|
Name |
Accession |
Description |
Interval |
E-value |
| PspF |
COG1221 |
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ... |
23-806 |
9.02e-172 |
|
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: 519.66 E-value: 9.02e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 23 AVAISEALHLSRNMVSQYLNQLWNEGKLVKINTRPVLFYDVQTLEKLFSIHLKEKEFTSKKEFVKALQPQEAKDFEKLIG 102
Cdd:COG1221 29 AEEIAEKLGISRNNVSHELNELVKEGKLIKINGRPVLFLDKEAFEEQFGTKLKSEYSFVELLAEKENNEEEEDPFDNLIG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 103 AQESLANVVNQCKATISYPPNGLPLLLYGPTGTGKSFMAQLMYEYALNHQLIEADKKFLIVNCSEYANNPELLTANLFGH 182
Cdd:COG1221 109 ANGSLKNAIEQAKAAILYPPKGLHTLILGPTGVGKSFFAELMYEYAIEIGVLPEDAPFVVFNCADYANNPQLLMSQLFGY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 183 KKGAFTGADKDNPGLIKLAEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNEKWYQSSLRLIFATTEKPEEVLLKT 262
Cdd:COG1221 189 VKGAFTGADKDKEGLIEKADGGILFLDEVHRLPPEGQEMLFTFMDKGIYRRLGETEKTRKANVRIIFATTEDPESSLLKT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 263 LLRRIPMIITIPSLEERGTHERLQLIHSIFAAEETRIHKSIYLSTLVYQTLLSTTFNANIGELKNAIQASCVNA-LFHAD 341
Cdd:COG1221 269 FLRRIPMVIKLPSLEERSLEERLELIKHFFKEEAKRLNKPIKVSKEVLKALLLYDCPGNIGQLKSDIQLACAKAfLNYIT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 342 PNKDRLEIRAYNLPETLKEPKMNVPSMTE--QKLISVHELAKFVSHERailkcNEELLKAYDARENSDLFLKTACQSIDE 419
Cdd:COG1221 349 NKKEEIEITLSDLPENVKKGLLKLKENREelDKLSEYLEEYLIISPDT-----EKKLISEEDEYELPYNFYEIIEDKYEE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 420 YQETIVfqKKKTIrkNEYLQGIVSNIFDMLSSRYGFKF---------VNNDVIAIASYIDDYSRNLL------------- 477
Cdd:COG1221 424 LKSEGL--SEEEI--NKIISKDIESYFKKLIFKLDKSNiseelllivVDEVIVNVVEIFEEAEKKLLrynssnlfialsl 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 478 ----EMNNWLEQEKKHVKQLLSYIKSEWHREYAIAQEIVENLTVNLDMEFD--AMFTSVLALNLKKLNRITDLNKRIGII 551
Cdd:COG1221 500 hllsTLLRIKKGKKIINPQLNEIKKKYYEEFILAAEAIKIIEEELKILIPDeeEGFILLLLIELKEEKSLSENVIVVVVI 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 552 IAHGFSTASSMADAANKLLGRYVFDAMDMPLQLSSTQIIEQLNRYLAKIPQYEELFLLVDMGSL---EEIYKGLEVSNas 628
Cdd:COG1221 580 AHGGAAASSSMAVVNLLLLEVAVAAIDDPPLEVVDVLIEEKTIVVIINKGKGGLLLLLDDGGSLfgiIIIEEEGIIIV-- 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 629 IGIMNNVTTRLALEIGQGIISNTPMKEIFETAVDYSSANYHI----VEHKNREKVILCSCASGMGTAEKLKKILVDSLPC 704
Cdd:COG1221 658 TVVIVSTTTVLEAAARKKLLELDLDEIIVLEELLKNPLESKKikisTSKKKKIIVTTIAITTGEAGGILILILIIELLDK 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 705 DLPIHVYTYDYNTLLEKQLHDAFFENYEVICIVGTlnpnIPDIRFIPIEDLIINDTLDELHDYFKDYISDSEMKTFQQNI 784
Cdd:COG1221 738 DLILIIIEILLIIIKEEILEKIIEEKKEVIIIVII----SIIPLIIPPIILLLALKLIILIEILVLLEILIDKEKIENII 813
|
810 820
....*....|....*....|..
gi 515712161 785 LKNFSLSNIMNNLTILNPSKLL 806
Cdd:COG1221 814 KELLSLLNIIIVLLIIDILILI 835
|
|
| Sigma54_activat |
pfam00158 |
Sigma-54 interaction domain; |
100-266 |
5.70e-47 |
|
Sigma-54 interaction domain;
Pssm-ID: 425491 [Multi-domain] Cd Length: 168 Bit Score: 165.27 E-value: 5.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 100 LIGAQESLANVVNQCKATISYPpngLPLLLYGPTGTGKSFMAQLMyeyalnHQLIE-ADKKFLIVNCSeyANNPELLTAN 178
Cdd:pfam00158 1 IIGESPAMQEVLEQAKRVAPTD---APVLITGESGTGKELFARAI------HQLSPrADGPFVAVNCA--AIPEELLESE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 179 LFGHKKGAFTGADKDNPGLIKLAEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNeKWYQSSLRLIFATTEKPEEV 258
Cdd:pfam00158 70 LFGHEKGAFTGADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGT-KPIKVDVRIIAATNRDLEEA 148
|
....*...
gi 515712161 259 LLKTLLRR 266
Cdd:pfam00158 149 VAEGRFRE 156
|
|
| PEP_resp_reg |
TIGR02915 |
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ... |
65-375 |
1.69e-23 |
|
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: 104.45 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 65 TLEKLFSIHLKEKEftsKKEFVKALQPQEakdFEKLIGAQESLANVvnqCKATISYPPNGLPLLLYGPTGTGKSFMAQLM 144
Cdd:TIGR02915 112 IVDRAFHLYTLETE---NRRLQSALGGTA---LRGLITSSPGMQKI---CRTIEKIAPSDITVLLLGESGTGKEVLARAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 145 YEYALnhqliEADKKFLIVNCSEYANNpeLLTANLFGHKKGAFTGADKDNPGLIKLAEGGVLFLDEVHCLPPECQEKLFL 224
Cdd:TIGR02915 183 HQLSD-----RKDKRFVAINCAAIPEN--LLESELFGYEKGAFTGAVKQTLGKIEYAHGGTLFLDEIGDLPLNLQAKLLR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 225 FMDKGIYHMVGDNEKwYQSSLRLIFATTEKPEEVLLKTLLR-----RIPMI-ITIPSLEERGTHERL--QLIHSIFAAEE 296
Cdd:TIGR02915 256 FLQERVIERLGGREE-IPVDVRIVCATNQDLKRMIAEGTFRedlfyRIAEIsITIPPLRSRDGDAVLlaNAFLERFAREL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 297 TRIHKSIYLSTLVYqtLLSTTFNANIGELKNAIQASCVNALFH----ADPNKDRLEIRAYNLPETLKEPKMNVPSMTEQK 372
Cdd:TIGR02915 335 KRKTKGFTDDALRA--LEAHAWPGNVRELENKVKRAVIMAEGNqitaEDLGLDARERAETPLEVNLREVRERAEREAVRK 412
|
...
