEQLEkdlhwQEERLETLTSSFLSAQFACSRNLISHYMSEFQQKGLVIKTNTRPVYFFWRKSLENRFGV 113
Cdd:COG1221     4 KEKILNYLKELTKNLS-----LEKKSEGFTAEEIAEKLGISRNNVSHELNELVKEGKLIKINGRPVLFLDKEAFEEQFGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 114 ILKAELYETLEDLKNILEKKQQHAFHNLIGANDSLSYVVEQCKAAISYPEHGLPILLQGPTGTGKSLIAQLMYQYGVEME 193
Cdd:COG1221    79 KLKSEYSFVELLAEKENNEEEEDPFDNLIGANGSLKNAIEQAKAAILYPPKGLHTLILGPTGVGKSFFAELMYEYAIEIG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 194 ILSKDSRFMTMNCSEYANNPEMLMTNLFGYKKGSYTGAEKDTQGLLALADGGILFMDEVHGLKPECQEKIFLFMDKGIYH 273
Cdd:COG1221   159 VLPEDAPFVVFNCADYANNPQLLMSQLFGYVKGAFTGADKDKEGLIEKADGGILFLDEVHRLPPEGQEMLFTFMDKGIYR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 274 MVGDNDTWYVSNARLIFATTEQPDEVLLKTLLRRIPLIVKVPSLAERPLQEKRELLQFLIQEEEKHIQRKISMSDLVFRT 353
Cdd:COG1221   239 RLGETEKTRKANVRIIFATTEDPESSLLKTFLRRIPMVIKLPSLEERSLEERLELIKHFFKEEAKRLNKPIKVSKEVLKA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 354 LERHTFTGNIGELKNVIRASVAKAFLRN-QKDMDDVSLHIYDLSSDLLESTGKDVT-------LYDYDDRAMI--HSEDM 423
Cdd:COG1221   319 LLLYDCPGNIGQLKSDIQLACAKAFLNYiTNKKEEIEITLSDLPENVKKGLLKLKEnreeldkLSEYLEEYLIisPDTEK 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 424 FLSIHKDSRLYNFNAY--LIHKFHTLHAY---EKDLNayldsccLKLEQYIDSLFTEHTYHSPKLDMINHLLTNIMNIVI 498
Cdd:COG1221   399 KLISEEDEYELPYNFYeiIEDKYEELKSEglsEEEIN-------KIISKDIESYFKKLIFKLDKSNISEELLLIVVDEVI 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 499 hKYDLEKFSNNEISMIVHFLNDYMQSLSSINQLKIQNRKEAEE----LQNRIHNEYTNEYNVIGDIWQLISDALSFTPGP 574
Cdd:COG1221   472 -VNVVEIFEEAEKKLLRYNSSNLFIALSLHLLSTLLRIKKGKKiinpQLNEIKKKYYEEFILAAEAIKIIEEELKILIPD 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 575 FGYLDLFLFFRYFNREMVASPIP---AVIIAHGYAIASGIAEVANQLLKQRIFDAIDMPIESDFNDTVKKLGEYIKGKEN 651
Cdd:COG1221   551 EEEGFILLLLIELKEEKSLSENVivvVVIAHGGAAASSSMAVVNLLLLEVAVAAIDDPPLEVVDVLIEEKTIVVIINKGK 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 652 YNEVIVMVDMGSLEAIHQKMEGMKRMDIGIINNVTT-----KLALDIGSMILEEMPIQEILKQASHRNQYRYEFVKNRKK 726
Cdd:COG1221   631 GGLLLLLDDGGSLFGIIIIEEEGIIIVTVVIVSTTTvleaaARKKLLELDLDEIIVLEELLKNPLESKKIKISTSKKKKI 710
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 727 QDAILAVCETGIGTAEKISKLMEDSLPKTvsIAMIPYDYDSLVKSGTTSLVFEKYNVLFTVGTKDPKIFDVPFISLEEMI 806
Cdd:COG1221   711 IVTTIAITTGEAGGILILILIIELLDKDL--ILIIIEILLIIIKEEILEKIIEEKKEVIIIVIISIIPLIIPPIILLLAL 788
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|
gi 1589195055 807 EQKSVEKTNSVfesIMRPDQIETFNENMIKNFSMDNLLSYLTILDSDKII 856
Cdd:COG1221   789 KLIILIEILVL---LEILIDKEKIENIIKELLSLLNIIIVLLIIDILILI 835
Sigma54_activat pfam00158
Sigma-54 interaction domain;
141-307 1.16e-43

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 156.02  E-value: 1.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 141 LIGANDSLSYVVEQCKAAISYPehgLPILLQGPTGTGKSLIAQLMYQYGVEmeilsKDSRFMTMNCSeyANNPEMLMTNL 220
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTD---APVLITGESGTGKELFARAIHQLSPR-----ADGPFVAVNCA--AIPEELLESEL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 221 FGYKKGSYTGAEKDTQGLLALADGGILFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVsNARLIFATTEQPDEVL 300
Cdd:pfam00158  71 FGHEKGAFTGADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKV-DVRIIAATNRDLEEAV 149

                  ....*..
gi 1589195055 301 LKTLLRR 307
Cdd:pfam00158 150 AEGRFRE 156
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
140-374 1.71e-21

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 96.66  E-value: 1.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 140 NLIGANDSLSYVVEQCKAAISYPEhglPILLQGPTGTGKSLIAQ-LMYqygvemeiLSK--DSRFMTMNCSeyANNPEML 216
Cdd:PRK11608    7 NLLGEANSFLEVLEQVSRLAPLDK---PVLIIGERGTGKELIASrLHY--------LSSrwQGPFISLNCA--ALNENLL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 217 MTNLFGYKKGSYTGAEKDTQGLLALADGGILFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVsNARLIFATTEQ- 295
Cdd:PRK11608   74 DSELFGHEAGAFTGAQKRHPGRFERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQV-NVRLVCATNADl 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 296 PDEVLLKT----LLRRIPL-IVKVPSLAERplQEKRELL--QFLIQeeekhIQRKISM------SDLVFRTLERHTFTGN 362
Cdd:PRK11608  153 PAMVAEGKfradLLDRLAFdVVQLPPLRER--QSDIMLMaeHFAIQ-----MCRELGLplfpgfTERARETLLNYRWPGN 225
                         250
                  ....*....|..
gi 1589195055 363 IGELKNVIRASV 374
Cdd:PRK11608  226 IRELKNVVERSV 237
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
168-374 6.77e-21