gi 515712161 373 LIS 375
Cdd:TIGR02915 413 AIA 415
|
|
| pspF |
PRK11608 |
phage shock protein operon transcriptional activator; Provisional |
94-332 |
1.58e-21 |
|
phage shock protein operon transcriptional activator; Provisional
Pssm-ID: 236936 [Multi-domain] Cd Length: 326 Bit Score: 96.66 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 94 AKDFEKLIGAQESLANVVNQCKAtisYPPNGLPLLLYGPTGTGKSFMAQLMyeyalnHQLIEA-DKKFLIVNCSeyANNP 172
Cdd:PRK11608 2 AEYKDNLLGEANSFLEVLEQVSR---LAPLDKPVLIIGERGTGKELIASRL------HYLSSRwQGPFISLNCA--ALNE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 173 ELLTANLFGHKKGAFTGADKDNPGLIKLAEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNEKwYQSSLRLIFATT 252
Cdd:PRK11608 71 NLLDSELFGHEAGAFTGAQKRHPGRFERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQP-LQVNVRLVCATN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 253 EK-----PEEVLLKTLLRRIPM-IITIPSLEERgtHERLQLIHSIFAAEETR-IHKSIY--LSTLVYQTLLSTTFNANIG 323
Cdd:PRK11608 150 ADlpamvAEGKFRADLLDRLAFdVVQLPPLRER--QSDIMLMAEHFAIQMCReLGLPLFpgFTERARETLLNYRWPGNIR 227
|
....*....
gi 515712161 324 ELKNAIQAS 332
Cdd:PRK11608 228 ELKNVVERS 236
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
122-275 |
6.19e-18 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 81.42 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 122 PNGLPLLLYGPTGTGKSFMAQlmyeyALNHQLIEADKKFLIVNCSEYANnpELLTANLFGHkkgaftGADKDNPGLIKLA 201
Cdd:cd00009 17 PPPKNLLLYGPPGTGKTTLAR-----AIANELFRPGAPFLYLNASDLLE--GLVVAELFGH------FLVRLLFELAEKA 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515712161 202 EGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGdnekwyQSSLRLIFATTEKPEEVLLKTLLRRIPMIITIPS 275
Cdd:cd00009 84 KPGVLFIDEIDSLSRGAQNALLRVLETLNDLRID------RENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
124-267 |
1.34e-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: 54.69 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 124 GLPLLLYGPTGTGKSFMAQlmyeyALNHQLIEADKKFLIVNCSEYANNPELLTANLFGHKKGAFTGADKDNPGLIKLAEG 203
Cdd:smart00382 2 GEVILIVGPPGSGKTTLAR-----ALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARK 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515712161 204 ---GVLFLDEVHCLPPECQEKLFLFMDkgiyHMVGDNEKWYQSSLRLIFATTekPEEVLLKTLLRRI 267
Cdd:smart00382 77 lkpDVLILDEITSLLDAEQEALLLLLE----ELRLLLLLKSEKNLTVILTTN--DEKDLGPALLRRR 137
|
|
| BglG |
COG3711 |
Transcriptional antiterminator [Transcription]; |
771-899 |
2.77e-06 |
|
Transcriptional antiterminator [Transcription];
Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 51.01 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 771 YISDSEMK--TFQQNILKNFSLSNIMNNLTILN--PSKLLEHVADAIDKLQNDLQVRLTNNTCVGLYVHVCCLIERLVTR 846
Cdd:COG3711 140 KLEGSELDirKALAELLSELLSENDLLSLLLLKliPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKG 219
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 515712161 847 KSI----ETYTNVEDFAEKEIAfiksvKKAFSVVENYYSVEIPVEEIGYIFDYVKNN 899
Cdd:COG3711 220 KYIkldnPLLWEIKKPKEYEIA-----KEILKLIEERLGISLPEDEIGYIALHLLGA 271
|
|
| PRD |
pfam00874 |
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ... |
811-892 |
4.59e-05 |
|
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: 43.01 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 811 DAIDKLQNDLQVRLTNNTCV-GLYVHVCCLIERLVTRKSIEtYTNVEDFAEKEIAFIKSVKKAFSVVENYYSVEIPVEEI 889
Cdd:pfam00874 2 EIIELIEKKLGITFDDDILYiRLILHLAFAIERIKEGITIE-NPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEI 80
|
...
gi 515712161 890 GYI 892
Cdd:pfam00874 81 GYI 83
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PspF |
COG1221 |
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ... |
23-806 |
9.02e-172 |
|
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: 519.66 E-value: 9.02e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 23 AVAISEALHLSRNMVSQYLNQLWNEGKLVKINTRPVLFYDVQTLEKLFSIHLKEKEFTSKKEFVKALQPQEAKDFEKLIG 102
Cdd:COG1221 29 AEEIAEKLGISRNNVSHELNELVKEGKLIKINGRPVLFLDKEAFEEQFGTKLKSEYSFVELLAEKENNEEEEDPFDNLIG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 103 AQESLANVVNQCKATISYPPNGLPLLLYGPTGTGKSFMAQLMYEYALNHQLIEADKKFLIVNCSEYANNPELLTANLFGH 182
Cdd:COG1221 109 ANGSLKNAIEQAKAAILYPPKGLHTLILGPTGVGKSFFAELMYEYAIEIGVLPEDAPFVVFNCADYANNPQLLMSQLFGY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 183 KKGAFTGADKDNPGLIKLAEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNEKWYQSSLRLIFATTEKPEEVLLKT 262
Cdd:COG1221 189 VKGAFTGADKDKEGLIEKADGGILFLDEVHRLPPEGQEMLFTFMDKGIYRRLGETEKTRKANVRIIFATTEDPESSLLKT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 263 LLRRIPMIITIPSLEERGTHERLQLIHSIFAAEETRIHKSIYLSTLVYQTLLSTTFNANIGELKNAIQASCVNA-LFHAD 341
Cdd:COG1221 269 FLRRIPMVIKLPSLEERSLEERLELIKHFFKEEAKRLNKPIKVSKEVLKALLLYDCPGNIGQLKSDIQLACAKAfLNYIT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 342 PNKDRLEIRAYNLPETLKEPKMNVPSMTE--QKLISVHELAKFVSHERailkcNEELLKAYDARENSDLFLKTACQSIDE 419
Cdd:COG1221 349 NKKEEIEITLSDLPENVKKGLLKLKENREelDKLSEYLEEYLIISPDT-----EKKLISEEDEYELPYNFYEIIEDKYEE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 420 YQETIVfqKKKTIrkNEYLQGIVSNIFDMLSSRYGFKF---------VNNDVIAIASYIDDYSRNLL------------- 477
Cdd:COG1221 424 LKSEGL--SEEEI--NKIISKDIESYFKKLIFKLDKSNiseelllivVDEVIVNVVEIFEEAEKKLLrynssnlfialsl 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 478 ----EMNNWLEQEKKHVKQLLSYIKSEWHREYAIAQEIVENLTVNLDMEFD--AMFTSVLALNLKKLNRITDLNKRIGII 551
Cdd:COG1221 500 hllsTLLRIKKGKKIINPQLNEIKKKYYEEFILAAEAIKIIEEELKILIPDeeEGFILLLLIELKEEKSLSENVIVVVVI 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 552 IAHGFSTASSMADAANKLLGRYVFDAMDMPLQLSSTQIIEQLNRYLAKIPQYEELFLLVDMGSL---EEIYKGLEVSNas 628
Cdd:COG1221 580 AHGGAAASSSMAVVNLLLLEVAVAAIDDPPLEVVDVLIEEKTIVVIINKGKGGLLLLLDDGGSLfgiIIIEEEGIIIV-- 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 629 IGIMNNVTTRLALEIGQGIISNTPMKEIFETAVDYSSANYHI----VEHKNREKVILCSCASGMGTAEKLKKILVDSLPC 704
Cdd:COG1221 658 TVVIVSTTTVLEAAARKKLLELDLDEIIVLEELLKNPLESKKikisTSKKKKIIVTTIAITTGEAGGILILILIIELLDK 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 705 DLPIHVYTYDYNTLLEKQLHDAFFENYEVICIVGTlnpnIPDIRFIPIEDLIINDTLDELHDYFKDYISDSEMKTFQQNI 784
Cdd:COG1221 738 DLILIIIEILLIIIKEEILEKIIEEKKEVIIIVII----SIIPLIIPPIILLLALKLIILIEILVLLEILIDKEKIENII 813
|
810 820
....*....|....*....|..
gi 515712161 785 LKNFSLSNIMNNLTILNPSKLL 806
Cdd:COG1221 814 KELLSLLNIIIVLLIIDILILI 835
|
|
| LevR |
COG3933 |
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription]; |
34-898 |
2.57e-158 |
|
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
Pssm-ID: 443134 [Multi-domain] Cd Length: 916 Bit Score: 487.32 E-value: 2.57e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 34 RNMVSQYLNQLWNEGKLVKINTRPVLFYDVQTLEKLFSIHLKEKEFTSKKEFVKALQPQEAKDFEKLIGAQESLANVVNQ 113
Cdd:COG3933 32 LLKESTGLLKLLALLLLLKRLSELLLELKKLKKEKKTLKKERSLLEKKKNKLNLKEEKKEKLDFKALIGLSLSLLSAAAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 114 CKATISYPPNGLPLLLYGPTGTGKSFMAQLMYEYALnhQLIEADKKFLIVNCSEYANNPELLTANLFGHKKGAFTGADKD 193
Cdd:COG3933 112 AKAAKPPPPLGLLTLLLGGTGGGKSAFAGYMYAFAA--KIAELAAPFVFFNFANAAYNPNLLLLLLFGLGGGAGGGAGAD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 194 NPGLIKLAEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNEKWYQSSLRLIFATTEKPEEVLLKTLLRRIPMIITI 273
Cdd:COG3933 190 GGGLGGAAGAGGGLLDLLDELPLEGEEQEELFFLLGKGLFRGEGGESRSRRVRIIRATTETEESLLLTTLTRRIRIIIIL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 274 PSLEERGT--HERLQLIHSIFAAEETRIHKSIYLSTLVYQTLLSTTFNANIGELKNAIQASCVNALFHA----------- 340
Cdd:COG3933 270 PRLPILERreRERLLLLLFEFEEEEIRIIKILIVLLLALLLLLLYVNNLGQLGLLKLLIKAAAAAALAKaikeatiilrl 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 341 -DPNKDRLEIRAYNLPETLKE-----PKMNVPSMTEQKLISVHELAKFVSHERAILKCNEELLKAYDARENSDLFLKTAC 414
Cdd:COG3933 350 lSKLLKLLLLLLLNERLLLLElkiliEPLDIFFDSSASSDESDESEEDENLYEIIEIKKKLLLELGIDEEEINIIIEIDI 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 415 QS---IDEYQETIVFQKKK--TIRKNEYLQgIVSNIFDMLSSRYGFKFVNNDVIAIASYIddYSrnlleMNNWLEQEKKH 489
Cdd:COG3933 430 DVhllKFIYDDNKNFNKEElaKIVDEDIIN-VVEEILELAEKKLGRKFSENFIYALSLHL--SS-----FIERIKEGKEI 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 490 VKQLLSYIKSEWHREYAIAQEIVENLTVNLDMEFDAMFTSVLALNLKKLNrITDLNKRIGIII-AHGFSTASSMADAANK 568
Cdd:COG3933 502 INPNLNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLTLFLVSLN-ENNESGKVGVIVlAHGYSTASSMAEVANR 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 569 LLGRYVFDAMDMPLQLSSTQIIEQLNRYLAKIPQYEELFLLVDMGSLEEIYKGL-EVSNASIGIMNNVTTRLALEIGQGI 647
Cdd:COG3933 581 LLGTNIFEAIDMPLDMSPEDILEKLKEYVKKIDTGKGVLLLVDMGSLTTFGEIIeEETGIPVKTIDMVSTPLVLEAGRKA 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 648 ISNTPMKEIFETAVD---YSSANYHIVEHKNREKVILCSCASGMGTAEKLKKILVDSLP-CDLPIHVYTYDYNTLLE-KQ 722
Cdd:COG3933 661 LLGMSLEEIYESLKNfnpYEKIISKNKPEKNKKKAIITTCFTGEGTAVKIKDLLEKSLPeDEDNIEIIPLDYLELEEfKE 740
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 723 LHDAFFENYEVICIVGTLNPNIPDIRFIPIEDLIINDTLDELHDYFKDYISDSEMKTFQQNILKNFSLSNIMNNLTILNP 802
Cdd:COG3933 741 KIDEIFKEYEILAIVGTIDPEIPDIPFISLEDLISGEGIEKLQKLLGGELDAEEIEEINNEIIKNFSLESLIESLTILNP 820
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 803 SKLLEHVADAIDKLQNDLQVRLTNNTCVGLYVHVCCLIERLVTRKSIETYTNVEDFAEKEIAFIKSVKKAFSVVENYYSV 882
Cdd:COG3933 821 EKIINELEDFISRLENLLGIKLDNDVKIGLILHIACMIERLVTGEEILTYPNKEEFIQENESEYAVIKEAFSPIEEKYNI 900
|
890
....*....|....*.