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: 96.74  E-value: 6.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 168 ILLQGPTGTGKSLIAQLMYQYGvemeiLSKDSRFMTMNCseyANNPEMLM-TNLFGYKKGSYTGAEKDTQGLLALADGGI 246
Cdd:TIGR02915 165 VLLLGESGTGKEVLARALHQLS-----DRKDKRFVAINC---AAIPENLLeSELFGYEKGAFTGAVKQTLGKIEYAHGGT 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 247 LFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVsNARLIFATTEQPDEVLLKTLLR-----RIPLI-VKVPSLAER 320
Cdd:TIGR02915 237 LFLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPV-DVRIVCATNQDLKRMIAEGTFRedlfyRIAEIsITIPPLRSR 315
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1589195055 321 PlqEKRELLQ--FLIQEEEKHIQRKISMSDLVFRTLERHTFTGNIGELKNVIRASV 374
Cdd:TIGR02915 316 D--GDAVLLAnaFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAV 369
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
151-316 2.10e-15

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: 74.49  E-value: 2.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 151 VVEQCKAAISYPeHGLPILLQGPTGTGKSLIAQLMYQygvemEILSKDSRFMTMNCSEYANNPEMLmtNLFGYkkgsytG 230
Cdd:cd00009     6 AIEALREALELP-PPKNLLLYGPPGTGKTTLARAIAN-----ELFRPGAPFLYLNASDLLEGLVVA--ELFGH------F 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 231 AEKDTQGLLALADGGILFMDEVHGLKPECQEKIFLFMDKGIYHMVGdndtwyVSNARLIFATTEQPDEVLLKTLLRRIPL 310
Cdd:cd00009    72 LVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRID------RENVRVIGATNRPLLGDLDRALYDRLDI 145

                  ....*.
gi 1589195055 311 IVKVPS 316
Cdd:cd00009   146 RIVIPL 151
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
860-943 1.28e-11

PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory domain found in bacterial transcriptional antiterminator such as BglG, SacY and LicT, as well as in activators such as MtlR and LevR. The PRD is phosphorylated on one or two conserved histidine residues. PRD-containing proteins are involved in the regulation of catabolic operons in Gram+ and Gram- bacteria and are often characterized by a short N-terminal effector domain that binds to either RNA (CAT-RBD for antiterminators pfam03123) or DNA (for activators), and a duplicated PRD module which is phosphorylated by the sugar phosphotransferase system (PTS) in response to the availability of carbon source. The phosphorylations modify the conformation and stability of the dimeric proteins and thereby the RNA- or DNA-binding activity of the effector domain. The structure of the LicT PRD domains has been solved in both the active (pdb:1h99) and inactive state (pdb:1tlv), revealing massive structural rearrangements upon activation.


Pssm-ID: 459973 [Multi-domain]  Cd Length: 90  Bit Score: 61.50  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 860 EKIIKTIQKELHMKL-SSSVILGLYIHISCLIERLIINKNVTKFEHLETFEKTQTEFiRIVKKAFHDVEQHYNVKIPVSE 938
Cdd:pfam00874   1 EEIIELIEKKLGITFdDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEF-EIAKKILEILEEELGIELPEDE 79

                  ....*
gi 1589195055 939 IGYIY 943
Cdd:pfam00874  80 IGYIA 84
BglG COG3711
Transcriptional antiterminator [Transcription];
833-943 4.30e-10

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 63.73  E-value: 4.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 833 NMIKNFSMDNLLSYLTILD--SDKIIDSVEKIIKTIQKELHMKLSSSVILGLYIHISCLIERLIINKNVTKFEHLETFEK 910
Cdd:COG3711   154 ELLSELLSENDLLSLLLLKliPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWEIK 233
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1589195055 911 TQTEFiRIVKKAFHDVEQHYNVKIPVSEIGYIY 943
Cdd:COG3711   234 KPKEY-EIAKEILKLIEERLGISLPEDEIGYIA 265
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
164-308 5.47e-08

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 53.15  E-value: 5.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055  164 HGLPILLQGPTGTGKSLIAQLMYQygvemEILSKDSRFMTMNCSEYANNPEMLMTNLFGYKKGSYTGAEKDTQGLLALA- 242
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAR-----ELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALAr 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1589195055  243 --DGGILFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTwyvsNARLIFATteQPDEVLLKTLLRRI 308
Cdd:smart00382  76 klKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK----NLTVILTT--NDEKDLGPALLRRR 137
 
Name Accession Description Interval E-value
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
34-856 1.48e-156

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: 482.30  E-value: 1.48e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055  34 REKLQETLQVECEQLEkdlhwQEERLETLTSSFLSAQFACSRNLISHYMSEFQQKGLVIKTNTRPVYFFWRKSLENRFGV 113
Cdd:COG1221     4 KEKILNYLKELTKNLS-----LEKKSEGFTAEEIAEKLGISRNNVSHELNELVKEGKLIKINGRPVLFLDKEAFEEQFGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 114 ILKAELYETLEDLKNILEKKQQHAFHNLIGANDSLSYVVEQCKAAISYPEHGLPILLQGPTGTGKSLIAQLMYQYGVEME 193
Cdd:COG1221    79 KLKSEYSFVELLAEKENNEEEEDPFDNLIGANGSLKNAIEQAKAAILYPPKGLHTLILGPTGVGKSFFAELMYEYAIEIG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 194 ILSKDSRFMTMNCSEYANNPEMLMTNLFGYKKGSYTGAEKDTQGLLALADGGILFMDEVHGLKPECQEKIFLFMDKGIYH 273
Cdd:COG1221   159 VLPEDAPFVVFNCADYANNPQLLMSQLFGYVKGAFTGADKDKEGLIEKADGGILFLDEVHRLPPEGQEMLFTFMDKGIYR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 274 MVGDNDTWYVSNARLIFATTEQPDEVLLKTLLRRIPLIVKVPSLAERPLQEKRELLQFLIQEEEKHIQRKISMSDLVFRT 353
Cdd:COG1221   239 RLGETEKTRKANVRIIFATTEDPESSLLKTFLRRIPMVIKLPSLEERSLEERLELIKHFFKEEAKRLNKPIKVSKEVLKA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 354 LERHTFTGNIGELKNVIRASVAKAFLRN-QKDMDDVSLHIYDLSSDLLESTGKDVT-------LYDYDDRAMI--HSEDM 423
Cdd:COG1221   319 LLLYDCPGNIGQLKSDIQLACAKAFLNYiTNKKEEIEITLSDLPENVKKGLLKLKEnreeldkLSEYLEEYLIisPDTEK 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 424 FLSIHKDSRLYNFNAY--LIHKFHTLHAY---EKDLNayldsccLKLEQYIDSLFTEHTYHSPKLDMINHLLTNIMNIVI 498
Cdd:COG1221   399 KLISEEDEYELPYNFYeiIEDKYEELKSEglsEEEIN-------KIISKDIESYFKKLIFKLDKSNISEELLLIVVDEVI 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 499 hKYDLEKFSNNEISMIVHFLNDYMQSLSSINQLKIQNRKEAEE----LQNRIHNEYTNEYNVIGDIWQLISDALSFTPGP 574
Cdd:COG1221   472 -VNVVEIFEEAEKKLLRYNSSNLFIALSLHLLSTLLRIKKGKKiinpQLNEIKKKYYEEFILAAEAIKIIEEELKILIPD 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 575 FGYLDLFLFFRYFNREMVASPIP---AVIIAHGYAIASGIAEVANQLLKQRIFDAIDMPIESDFNDTVKKLGEYIKGKEN 651
Cdd:COG1221   551 EEEGFILLLLIELKEEKSLSENVivvVVIAHGGAAASSSMAVVNLLLLEVAVAAIDDPPLEVVDVLIEEKTIVVIINKGK 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 652 YNEVIVMVDMGSLEAIHQKMEGMKRMDIGIINNVTT-----KLALDIGSMILEEMPIQEILKQASHRNQYRYEFVKNRKK 726
Cdd:COG1221   631 GGLLLLLDDGGSLFGIIIIEEEGIIIVTVVIVSTTTvleaaARKKLLELDLDEIIVLEELLKNPLESKKIKISTSKKKKI 710
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 727 QDAILAVCETGIGTAEKISKLMEDSLPKTvsIAMIPYDYDSLVKSGTTSLVFEKYNVLFTVGTKDPKIFDVPFISLEEMI 806
Cdd:COG1221   711 IVTTIAITTGEAGGILILILIIELLDKDL--ILIIIEILLIIIKEEILEKIIEEKKEVIIIVIISIIPLIIPPIILLLAL 788
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|
gi 1589195055 807 EQKSVEKTNSVfesIMRPDQIETFNENMIKNFSMDNLLSYLTILDSDKII 856
Cdd:COG1221   789 KLIILIEILVL---LEILIDKEKIENIIKELLSLLNIIIVLLIIDILILI 835
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
75-948 8.21e-140

Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 441.09  E-value: 8.21e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055  75 RNLISHYMSEFQQKGLVIKTNTRPVYFFWRKSLENRFGVILKAELYETLEDLKNILEKKQQHAFHNLIGANDSLSYVVEQ 154
Cdd:COG3933    32 LLKESTGLLKLLALLLLLKRLSELLLELKKLKKEKKTLKKERSLLEKKKNKLNLKEEKKEKLDFKALIGLSLSLLSAAAA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 155 CKAAISYPEHGLPILLQGPTGTGKSLIAqlMYQYGVEMEILSKDSRFMTMNCSEYANNPEMLMTNLFGYKKGSYTGAEKD 234
Cdd:COG3933   112 AKAAKPPPPLGLLTLLLGGTGGGKSAFA--GYMYAFAAKIAELAAPFVFFNFANAAYNPNLLLLLLFGLGGGAGGGAGAD 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 235 TQGLLALADGGILFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVSNARLIFATTEQPDEVLLKTLLRRIPLI-VK 313
Cdd:COG3933   190 GGGLGGAAGAGGGLLDLLDELPLEGEEQEELFFLLGKGLFRGEGGESRSRRVRIIRATTETEESLLLTTLTRRIRIIiIL 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 314 VPSLAERPLQEKRELLQFLIQEEEKHIQRKISMSDLVFRTLERHTFT--GNIGELKNVIRASVAKAFLRN-QKDMDDVSL 390
Cdd:COG3933   270 PRLPILERRERERLLLLLFEFEEEEIRIIKILIVLLLALLLLLLYVNnlGQLGLLKLLIKAAAAAALAKAiKEATIILRL 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 391 HIYD---LSSDLLESTGKDVTLYDYDDRAMIHSEDMFLSIHKDSRLYNFNAYLIHKFhtlhAYEKDLNAYLDSCCLKLEQ 467
Cdd:COG3933   350 LSKLlklLLLLLLNERLLLLELKILIEPLDIFFDSSASSDESDESEEDENLYEIIEI----KKKLLLELGIDEEEINIII 425
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 468 YIDSLFTEHTYHspKLDMINHLLTNIMNIVIhkYDLEKFSNNEISMIVHFLNDYMQS----------LSSINQLKiQNRK 537
Cdd:COG3933   426 EIDIDVHLLKFI--YDDNKNFNKEELAKIVD--EDIINVVEEILELAEKKLGRKFSEnfiyalslhlSSFIERIK-EGKE 500
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 538 EAEELQNRIHNEYTNEYNVIGDIWQLISDALSFTPGPF--GYLDLFLffRYFNREMVASPIPAVIIAHGYAIASGIAEVA 615
Cdd:COG3933   501 IINPNLNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDevGFLTLFL--VSLNENNESGKVGVIVLAHGYSTASSMAEVA 578
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 616 NQLLKQRIFDAIDMPIESDFNDTVKKLGEYIKGKENYNEVIVMVDMGSLEAIHQKMEGMKRMDIGIINNVTTKLALDIGS 695
Cdd:COG3933   579 NRLLGTNIFEAIDMPLDMSPEDILEKLKEYVKKIDTGKGVLLLVDMGSLTTFGEIIEEETGIPVKTIDMVSTPLVLEAGR 658
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 696 MILEEMPIQEI---LKQASHRNQYRYEFVKNRKKQDAILAVCETGIGTAEKISKLMEDSLPKTVS-IAMIPYDYDSLVK- 770
Cdd:COG3933   659 KALLGMSLEEIyesLKNFNPYEKIISKNKPEKNKKKAIITTCFTGEGTAVKIKDLLEKSLPEDEDnIEIIPLDYLELEEf 738
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 771 SGTTSLVFEKYNVLFTVGTKDPKIFDVPFISLEEMIEQKSVEKTNSVFESIMRPDQIETFNENMIKNFSMDNLLSYLTIL 850
Cdd:COG3933   739 KEKIDEIFKEYEILAIVGTIDPEIPDIPFISLEDLISGEGIEKLQKLLGGELDAEEIEEINNEIIKNFSLESLIESLTIL 818
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 851 DSDKIIDSVEKIIKTIQKELHMKLSSSVILGLYIHISCLIERLIINKNVTKFEHLETFEKTQTEFIRIVKKAFHDVEQHY 930
Cdd:COG3933   819 NPEKIINELEDFISRLENLLGIKLDNDVKIGLILHIACMIERLVTGEEILTYPNKEEFIQENESEYAVIKEAFSPIEEKY 898
                         890
                  ....*....|....*...
gi 1589195055 931 NVKIPVSEIGYIYECIFQ 948
Cdd:COG3933   899 NIKIPDSEIAYIYDILKN 916
Sigma54_activat pfam00158
Sigma-54 interaction domain;
141-307 1.16e-43