gi 515712161 883 EIPVEEIGYIFDYVKN 898
Cdd:COG3933 901 KIPDSEIAYIYDILKN 916
|
|
| Sigma54_activat |
pfam00158 |
Sigma-54 interaction domain; |
100-266 |
5.70e-47 |
|
Sigma-54 interaction domain;
Pssm-ID: 425491 [Multi-domain] Cd Length: 168 Bit Score: 165.27 E-value: 5.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 100 LIGAQESLANVVNQCKATISYPpngLPLLLYGPTGTGKSFMAQLMyeyalnHQLIE-ADKKFLIVNCSeyANNPELLTAN 178
Cdd:pfam00158 1 IIGESPAMQEVLEQAKRVAPTD---APVLITGESGTGKELFARAI------HQLSPrADGPFVAVNCA--AIPEELLESE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 179 LFGHKKGAFTGADKDNPGLIKLAEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNeKWYQSSLRLIFATTEKPEEV 258
Cdd:pfam00158 70 LFGHEKGAFTGADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGT-KPIKVDVRIIAATNRDLEEA 148
|
....*...
gi 515712161 259 LLKTLLRR 266
Cdd:pfam00158 149 VAEGRFRE 156
|
|
| AtoC |
COG2204 |
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ... |
92-360 |
7.21e-32 |
|
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: 129.31 E-value: 7.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 92 QEAKDFEKLIGAQESLANVVNQCKATIsypPNGLPLLLYGPTGTGKSFMAQlmyeyALNHQLIEADKKFLIVNCSeyANN 171
Cdd:COG2204 125 RENAEDSGLIGRSPAMQEVRRLIEKVA---PSDATVLITGESGTGKELVAR-----AIHRLSPRADGPFVAVNCA--AIP 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 172 PELLTANLFGHKKGAFTGADKDNPGLIKLAEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNEKwYQSSLRLIFAT 251
Cdd:COG2204 195 EELLESELFGHEKGAFTGAVARRIGKFELADGGTLFLDEIGEMPLALQAKLLRVLQEREFERVGGNKP-IPVDVRVIAAT 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 252 TEKPEEVLLKTLLR-----RIPMI-ITIPSLEERGThERLQLIHSIFAAEETRIHKSIYLSTLVYQTLLSTTFNANIGEL 325
Cdd:COG2204 274 NRDLEELVEEGRFRedlyyRLNVFpIELPPLRERRE-DIPLLARHFLARFAAELGKPVKLSPEALEALLAYDWPGNVREL 352
|
250 260 270
....*....|....*....|....*....|....*
gi 515712161 326 KNAIQASCVNAlfhadpnkDRLEIRAYNLPETLKE 360
Cdd:COG2204 353 ENVIERAVILA--------DGEVITAEDLPEALEE 379
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
91-391 |
4.23e-29 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 123.86 E-value: 4.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 91 PQEAKDFEKLIGAQESLANVVNQCKATIsypPNGLPLLLYGPTGTGKSFMAQlmyeyALNHQLIEADKKFLIVNCSeyAN 170
Cdd:COG3284 314 APAPAALAALAGGDPAMRRALRRARRLA---DRDIPVLILGETGTGKELFAR-----AIHAASPRADGPFVAVNCA--AI 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 171 NPELLTANLFGHKKGAFTGADKD-NPGLIKLAEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNeKWYQSSLRLIf 249
Cdd:COG3284 384 PEELIESELFGYEPGAFTGARRKgRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGT-KPIPVDVRLI- 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 250 ATTEK--PEEVLLKT----LLRRI-PMIITIPSLEERGthERLQLIHSIFAAEETRiHKSIYLSTLVYQTLLSTTFNANI 322
Cdd:COG3284 462 AATHRdlRELVAAGRfredLYYRLnGLTLTLPPLRERE--DLPALIEHLLRELAAG-RGPLRLSPEALALLAAYPWPGNV 538
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515712161 323 GELKNAIQAscvnALFHADPNkdrlEIRAYNLPETLKEPKMNVPSMTEQKLISVHELAKfvsheRAILK 391
Cdd:COG3284 539 RELRNVLRT----ALALADGG----VITVEDLPDELRAELAAAAPAAAAPLTSLEEAER-----DAILR 594
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
46-400 |
8.82e-27 |
|
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: 114.48 E-value: 8.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 46 NEGKLVKINTRPVL-----------FYDVQTLEKLfsihlkeKEFTSKKEFVKALQPQEAkdFEKLIGAQESLANVVNQC 114
Cdd:COG3829 84 GKGKTVIVTAIPIFedgevigavetFRDITELKRL-------ERKLREEELERGLSAKYT--FDDIIGKSPAMKELLELA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 115 K------ATIsyppnglplLLYGPTGTGKSFMAQLMyeyalnHQLIE-ADKKFLIVNCSeyANNPELLTANLFGHKKGAF 187
Cdd:COG3829 155 KrvaksdSTV---------LILGESGTGKELFARAI------HNASPrRDGPFVAVNCA--AIPENLLESELFGYEKGAF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 188 TGADK-DNPGLIKLAEGGVLFLDEVHCLPPECQEKL--FLfMDKGIYHmVGDNEKwYQSSLRLIFATTEKPEEVLLKTLL 264
Cdd:COG3829 218 TGAKKgGKPGLFELADGGTLFLDEIGEMPLSLQAKLlrVL-QEKEVRR-VGGTKP-IPVDVRIIAATNRDLEEMVEEGRF 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 265 RR--------IPmiITIPSLEERgtheR---LQLIHSIFAAEETRIHKSI-YLSTLVYQTLLSTTFNANIGELKNAIQAS 332
Cdd:COG3829 295 REdlyyrlnvIP--IHIPPLRER----KediPLLAEHFLEKFNKKYGKNIkGISPEALELLLAYDWPGNVRELENVIERA 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515712161 333 CVNAlfhadpnkDRLEIRAYNLPETLKEPKMNVPSMTEQKLISVHELAkfvshERAILkcnEELLKAY 400
Cdd:COG3829 369 VVLS--------EGDVITPEHLPEYLLEEAEAASAAEEGSLKEALEEV-----EKELI---EEALEKT 420
|
|
| PEP_resp_reg |
TIGR02915 |
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ... |
65-375 |
1.69e-23 |
|
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: 104.45 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 65 TLEKLFSIHLKEKEftsKKEFVKALQPQEakdFEKLIGAQESLANVvnqCKATISYPPNGLPLLLYGPTGTGKSFMAQLM 144
Cdd:TIGR02915 112 IVDRAFHLYTLETE---NRRLQSALGGTA---LRGLITSSPGMQKI---CRTIEKIAPSDITVLLLGESGTGKEVLARAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 145 YEYALnhqliEADKKFLIVNCSEYANNpeLLTANLFGHKKGAFTGADKDNPGLIKLAEGGVLFLDEVHCLPPECQEKLFL 224
Cdd:TIGR02915 183 HQLSD-----RKDKRFVAINCAAIPEN--LLESELFGYEKGAFTGAVKQTLGKIEYAHGGTLFLDEIGDLPLNLQAKLLR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 225 FMDKGIYHMVGDNEKwYQSSLRLIFATTEKPEEVLLKTLLR-----RIPMI-ITIPSLEERGTHERL--QLIHSIFAAEE 296
Cdd:TIGR02915 256 FLQERVIERLGGREE-IPVDVRIVCATNQDLKRMIAEGTFRedlfyRIAEIsITIPPLRSRDGDAVLlaNAFLERFAREL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 297 TRIHKSIYLSTLVYqtLLSTTFNANIGELKNAIQASCVNALFH----ADPNKDRLEIRAYNLPETLKEPKMNVPSMTEQK 372
Cdd:TIGR02915 335 KRKTKGFTDDALRA--LEAHAWPGNVRELENKVKRAVIMAEGNqitaEDLGLDARERAETPLEVNLREVRERAEREAVRK 412
|
...