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 156.02  E-value: 1.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 141 LIGANDSLSYVVEQCKAAISYPehgLPILLQGPTGTGKSLIAQLMYQYGVEmeilsKDSRFMTMNCSeyANNPEMLMTNL 220
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTD---APVLITGESGTGKELFARAIHQLSPR-----ADGPFVAVNCA--AIPEELLESEL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 221 FGYKKGSYTGAEKDTQGLLALADGGILFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVsNARLIFATTEQPDEVL 300
Cdd:pfam00158  71 FGHEKGAFTGADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKV-DVRIIAATNRDLEEAV 149

                  ....*..
gi 1589195055 301 LKTLLRR 307
Cdd:pfam00158 150 AEGRFRE 156
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
111-377 4.14e-30

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: 124.31  E-value: 4.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 111 FGVILK----AELYETLED-LKNILEKKQQHAFHNLIGANDSLSYVVEQ-CKAAISypehGLPILLQGPTGTGKSLIAQL 184
Cdd:COG2204    98 FDYLTKpfdlEELLAAVERaLERRRLRRENAEDSGLIGRSPAMQEVRRLiEKVAPS----DATVLITGESGTGKELVARA 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 185 MYQYGvemeiLSKDSRFMTMNCSeyANNPEMLMTNLFGYKKGSYTGAEKDTQGLLALADGGILFMDEVHGLKPECQEKIF 264
Cdd:COG2204   174 IHRLS-----PRADGPFVAVNCA--AIPEELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGEMPLALQAKLL 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 265 LFMDKGIYHMVGDNDTWYVsNARLIFATTEQPDEVLLKTLLR-----RIPLI-VKVPSLAERPlQEKRELLQFLIQEEEK 338
Cdd:COG2204   247 RVLQEREFERVGGNKPIPV-DVRVIAATNRDLEELVEEGRFRedlyyRLNVFpIELPPLRERR-EDIPLLARHFLARFAA 324
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1589195055 339 HIQRKISMSDLVFRTLERHTFTGNIGELKNVIRASVAKA 377
Cdd:COG2204   325 ELGKPVKLSPEALEALLAYDWPGNVRELENVIERAVILA 363
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
136-377 7.34e-29

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 123.47  E-value: 7.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 136 HAFHNLIGANDSLSYVVEQCKAAIsypEHGLPILLQGPTGTGKSLIAQLMYQYGVemeilSKDSRFMTMNCseyANNPEM 215
Cdd:COG3284   318 AALAALAGGDPAMRRALRRARRLA---DRDIPVLILGETGTGKELFARAIHAASP-----RADGPFVAVNC---AAIPEE 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 216 LM-TNLFGYKKGSYTGAEKD-TQGLLALADGGILFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVsNARLIfATT 293
Cdd:COG3284   387 LIeSELFGYEPGAFTGARRKgRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPIPV-DVRLI-AAT 464
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 294 EQPDEVLLKT------LLRRI-PLIVKVPSLAERplQEKRELLQFLIQEEEKHIQRkISMSDLVFRTLERHTFTGNIGEL 366
Cdd:COG3284   465 HRDLRELVAAgrfredLYYRLnGLTLTLPPLRER--EDLPALIEHLLRELAAGRGP-LRLSPEALALLAAYPWPGNVREL 541
                         250
                  ....*....|.
gi 1589195055 367 KNVIRASVAKA 377
Cdd:COG3284   542 RNVLRTALALA 552
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
118-374 6.47e-26

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: 112.17  E-value: 6.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 118 ELYETLEDLKNILEKKQQHAFHNLIGANDSLSYVVEQC-KAAISypehGLPILLQGPTGTGKSLIAQLMYQygvemeiLS 196
Cdd:COG3829   117 RLERKLREEELERGLSAKYTFDDIIGKSPAMKELLELAkRVAKS----DSTVLILGESGTGKELFARAIHN-------AS 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 197 --KDSRFMTMNC---------SEyannpemlmtnLFGYKKGSYTGAEK-DTQGLLALADGGILFMDEVHGLKPECQEKI- 263
Cdd:COG3829   186 prRDGPFVAVNCaaipenlleSE-----------LFGYEKGAFTGAKKgGKPGLFELADGGTLFLDEIGEMPLSLQAKLl 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 264 -FLfMDKGIYHmVGDNDTWYVsNARLIFATTEQPDEVLLKTLLRR--------IPLivKVPSLAERplqekRE----LLQ 330
Cdd:COG3829   255 rVL-QEKEVRR-VGGTKPIPV-DVRIIAATNRDLEEMVEEGRFREdlyyrlnvIPI--HIPPLRER-----KEdiplLAE 324
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1589195055 331 FLIQEEEKHIQRKI-SMSDLVFRTLERHTFTGNIGELKNVI-RASV 374
Cdd:COG3829   325 HFLEKFNKKYGKNIkGISPEALELLLAYDWPGNVRELENVIeRAVV 370
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
140-374 1.71e-21