gi 515712161 373 LIS 375
Cdd:TIGR02915 413 AIA 415
|
|
| pspF |
PRK11608 |
phage shock protein operon transcriptional activator; Provisional |
94-332 |
1.58e-21 |
|
phage shock protein operon transcriptional activator; Provisional
Pssm-ID: 236936 [Multi-domain] Cd Length: 326 Bit Score: 96.66 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 94 AKDFEKLIGAQESLANVVNQCKAtisYPPNGLPLLLYGPTGTGKSFMAQLMyeyalnHQLIEA-DKKFLIVNCSeyANNP 172
Cdd:PRK11608 2 AEYKDNLLGEANSFLEVLEQVSR---LAPLDKPVLIIGERGTGKELIASRL------HYLSSRwQGPFISLNCA--ALNE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 173 ELLTANLFGHKKGAFTGADKDNPGLIKLAEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNEKwYQSSLRLIFATT 252
Cdd:PRK11608 71 NLLDSELFGHEAGAFTGAQKRHPGRFERADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQP-LQVNVRLVCATN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 253 EK-----PEEVLLKTLLRRIPM-IITIPSLEERgtHERLQLIHSIFAAEETR-IHKSIY--LSTLVYQTLLSTTFNANIG 323
Cdd:PRK11608 150 ADlpamvAEGKFRADLLDRLAFdVVQLPPLRER--QSDIMLMAEHFAIQMCReLGLPLFpgFTERARETLLNYRWPGNIR 227
|
....*....
gi 515712161 324 ELKNAIQAS 332
Cdd:PRK11608 228 ELKNVVERS 236
|
|
| nifA |
TIGR01817 |
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ... |
100-334 |
1.59e-21 |
|
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: 99.40 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 100 LIGAQESLANVVNQCKatISYPPNGLPLLLyGPTGTGKSFMAQlmyeyALNHQLIEADKKFLIVNCSEYANNpeLLTANL 179
Cdd:TIGR01817 198 IIGKSPAMRQVVDQAR--VVARSNSTVLLR-GESGTGKELIAK-----AIHYLSPRAKRPFVKVNCAALSET--LLESEL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 180 FGHKKGAFTGADKDNPGLIKLAEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNEKwYQSSLRLIFATTEKPEEVL 259
Cdd:TIGR01817 268 FGHEKGAFTGAIAQRKGRFELADGGTLFLDEIGEISPAFQAKLLRVLQEGEFERVGGNRT-LKVDVRLVAATNRDLEEAV 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 260 LKTLLR-----RIP-MIITIPSLEERG------THERLQLihsiFAAEEtriHKSIYLSTLVYQTLLSTTFNANIGELKN 327
Cdd:TIGR01817 347 AKGEFRadlyyRINvVPIFLPPLRERRedipllAEAFLEK----FNREN---GRPLTITPSAIRVLMSCKWPGNVRELEN 419
|
....*..
gi 515712161 328 AIQASCV 334
Cdd:TIGR01817 420 CLERTAT 426
|
|
| RtcR |
COG4650 |
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ... |
126-211 |
2.47e-20 |
|
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: 95.67 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 126 PLLLYGPTGTGKSFMAQLMYEYALN-HQLieaDKKFLIVNCSeyannpellT-------ANLFGHKKGAFTGADKDNPGL 197
Cdd:COG4650 210 PILLTGPTGAGKSQLARRIYELKKArHQV---SGRFVEVNCA---------TlrgdgamSALFGHVKGAFTGAVSDRAGL 277
|
90
....*....|....
gi 515712161 198 IKLAEGGVLFLDEV 211
Cdd:COG4650 278 LRSADGGVLFLDEI 291
|
|
| PRK10365 |
PRK10365 |
sigma-54-dependent response regulator transcription factor ZraR; |
56-334 |
6.97e-20 |
|
sigma-54-dependent response regulator transcription factor ZraR;
Pssm-ID: 182412 [Multi-domain] Cd Length: 441 Bit Score: 93.56 E-value: 6.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 56 RPVLFYDVQ-TLEKLFSiHLKEkeftskkefVKALQPQEAKDFEKLIGAQESLANVVNQCKATisyPPNGLPLLLYGPTG 134
Cdd:PRK10365 106 KPLDFDNLQaTLEKALA-HTHS---------IDAETPAVTASQFGMVGKSPAMQHLLSEIALV---APSEATVLIHGDSG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 135 TGKSFMAQlmyeyALNHQLIEADKKFLIVNCSeyANNPELLTANLFGHKKGAFTGADKDNPGLIKLAEGGVLFLDEVHCL 214
Cdd:PRK10365 173 TGKELVAR-----AIHASSARSEKPLVTLNCA--ALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEIGDI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 215 PPECQEKLFLFMDKGIYHMVGDNEKwYQSSLRLIFATTEK-PEEV----LLKTLLRRIPMI-ITIPSLEERgtHERLQLI 288
Cdd:PRK10365 246 SPMMQVRLLRAIQEREVQRVGSNQT-ISVDVRLIAATHRDlAAEVnagrFRQDLYYRLNVVaIEVPSLRQR--REDIPLL 322
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 515712161 289 HSIFA---AEETRihKSIY-LSTLVYQTLLSTTFNANIGELKNAIQASCV 334
Cdd:PRK10365 323 AGHFLqrfAERNR--KAVKgFTPQAMDLLIHYDWPGNIRELENAVERAVV 370
|
|
| TyrR |
COG3283 |
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ... |
87-329 |
8.31e-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: 94.10 E-value: 8.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 87 KALQPQEAKDFEKLIGAQESLANVVNQCK--ATISyppngLPLLLYGPTGTGKSFMAQlmyeyALnHQL-IEADKKFLIV 163
Cdd:COG3283 193 QALQVNDDSGFDHIVASSPKMRQVIRQAKkmAMLD-----APLLIQGETGTGKELLAR-----AC-HLAsPRGDKPFLAL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 164 NCseyANNPELLT-ANLFGHKKGAFTGADKDNPGLIKLAEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDnEKWYQ 242
Cdd:COG3283 262 NC---AALPDDVAeSELFGYAPGAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGE-EQEVK 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 243 SSLRLIFATTEKPEEVLLKTLLR-----RIPMI-ITIPSLEERGthERLQLIHSIF---AAEETRIHKsIYLSTLVYQTL 313
Cdd:COG3283 338 VDVRVICATQKDLAELVQEGEFRedlyyRLNVLtLTLPPLRERK--SDILPLAEHFvarFSQQLGRPR-PRLSPDLVDFL 414
|
250
....*....|....*.
gi 515712161 314 LSTTFNANIGELKNAI 329
Cdd:COG3283 415 QSYPWPGNVRQLENAL 430
|
|
| PRK11361 |
PRK11361 |
acetoacetate metabolism transcriptional regulator AtoC; |
114-361 |
1.55e-19 |
|
acetoacetate metabolism transcriptional regulator AtoC;
Pssm-ID: 183099 [Multi-domain] Cd Length: 457 Bit Score: 92.60 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 114 CKATISYPPNGLPLLLYGPTGTGKSFMAQlmyeyALNHQLIEADKKFLIVNCseyANNPE-LLTANLFGHKKGAFTGADK 192
Cdd:PRK11361 156 CKDTAKIALSQASVLISGESGTGKELIAR-----AIHYNSRRAKGPFIKVNC---AALPEsLLESELFGHEKGAFTGAQT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 193 DNPGLIKLAEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNEKwYQSSLRLIFATTEKPEEVLLKTLLR-----RI 267
Cdd:PRK11361 228 LRQGLFERANEGTLLLDEIGEMPLVLQAKLLRILQEREFERIGGHQT-IKVDIRIIAATNRDLQAMVKEGTFRedlfyRL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 268 PMI-ITIPSLEERGTHERLQLIHSI--FAAEETRihKSIYLSTLVYQTLLSTTFNANIGELKNAIQASCVNALFHAdpnk 344
Cdd:PRK11361 307 NVIhLILPPLRDRREDISLLANHFLqkFSSENQR--DIIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPI---- 380
|
250
....*....|....*..
gi 515712161 345 drleIRAYNLPETLKEP 361
Cdd:PRK11361 381 ----IFSEDLPPQIRQP 393
|
|
| PRK15115 |
PRK15115 |
response regulator GlrR; Provisional |
127-334 |
1.00e-18 |
|
response regulator GlrR; Provisional
Pssm-ID: 185070 [Multi-domain] Cd Length: 444 Bit Score: 89.90 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 127 LLLYGPTGTGKSFMAQlmyeyALNHQLIEADKKFLIVNCSEYannPE-LLTANLFGHKKGAFTGADKDNPGLIKLAEGGV 205
Cdd:PRK15115 160 VLINGQSGTGKEILAQ-----AIHNASPRASKPFIAINCGAL---PEqLLESELFGHARGAFTGAVSNREGLFQAAEGGT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 206 LFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNEKwYQSSLRLIFATTEKPEEVLLKTLLR-----RIPMI-ITIPSLEER 279
Cdd:PRK15115 232 LFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRD-IDIDVRIISATHRDLPKAMARGEFRedlyyRLNVVsLKIPALAER 310
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515712161 280 GthERLQLIHSIFAAEETRIHKSIY--LSTLVYQTLLSTTFNANIGELKNAIQaSCV 334
Cdd:PRK15115 311 T--EDIPLLANHLLRQAAERHKPFVraFSTDAMKRLMTASWPGNVRQLVNVIE-QCV 364
|
|
| PRK15429 |
PRK15429 |
formate hydrogenlyase transcriptional activator FlhA; |
96-330 |
5.18e-18 |
|
formate hydrogenlyase transcriptional activator FlhA;
Pssm-ID: 237965 [Multi-domain] Cd Length: 686 Bit Score: 89.12 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 96 DFEKLIGAQESLANVVNQCKATISyppNGLPLLLYGPTGTGKSFMAQLMyeyalnHQLIE-ADKKFLIVNCSeyANNPEL 174
Cdd:PRK15429 374 EFGEIIGRSEAMYSVLKQVEMVAQ---SDSTVLILGETGTGKELIARAI------HNLSGrNNRRMVKMNCA--AMPAGL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 175 LTANLFGHKKGAFTGADKDNPGLIKLAEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNeKWYQSSLRLIFATTEK 254
Cdd:PRK15429 443 LESDLFGHERGAFTGASAQRIGRFELADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSN-KIIQTDVRLIAATNRD 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 255 PEEVLLKTLLR-----RIPMI-ITIPSLEERGthERLQLIHSIFAAEETRIHK----SIYLSTLvyQTLLSTTFNANIGE 324
Cdd:PRK15429 522 LKKMVADREFRsdlyyRLNVFpIHLPPLRERP--EDIPLLVKAFTFKIARRMGrnidSIPAETL--RTLSNMEWPGNVRE 597
|
....*.
gi 515712161 325 LKNAIQ 330
Cdd:PRK15429 598 LENVIE 603
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
122-275 |
6.19e-18 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 81.42 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 122 PNGLPLLLYGPTGTGKSFMAQlmyeyALNHQLIEADKKFLIVNCSEYANnpELLTANLFGHkkgaftGADKDNPGLIKLA 201
Cdd:cd00009 17 PPPKNLLLYGPPGTGKTTLAR-----AIANELFRPGAPFLYLNASDLLE--GLVVAELFGH------FLVRLLFELAEKA 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515712161 202 EGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGdnekwyQSSLRLIFATTEKPEEVLLKTLLRRIPMIITIPS 275
Cdd:cd00009 84 KPGVLFIDEIDSLSRGAQNALLRVLETLNDLRID------RENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
|
|
| PRK15424 |
PRK15424 |
propionate catabolism operon regulatory protein PrpR; Provisional |
110-388 |
5.27e-17 |
|
propionate catabolism operon regulatory protein PrpR; Provisional
Pssm-ID: 237963 [Multi-domain] Cd Length: 538 Bit Score: 85.16 E-value: 5.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 110 VVNQCKATIS-YPPNGLPLLLYGPTGTGKSFMAQLMY-EYALNHQLIEADKK--FLIVNCSEYANNpeLLTANLFGHKKG 185
Cdd:PRK15424 227 QMEQVRQTILlYARSSAAVLIQGETGTGKELAAQAIHrEYFARHDARQGKKShpFVAVNCGAIAES--LLEAELFGYEEG 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 186 AFTGADK-DNPGLIKLAEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNEKwYQSSLRLIFATTEKPEEVLLKTLL 264
Cdd:PRK15424 305 AFTGSRRgGRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQP-VPVDVRVISATHCDLEEDVRQGRF 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 265 RR------IPMIITIPSLEERGTHERLQLIH---SIFAAEETRIHKSIYLSTLVYQTLL-STTFNANIGELKNAIQASCV 334
Cdd:PRK15424 384 RRdlfyrlSILRLQLPPLRERVADILPLAESflkQSLAALSAPFSAALRQGLQQCETLLlHYDWPGNVRELRNLMERLAL 463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 515712161 335 NALFHADPNKDRLEIRAYnLPETLKEPKMNVPSMTEQKliSVHE-LAKFVSHERA 388
Cdd:PRK15424 464 FLSVEPTPDLTPQFLQLL-LPELARESAKTPAPRLLAA--TLQQaLERFNGDKTA 515
|
|
| PRK05022 |
PRK05022 |
nitric oxide reductase transcriptional regulator NorR; |
125-222 |
5.70e-17 |
|
nitric oxide reductase transcriptional regulator NorR;
Pssm-ID: 235331 [Multi-domain] Cd Length: 509 Bit Score: 84.84 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 125 LPLLLYGPTGTGKSFMAQlmyeyALNHQLIEADKKFLIVNCseyANNPE-LLTANLFGHKKGAFTGADKDNPGLIKLAEG 203
Cdd:PRK05022 211 LNVLILGETGVGKELVAR-----AIHAASPRADKPLVYLNC---AALPEsLAESELFGHVKGAFTGAISNRSGKFELADG 282
|
90
....*....|....*....