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 96.66  E-value: 1.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 140 NLIGANDSLSYVVEQCKAAISYPEhglPILLQGPTGTGKSLIAQ-LMYqygvemeiLSK--DSRFMTMNCSeyANNPEML 216
Cdd:PRK11608    7 NLLGEANSFLEVLEQVSRLAPLDK---PVLIIGERGTGKELIASrLHY--------LSSrwQGPFISLNCA--ALNENLL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 217 MTNLFGYKKGSYTGAEKDTQGLLALADGGILFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVsNARLIFATTEQ- 295
Cdd:PRK11608   74 DSELFGHEAGAFTGAQKRHPGRFERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQV-NVRLVCATNADl 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 296 PDEVLLKT----LLRRIPL-IVKVPSLAERplQEKRELL--QFLIQeeekhIQRKISM------SDLVFRTLERHTFTGN 362
Cdd:PRK11608  153 PAMVAEGKfradLLDRLAFdVVQLPPLRER--QSDIMLMaeHFAIQ-----MCRELGLplfpgfTERARETLLNYRWPGN 225
                         250
                  ....*....|..
gi 1589195055 363 IGELKNVIRASV 374
Cdd:PRK11608  226 IRELKNVVERSV 237
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
168-374 6.77e-21

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: 96.74  E-value: 6.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 168 ILLQGPTGTGKSLIAQLMYQYGvemeiLSKDSRFMTMNCseyANNPEMLM-TNLFGYKKGSYTGAEKDTQGLLALADGGI 246
Cdd:TIGR02915 165 VLLLGESGTGKEVLARALHQLS-----DRKDKRFVAINC---AAIPENLLeSELFGYEKGAFTGAVKQTLGKIEYAHGGT 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 247 LFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVsNARLIFATTEQPDEVLLKTLLR-----RIPLI-VKVPSLAER 320
Cdd:TIGR02915 237 LFLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPV-DVRIVCATNQDLKRMIAEGTFRedlfyRIAEIsITIPPLRSR 315
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1589195055 321 PlqEKRELLQ--FLIQEEEKHIQRKISMSDLVFRTLERHTFTGNIGELKNVIRASV 374
Cdd:TIGR02915 316 D--GDAVLLAnaFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKVKRAV 369
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
113-372 3.74e-20

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 95.26  E-value: 3.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 113 VILKAElYETLEDLKNiLEKKQQHAFHNLIGANDSLSYVVEQCK--AAISypehgLPILLQGPTGTGKSLIAQLMYQYGv 190
Cdd:COG3283   180 VTLKSA-ARLGEQLQA-LQVNDDSGFDHIVASSPKMRQVIRQAKkmAMLD-----APLLIQGETGTGKELLARACHLAS- 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 191 emeiLSKDSRFMTMNCseyANNPEMLM-TNLFGYKKGSYTGAEKDTQGLLALADGGILFMDEVHGLKPECQEKIFLFMDK 269
Cdd:COG3283   252 ----PRGDKPFLALNC---AALPDDVAeSELFGYAPGAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQD 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 270 GIYHMVGDNDTWYVsNARLIFATTEQPDEVLLKTLLR-----RIP-LIVKVPSLAER-----PLQEkrellQFLIQEEEK 338
Cdd:COG3283   325 GTFRRVGEEQEVKV-DVRVICATQKDLAELVQEGEFRedlyyRLNvLTLTLPPLRERksdilPLAE-----HFVARFSQQ 398
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1589195055 339 HIQRKISMSDLVFRTLERHTFTGNIGELKNVI-RA 372
Cdd:COG3283   399 LGRPRPRLSPDLVDFLQSYPWPGNVRQLENALyRA 433
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
168-374 1.20e-18

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 89.70  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 168 ILLQGPTGTGKSLIAQLMYQYGVEmeilsKDSRFMTMNCSeyANNPEMLMTNLFGYKKGSYTGAEKDTQGLLALADGGIL 247
Cdd:PRK10365  165 VLIHGDSGTGKELVARAIHASSAR-----SEKPLVTLNCA--ALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTL 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 248 FMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVsNARLIFATTEQ-PDEV----LLKTLLRRIPLI-VKVPSLAERp 321
Cdd:PRK10365  238 FLDEIGDISPMMQVRLLRAIQEREVQRVGSNQTISV-DVRLIAATHRDlAAEVnagrFRQDLYYRLNVVaIEVPSLRQR- 315
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1589195055 322 lQEKRELL--QFLIQEEEKHIQRKISMSDLVFRTLERHTFTGNIGELKNVIRASV 374
Cdd:PRK10365  316 -REDIPLLagHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVERAV 369
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
138-374 7.96e-18

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 88.73  E-value: 7.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 138 FHNLIGANDSLSYVVEQCKAAisyPEHGLPILLQGPTGTGKSLIAQLMYQygvemeiLS--KDSRFMTMNCSeyANNPEM 215
Cdd:PRK15429  375 FGEIIGRSEAMYSVLKQVEMV---AQSDSTVLILGETGTGKELIARAIHN-------LSgrNNRRMVKMNCA--AMPAGL 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 216 LMTNLFGYKKGSYTGAEKDTQGLLALADGGILFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVsNARLIFATTEQ 295
Cdd:PRK15429  443 LESDLFGHERGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQT-DVRLIAATNRD 521
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 296 -----PDEVLLKTLLRRIPLI-VKVPSLAERPlQEKRELLQFLIQEEEKHIQRKI-SMSDLVFRTLERHTFTGNIGELKN 368
Cdd:PRK15429  522 lkkmvADREFRSDLYYRLNVFpIHLPPLRERP-EDIPLLVKAFTFKIARRMGRNIdSIPAETLRTLSNMEWPGNVRELEN 600

                  ....*.
gi 1589195055 369 VIRASV 374
Cdd:PRK15429  601 VIERAV 606
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
168-374 7.78e-17

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 84.51  E-value: 7.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 168 ILLQGPTGTGKSLIAQLMYqYGVEmeilSKDSRFMTMNCseyANNPEMLM-TNLFGYKKGSYTGAEKDTQGLLALADGGI 246
Cdd:PRK11361  169 VLISGESGTGKELIARAIH-YNSR----RAKGPFIKVNC---AALPESLLeSELFGHEKGAFTGAQTLRQGLFERANEGT 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 247 LFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVsNARLIFATTEQPDEVLLKTLLR-----RIPLI-VKVPSLAER 320
Cdd:PRK11361  241 LLLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKV-DIRIIAATNRDLQAMVKEGTFRedlfyRLNVIhLILPPLRDR 319
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1589195055 321 PlQEKRELLQFLIQEEEKHIQRKI-SMSDLVFRTLERHTFTGNIGELKNVI-RASV 374
Cdd:PRK11361  320 R-EDISLLANHFLQKFSSENQRDIiDIDPMAMSLLTAWSWPGNIRELSNVIeRAVV 374
PRK10820 PRK10820
transcriptional regulator TyrR;
136-408 2.31e-16

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 83.20  E-value: 2.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 136 HAFHNLIGANDSLSYVVEQC-KAAIsypeHGLPILLQGPTGTGKSLIAqlmyqYGVEMEILSKDSRFMTMNCseyANNPE 214
Cdd:PRK10820  201 SAFSQIVAVSPKMRQVVEQArKLAM----LDAPLLITGDTGTGKDLLA-----YACHLRSPRGKKPFLALNC---ASIPD 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 215 MLM-TNLFGYKKGSYTGAEKDTQGLLALADGGILFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVsNARLIFATT 293
Cdd:PRK10820  269 DVVeSELFGHAPGAYPNALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHV-DVRVICATQ 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 294 EQPDEVLLKTLLR-----RIP-LIVKVPSLAERPlQEKRELLQFLIQE--EEKHIQR-KISmSDLVfRTLERHTFTGNIG 364
Cdd:PRK10820  348 KNLVELVQKGEFRedlyyRLNvLTLNLPPLRDRP-QDIMPLTELFVARfaDEQGVPRpKLA-ADLN-TVLTRYGWPGNVR 424
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1589195055 365 ELKNVIRASVAK---AFLRNQkdmdDVSLHIYD----LSSDLLESTGKDVT 408
Cdd:PRK10820  425 QLKNAIYRALTQlegYELRPQ----DILLPDYDaavaVGEDAMEGSLDEIT 471
PRK15115 PRK15115
response regulator GlrR; Provisional
168-375 9.71e-16

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 81.04  E-value: 9.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 168 ILLQGPTGTGKSLIAQLMYQYGVEmeilsKDSRFMTMNCSEYannPEMLM-TNLFGYKKGSYTGAEKDTQGLLALADGGI 246
Cdd:PRK15115  160 VLINGQSGTGKEILAQAIHNASPR-----ASKPFIAINCGAL---PEQLLeSELFGHARGAFTGAVSNREGLFQAAEGGT 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 247 LFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVsNARLIFATTEQPDEVLLKTLLR-----RIPLI-VKVPSLAER 320
Cdd:PRK15115  232 LFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDI-DVRIISATHRDLPKAMARGEFRedlyyRLNVVsLKIPALAER 310
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1589195055 321 PlqEKRELL--QFLIQEEEKHIQRKISMSDLVFRTLERHTFTGNIGELKNVIRASVA 375
Cdd:PRK15115  311 T--EDIPLLanHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVA 365
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
151-316 2.10e-15

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: 74.49  E-value: 2.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 151 VVEQCKAAISYPeHGLPILLQGPTGTGKSLIAQLMYQygvemEILSKDSRFMTMNCSEYANNPEMLmtNLFGYkkgsytG 230
Cdd:cd00009     6 AIEALREALELP-PPKNLLLYGPPGTGKTTLARAIAN-----ELFRPGAPFLYLNASDLLEGLVVA--ELFGH------F 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 231 AEKDTQGLLALADGGILFMDEVHGLKPECQEKIFLFMDKGIYHMVGdndtwyVSNARLIFATTEQPDEVLLKTLLRRIPL 310
Cdd:cd00009    72 LVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRID------RENVRVIGATNRPLLGDLDRALYDRLDI 145

                  ....*.
gi 1589195055 311 IVKVPS 316
Cdd:cd00009   146 RIVIPL 151
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
136-420 3.22e-13

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 73.56  E-value: 3.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 136 HAFHNLIGANDSLSYVVEQCKAAIsypEHGLPILLQGPTGTGKSLIAQLMYQygvemEILSKDSRFMTMNCSEYanNPEM 215
Cdd:PRK11388  322 HTFDHMPQDSPQMRRLIHFGRQAA---KSSFPVLLCGEEGVGKALLAQAIHN-----ESERAAGPYIAVNCQLY--PDEA 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 216 LMTNLFGykkGSYTGAEKDTQGLLALADGGILFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVsNARLIFATTEQ 295
Cdd:PRK11388  392 LAEEFLG---SDRTDSENGRLSKFELAHGGTLFLEKVEYLSPELQSALLQVLKTGVITRLDSRRLIPV-DVRVIATTTAD 467
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 296 PDEVLLKTLLRRiPLIVKVPS--LAERPLQEKRELLQFLIQEE----EKHIQRKISMSDLVFRTLERHTFTGNIGELKNV 369
Cdd:PRK11388  468 LAMLVEQNRFSR-QLYYALHAfeITIPPLRMRREDIPALVNNKlrslEKRFSTRLKIDDDALARLVSYRWPGNDFELRSV 546
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1589195055 370 IRasvaKAFL---RNQKDMDDVSLHIYdLSSDLLESTGK----DVTLYDYDDRAMIHS 420
Cdd:PRK11388  547 IE----NLALssdNGRIRLSDLPEHLF-TEQATDDVSATrlstSLSLAELEKEAIINA 599
PTS_IIA_man cd00006
PTS_IIA, PTS system, mannose/sorbose specific IIA subunit. The bacterial phosphoenolpyruvate: ...
598-710 3.36e-13

PTS_IIA, PTS system, mannose/sorbose specific IIA subunit. The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. This family is one of four structurally and functionally distinct group IIA PTS system cytoplasmic enzymes, necessary for the uptake of carbohydrates across the cytoplasmic membrane and their phosphorylation. IIA subunits receive phosphoryl groups from HPr and transfer them to IIB subunits, which in turn phosphorylate the substrate.