gi 515712161 204 GVLFLDEVHCLPPECQEKL 222
Cdd:PRK05022 283 GTLFLDEIGELPLALQAKL 301
|
|
| PRK11388 |
PRK11388 |
DNA-binding transcriptional regulator DhaR; Provisional |
126-392 |
1.15e-16 |
|
DNA-binding transcriptional regulator DhaR; Provisional
Pssm-ID: 183114 [Multi-domain] Cd Length: 638 Bit Score: 84.73 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 126 PLLLYGPTGTGKSFMAQlmyeyALNHQLIEADKKFLIVNCSEYanNPELLTANLFGhkkGAFTGADKDNPGLIKLAEGGV 205
Cdd:PRK11388 350 PVLLCGEEGVGKALLAQ-----AIHNESERAAGPYIAVNCQLY--PDEALAEEFLG---SDRTDSENGRLSKFELAHGGT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 206 LFLDEVHCLPPECQEKLFLFMDKGIYhMVGDNEKWYQSSLRLIFATTEKPEEVLLKTLLRR-----IPMI-ITIPSLEER 279
Cdd:PRK11388 420 LFLEKVEYLSPELQSALLQVLKTGVI-TRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRqlyyaLHAFeITIPPLRMR 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 280 gtHERL-QLIHSIFAAEETRIHKSIYLSTLVYQTLLSTTFNANIGELKNAIQascvNALFHADPNKDRLEirayNLPETL 358
Cdd:PRK11388 499 --REDIpALVNNKLRSLEKRFSTRLKIDDDALARLVSYRWPGNDFELRSVIE----NLALSSDNGRIRLS----DLPEHL 568
|
250 260 270
....*....|....*....|....*....|....*.
gi 515712161 359 K--EPKMNVPSMTEQKLISVHELAKfvsheRAILKC 392
Cdd:PRK11388 569 FteQATDDVSATRLSTSLSLAELEK-----EAIINA 599
|
|
| ntrC |
TIGR01818 |
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ... |
125-279 |
3.46e-16 |
|
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: 82.09 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 125 LPLLLYGPTGTGKSFMAQlmyeyALNHQLIEADKKFLIVNCSeyANNPELLTANLFGHKKGAFTGADKDNPGLIKLAEGG 204
Cdd:TIGR01818 158 ITVLINGESGTGKELVAR-----ALHRHSPRANGPFIALNMA--AIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGG 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 205 VLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNEKwYQSSLRLIFATTEKPEEVLLKTLLR-----RIPMI-ITIPSLEE 278
Cdd:TIGR01818 231 TLFLDEIGDMPLDAQTRLLRVLADGEFYRVGGRTP-IKVDVRIVAATHQNLEALVRQGKFRedlfhRLNVIrIHLPPLRE 309
|
.
gi 515712161 279 R 279
Cdd:TIGR01818 310 R 310
|
|
| PRK10820 |
PRK10820 |
transcriptional regulator TyrR; |
92-329 |
1.22e-15 |
|
transcriptional regulator TyrR;
Pssm-ID: 236769 [Multi-domain] Cd Length: 520 Bit Score: 80.89 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 92 QEAKDFEKLIGAQESLANVVNQCK--ATISyppngLPLLLYGPTGTGKSFMAqlmyeYALNHQLIEADKKFLIVNCseyA 169
Cdd:PRK10820 198 NDDSAFSQIVAVSPKMRQVVEQARklAMLD-----APLLITGDTGTGKDLLA-----YACHLRSPRGKKPFLALNC---A 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 170 NNPE-LLTANLFGHKKGAFTGADKDNPGLIKLAEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDnEKWYQSSLRLI 248
Cdd:PRK10820 265 SIPDdVVESELFGHAPGAYPNALEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTFRRVGE-DHEVHVDVRVI 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 249 FATTEKPEEVLLKTLLR-----RIPMI-ITIPSLEERgTHERLQLIHSIFA--AEETRIHKSiYLSTLVYQTLLSTTFNA 320
Cdd:PRK10820 344 CATQKNLVELVQKGEFRedlyyRLNVLtLNLPPLRDR-PQDIMPLTELFVArfADEQGVPRP-KLAADLNTVLTRYGWPG 421
|
....*....
gi 515712161 321 NIGELKNAI 329
Cdd:PRK10820 422 NVRQLKNAI 430
|
|
| glnG |
PRK10923 |
nitrogen regulation protein NR(I); Provisional |
66-279 |
3.09e-13 |
|
nitrogen regulation protein NR(I); Provisional
Pssm-ID: 182842 [Multi-domain] Cd Length: 469 Bit Score: 72.98 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 66 LEKLFSIH----LKEKEFTSKKEFVKALQPQEAKDFEKLIGAQESLANVVN----QCKATISyppnglpLLLYGPTGTGK 137
Cdd:PRK10923 102 LPKPFDIDeavaLVERAISHYQEQQQPRNIQVNGPTTDIIGEAPAMQDVFRiigrLSRSSIS-------VLINGESGTGK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 138 SFMAqlmyeYALNHQLIEADKKFLIVNCSeyANNPELLTANLFGHKKGAFTGADKDNPGLIKLAEGGVLFLDEVHCLPPE 217
Cdd:PRK10923 175 ELVA-----HALHRHSPRAKAPFIALNMA--AIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMPLD 247
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515712161 218 CQEKLFLFMDKGIYHMVGDNEKwYQSSLRLIFATTEKPEEVLLKTLLR-----RIPMI-ITIPSLEER 279
Cdd:PRK10923 248 VQTRLLRVLADGQFYRVGGYAP-VKVDVRIIAATHQNLEQRVQEGKFRedlfhRLNVIrVHLPPLRER 314
|
|
| PTS_IIA_man |
cd00006 |
PTS_IIA, PTS system, mannose/sorbose specific IIA subunit. The bacterial phosphoenolpyruvate: ... |
548-662 |
5.25e-11 |
|
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: 60.70 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 548 IGIIIA-HGfSTASSMADAANKLLGRYV-FDAMDMPLQLSSTQIIEQLNRYLAKIPQYEELFLLVDM--GSLEEIYKGLE 623
Cdd:cd00006 1 VGIIIAtHG-GFASGLLNSAEMILGEQEnVEAIDFPPGESPDDLLEKIKAALAELDSGEGVLILTDLfgGSPNNAAARLS 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 515712161 624 VSNASIGIMNNVTTRLALEIGQGIISNTPMKEIFETAVD 662
Cdd:cd00006 80 MEHPPVEVIAGVNLPMLLEAARARELGLSLDELVENALE 118
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
126-266 |
1.08e-08 |
|
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: 54.61 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 126 PLLLYGPTGTGKSFMAQLMyEYALNhqlieaDKKFLIVNCSEYANNPEL-----LTANLFGHKKGAFTGADKdnpglikl 200
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERL-AAALS------NRPVFYVQLTRDTTEEDLfgrrnIDPGGASWVDGPLVRAAR-------- 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 201 aEGGVLFLDEVHCLPPECQEKLFLFMDKGIYHMVGDNEKWY--QSSLRLIFATTEKPEEV--LLKTLLRR 266