Pssm-ID: 237978 [Multi-domain]  Cd Length: 122  Bit Score: 67.25  E-value: 3.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 598 AVIIAHGyAIASGIAEVANQLL-KQRIFDAIDMPIESDFNDTVKKLGEYIKGKENYNEVIVMVDM--GSLEAIHQK-MEG 673
Cdd:cd00006     3 IIIATHG-GFASGLLNSAEMILgEQENVEAIDFPPGESPDDLLEKIKAALAELDSGEGVLILTDLfgGSPNNAAARlSME 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1589195055 674 MKRMDigIINNVTTKLALDIGSMILEEMPIQEILKQA 710
Cdd:cd00006    82 HPPVE--VIAGVNLPMLLEAARARELGLSLDELVENA 116
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
168-408 4.90e-13

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 72.60  E-value: 4.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 168 ILLQGPTGTGKSLIAQLMYQYGVEMEilskdSRFMTMNCSeyANNPEMLMTNLFGYKKGSYTGAEKDTQGLLALADGGIL 247
Cdd:PRK10923  164 VLINGESGTGKELVAHALHRHSPRAK-----APFIALNMA--AIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTL 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 248 FMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVsNARLIFATTEQPDEVLLKTLLR-----RIPLI-VKVPslaerP 321
Cdd:PRK10923  237 FLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKV-DVRIIAATHQNLEQRVQEGKFRedlfhRLNVIrVHLP-----P 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 322 LQEKRE----LLQFLIQEEEKH--IQRKISMSDlVFRTLERHTFTGNIGELKNVIR-ASVAKAflrNQKDMddvslhIYD 394
Cdd:PRK10923  311 LRERREdiprLARHFLQVAARElgVEAKLLHPE-TEAALTRLAWPGNVRQLENTCRwLTVMAA---GQEVL------IQD 380
                         250
                  ....*....|....
gi 1589195055 395 LSSDLLESTGKDVT 408
Cdd:PRK10923  381 LPGELFESTVPEST 394
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
166-398 1.79e-12

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 70.97  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 166 LPILLQGPTGTGKSLIAQLMYQygvemeiLSKDSR--FMTMNCseyANNPEMLM-TNLFGYKKGSYTGAEKDTQGLLALA 242
Cdd:PRK05022  211 LNVLILGETGVGKELVARAIHA-------ASPRADkpLVYLNC---AALPESLAeSELFGHVKGAFTGAISNRSGKFELA 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 243 DGGILFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVsNARLIFATTEQ-PDEVLLKT----LLRRI---PLIvkV 314
Cdd:PRK05022  281 DGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRV-DVRVIAATNRDlREEVRAGRfradLYHRLsvfPLS--V 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 315 PSLAERPlqekRELLQ----FLiqEEekhIQRKISMSDLVF-----RTLERHTFTGNIGELKNVI-RASVaKAFLRNQKd 384
Cdd:PRK05022  358 PPLRERG----DDVLLlagyFL--EQ---NRARLGLRSLRLspaaqAALLAYDWPGNVRELEHVIsRAAL-LARARGAG- 426
                         250
                  ....*....|....
gi 1589195055 385 mDDVSLHIYDLSSD 398
Cdd:PRK05022  427 -RIVTLEAQHLDLP 439
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
149-252 3.52e-12

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 70.13  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 149 SYVVEQCKAAIS-YPEHGLPILLQGPTGTGKSLIAQLMYQYGVEMEILSKDSR---FMTMNCSEYANNpeMLMTNLFGYK 224
Cdd:PRK15424  225 SPQMEQVRQTILlYARSSAAVLIQGETGTGKELAAQAIHREYFARHDARQGKKshpFVAVNCGAIAES--LLEAELFGYE 302
                          90       100
                  ....*....|....*....|....*....
gi 1589195055 225 KGSYTGAEKDTQ-GLLALADGGILFMDEV 252
Cdd:PRK15424  303 EGAFTGSRRGGRaGLFEIAHGGTLFLDEI 331
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
860-943 1.28e-11

PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory domain found in bacterial transcriptional antiterminator such as BglG, SacY and LicT, as well as in activators such as MtlR and LevR. The PRD is phosphorylated on one or two conserved histidine residues. PRD-containing proteins are involved in the regulation of catabolic operons in Gram+ and Gram- bacteria and are often characterized by a short N-terminal effector domain that binds to either RNA (CAT-RBD for antiterminators pfam03123) or DNA (for activators), and a duplicated PRD module which is phosphorylated by the sugar phosphotransferase system (PTS) in response to the availability of carbon source. The phosphorylations modify the conformation and stability of the dimeric proteins and thereby the RNA- or DNA-binding activity of the effector domain. The structure of the LicT PRD domains has been solved in both the active (pdb:1h99) and inactive state (pdb:1tlv), revealing massive structural rearrangements upon activation.


Pssm-ID: 459973 [Multi-domain]  Cd Length: 90  Bit Score: 61.50  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 860 EKIIKTIQKELHMKL-SSSVILGLYIHISCLIERLIINKNVTKFEHLETFEKTQTEFiRIVKKAFHDVEQHYNVKIPVSE 938
Cdd:pfam00874   1 EEIIELIEKKLGITFdDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEF-EIAKKILEILEEELGIELPEDE 79

                  ....*
gi 1589195055 939 IGYIY 943
Cdd:pfam00874  80 IGYIA 84
BglG COG3711
Transcriptional antiterminator [Transcription];
833-943 4.30e-10

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 63.73  E-value: 4.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 833 NMIKNFSMDNLLSYLTILD--SDKIIDSVEKIIKTIQKELHMKLSSSVILGLYIHISCLIERLIINKNVTKFEHLETFEK 910
Cdd:COG3711   154 ELLSELLSENDLLSLLLLKliPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWEIK 233
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1589195055 911 TQTEFiRIVKKAFHDVEQHYNVKIPVSEIGYIY 943
Cdd:COG3711   234 KPKEY-EIAKEILKLIEERLGISLPEDEIGYIA 265
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
164-308 5.47e-08

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 53.15  E-value: 5.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055  164 HGLPILLQGPTGTGKSLIAQLMYQygvemEILSKDSRFMTMNCSEYANNPEMLMTNLFGYKKGSYTGAEKDTQGLLALA- 242
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAR-----ELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALAr 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1589195055  243 --DGGILFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTwyvsNARLIFATteQPDEVLLKTLLRRI 308
Cdd:smart00382  76 klKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK----NLTVILTT--NDEKDLGPALLRRR 137
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
167-307 1.80e-06

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 48.06  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 167 PILLQGPTGTGKSLIAQLMyqygveMEILSKDSRFmTMNCSEYANNPEM-----LMTNLFGYKKGSYTGAEKdtqgllal 241
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERL------AAALSNRPVF-YVQLTRDTTEEDLfgrrnIDPGGASWVDGPLVRAAR-------- 65
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1589195055 242 aDGGILFMDEVHGLKPECQEKIFLFMDKGIYHMvgDNDTWYVS----NARLIFATTEQPDEV--LLKTLLRR 307
Cdd:pfam07728  66 -EGEIAVLDEINRANPDVLNSLLSLLDERRLLL--PDGGELVKaapdGFRLIATMNPLDRGLneLSPALRSR 134
BglG COG3711
Transcriptional antiterminator [Transcription];
845-942 3.77e-06

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 50.63  E-value: 3.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 845 SYLTILDSDKIIDSVEKIIKTIQKELHMKLSSSVIL--GLYIHISCLIERLIINKNVTKfEHLETFEKTQTEFIRIVKKA 922
Cdd:COG3711   277 NELSEIITLEITKLIKEIINIIEEELGIDLDEDSLLyeRLITHLKPAINRLKYGIPIRN-PLLEEIKEKYPEAFELAKKI 355
                          90       100
                  ....*....|....*....|
gi 1589195055 923 FHDVEQHYNVKIPVSEIGYI 942
Cdd:COG3711   356 AKYLEKELGIEIPEDEIGYL 375
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
168-403 4.12e-05

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: 46.76  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 168 ILLQGPTGTGKSLIAQLMYQYGvemeiLSKDSRFMTMNCseyANNPEMLMTNLfgykkgsytgaekdtqgllaladggil 247
Cdd:COG3604   118 VAILGETGTGKELVANAIHELS-----PRADKPFVKVNC---AALPESLLESL--------------------------- 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 248 fmdevhglkpecQEKIFlfmdkgiyHMVGDNDTWYVsNARLIFATTEQ-PDEVLLKT----LLRRIPLI-VKVPSLAERP 321
Cdd:COG3604   163 ------------QEGEF--------ERVGGDETIKV-DVRIIAATNRDlEEEVAEGRfredLYYRLNVFpIRLPPLRERR 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 322 lqEKRELL--QFLIQEEEKHIQRKISMSDLVFRTLERHTFTGNIGELKNVIRASVAKAflrnqkdmDDVSLHIYDLSSDL 399
Cdd:COG3604   222 --EDIPLLaeHFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVILA--------EGGVLDADDLAPGS 291

                  ....
gi 1589195055 400 LEST 403
Cdd:COG3604   292 REAL 295
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
168-315 1.75e-04

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: 42.20  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 168 ILLQGPTGTGKSLIAqlmyqygvemEILSKDS--RFMTMNCSEyannpemlmtnlfgyKKGSYTGA-EKDTQGLLALA-- 242
Cdd:pfam00004   1 LLLYGPPGTGKTTLA----------KAVAKELgaPFIEISGSE---------------LVSKYVGEsEKRLRELFEAAkk 55
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1589195055 243 -DGGILFMDEVHGLKPECQEKIFLFMDKGIYHMVGDNDTWYVSNARLIF-ATTEQPDEvLLKTLLRRIPLIVKVP 315
Cdd:pfam00004  56 lAPCVIFIDEIDALAGSRGSGGDSESRRVVNQLLTELDGFTSSNSKVIViAATNRPDK-LDPALLGRFDRIIEFP 129
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
800-943 2.39e-04

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: 45.10  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 800 ISLEEMIEQKSVE-----KTNSVFESIMRpDQIETFNENMIKNFSMDNLLSYLTILDSDKIIDSVEKIIKTIQKELHMKL 874
Cdd:COG1221   411 YNFYEIIEDKYEElksegLSEEEINKIIS-KDIESYFKKLIFKLDKSNISEELLLIVVDEVIVNVVEIFEEAEKKLLRYN 489
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1589195055 875 SSSVILGLYIHISCLIERLIINKNVTKFEHLETFEKTQTEFIRIVKKAFHDVEQHYNVkIPVSEIGYIY 943
Cdd:COG1221   490 SSNLFIALSLHLLSTLLRIKKGKKIINPQLNEIKKKYYEEFILAAEAIKIIEEELKIL-IPDEEEGFIL 557
AAA_7 pfam12775
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ...
163-228 2.94e-04

P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).


Pssm-ID: 463698 [Multi-domain]  Cd Length: 179  Bit Score: 42.76  E-value: 2.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1589195055 163 EHGLPILLQGPTGTGKSLIAQLMyqygveMEILSKDSR-FMTMNCSeYANNPEMLMTNLFGY----KKGSY 228
Cdd:pfam12775  29 KNGKPVLLVGPTGTGKTVIIQNL------LRKLDKEKYlPLFINFS-AQTTSNQTQDIIESKlekrRKGVY 92
ManX COG2893
Phosphotransferase system, mannose/fructose-specific component IIA [Carbohydrate transport and ...
599-661 5.75e-04

Phosphotransferase system, mannose/fructose-specific component IIA [Carbohydrate transport and metabolism];


Pssm-ID: 442138 [Multi-domain]  Cd Length: 126  Bit Score: 40.89  E-value: 5.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1589195055 599 VIIAHGyAIASGIAEVANQLL-KQRIFDAIDMPIESDFNDTVKKLGEYIKGKENYNEVIVMVDM 661
Cdd:COG2893     2 VIATHG-PLAEGLLSSAEMILgEQENVEAVDLYPGDDPEDLREKLEEAIAELDSGDGVLILTDL 64
EIIA-man pfam03610
PTS system fructose IIA component;
599-663 9.36e-04

PTS system fructose IIA component;


Pssm-ID: 427399 [Multi-domain]  Cd Length: 113  Bit Score: 39.93  E-value: 9.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1589195055 599 VIIAHGyAIASGIAEVANQLLK-QRIFDAIDMPIESDFNDTVKKLGEYIKGKENYNEVIVMVDMGS 663
Cdd:pfam03610   3 VIVSHG-ELAEGLLELAEMMAGeQENVIAVGGTPGESIGTSFEKIVEAIENLDSGDGVLVLVDLGG 67
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
168-314 1.26e-03

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: 40.34  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195055 168 ILLQGPTGTGKSLIAQ-LMYQYGVEMeILSKDSRFMtmncSEYANNPEMLMTNLFgykkgsyTGAEKdtqgllalADGGI 246
Cdd:cd19481    29 ILLYGPPGTGKTLLAKaLAGELGLPL-IVVKLSSLL----SKYVGESEKNLRKIF-------ERARR--------LAPCI 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1589195055 247 LFMDEVHGL--------KPECQEKIFLFMdkgIYHMVGDNDTWYVsnarLIFATTEQPDEvLLKTLLR--RIPLIVKV 314
Cdd:cd19481    89 LFIDEIDAIgrkrdssgESGELRRVLNQL---LTELDGVNSRSKV----LVIAATNRPDL-LDPALLRpgRFDEVIEF 158
 
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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