Cdd:pfam07728 66 -EGEIAVLDEINRANPDVLNSLLSLLDERRLLLPDGGELVKaaPDGFRLIATMNPLDRGLneLSPALRSR 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
124-267 |
1.34e-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: 54.69 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 124 GLPLLLYGPTGTGKSFMAQlmyeyALNHQLIEADKKFLIVNCSEYANNPELLTANLFGHKKGAFTGADKDNPGLIKLAEG 203
Cdd:smart00382 2 GEVILIVGPPGSGKTTLAR-----ALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARK 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515712161 204 ---GVLFLDEVHCLPPECQEKLFLFMDkgiyHMVGDNEKWYQSSLRLIFATTekPEEVLLKTLLRRI 267
Cdd:smart00382 77 lkpDVLILDEITSLLDAEQEALLLLLE----ELRLLLLLKSEKNLTVILTTN--DEKDLGPALLRRR 137
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
127-274 |
9.66e-08 |
|
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: 51.44 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 127 LLLYGPTGTGKSFMAqlmyeYALNHqliEADKKFLIVNCSEyannpelLTANLFGHK----KGAFTGADKDNPgliklae 202
Cdd:pfam00004 1 LLLYGPPGTGKTTLA-----KAVAK---ELGAPFIEISGSE-------LVSKYVGESekrlRELFEAAKKLAP------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 203 gGVLFLDEVHCLPP-----------ECQEKLFLFMDkgiyhmvgdnekWYQSSLR--LIFATTEKPEEvLLKTLLRRIPM 269
Cdd:pfam00004 59 -CVIFIDEIDALAGsrgsggdsesrRVVNQLLTELD------------GFTSSNSkvIVIAATNRPDK-LDPALLGRFDR 124
|
....*
gi 515712161 270 IITIP 274
Cdd:pfam00004 125 IIEFP 129
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
97-230 |
3.03e-07 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 51.41 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 97 FEKLIG---AQESLANVVNQCKATISYPPNGLP-LLLYGPTGTGKSFMAQlmyeyALNHQLIEADKKFLIVNCSEYAnnp 172
Cdd:cd19499 10 HERVVGqdeAVKAVSDAIRRARAGLSDPNRPIGsFLFLGPTGVGKTELAK-----ALAELLFGDEDNLIRIDMSEYM--- 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515712161 173 ELLT-ANLFG--------HKKGAFTGADKDNPgliklaeGGVLFLDEVHCLPPECQEKLFLFMDKGI 230
Cdd:cd19499 82 EKHSvSRLIGappgyvgyTEGGQLTEAVRRKP-------YSVVLLDEIEKAHPDVQNLLLQVLDDGR 141
|
|
| BglG |
COG3711 |
Transcriptional antiterminator [Transcription]; |
771-899 |
2.77e-06 |
|
Transcriptional antiterminator [Transcription];
Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 51.01 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 771 YISDSEMK--TFQQNILKNFSLSNIMNNLTILN--PSKLLEHVADAIDKLQNDLQVRLTNNTCVGLYVHVCCLIERLVTR 846
Cdd:COG3711 140 KLEGSELDirKALAELLSELLSENDLLSLLLLKliPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKG 219
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 515712161 847 KSI----ETYTNVEDFAEKEIAfiksvKKAFSVVENYYSVEIPVEEIGYIFDYVKNN 899
Cdd:COG3711 220 KYIkldnPLLWEIKKPKEYEIA-----KEILKLIEERLGISLPEDEIGYIALHLLGA 271
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
127-273 |
3.48e-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: 44.97 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 127 LLLYGPTGTGKSFMAQlmyeyALNHqliEADKKFLIVNCSEYAnnpelltanlfghkkGAFTGADKDNPG-LIKLAE--- 202
Cdd:cd19481 29 ILLYGPPGTGKTLLAK-----ALAG---ELGLPLIVVKLSSLL---------------SKYVGESEKNLRkIFERARrla 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 203 GGVLFLDEVHCLP--------PECQE----KLFLFMDkGIYHMVGdnekwyqsslRLIFATTEKPEEvLLKTLLR--RIP 268
Cdd:cd19481 86 PCILFIDEIDAIGrkrdssgeSGELRrvlnQLLTELD-GVNSRSK----------VLVIAATNRPDL-LDPALLRpgRFD 153
|
....*
gi 515712161 269 MIITI 273
Cdd:cd19481 154 EVIEF 158
|
|
| PRD |
pfam00874 |
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ... |
811-892 |
4.59e-05 |
|
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: 43.01 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 811 DAIDKLQNDLQVRLTNNTCV-GLYVHVCCLIERLVTRKSIEtYTNVEDFAEKEIAFIKSVKKAFSVVENYYSVEIPVEEI 889
Cdd:pfam00874 2 EIIELIEKKLGITFDDDILYiRLILHLAFAIERIKEGITIE-NPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEI 80
|
...
gi 515712161 890 GYI 892
Cdd:pfam00874 81 GYI 83
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
121-337 |
6.06e-05 |
|
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: 46.44 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 121 PPNGLplLLYGPTGTGKSFMAQLMYEyalnhqliEADKKFLIVNCSE----YANNPELLTANLFghkkgaftgadkdnpg 196
Cdd:COG0464 190 PPRGL--LLYGPPGTGKTLLARALAG--------ELGLPLIEVDLSDlvskYVGETEKNLREVF---------------- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 197 liKLAEG---GVLFLDEVHclppecqeklFLFMDKGiyhmvGDNEKW--------------YQSSLrLIFATTEKPEEvL 259
Cdd:COG0464 244 --DKARGlapCVLFIDEAD----------ALAGKRG-----EVGDGVgrrvvntlltemeeLRSDV-VVIAATNRPDL-L 304
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515712161 260 LKTLLRRIPMIITIPSLEErgtHERLQLIHSIFAaeETRIHKSIYLSTLVYQtllstTFNANIGELKNAIQASCVNAL 337
Cdd:COG0464 305 DPALLRRFDEIIFFPLPDA---EERLEIFRIHLR--KRPLDEDVDLEELAEA-----TEGLSGADIRNVVRRAALQAL 372
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
127-227 |
1.82e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 42.33 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 127 LLLYGPTGTGKSFMAQLmyeyaLNHQLIEADKKFLIVNCSEYANNPELLT--ANLFGHKKGAFTGADKDNPGLIKLAEG- 203
Cdd:pfam13401 8 LVLTGESGTGKTTLLRR-----LLEQLPEVRDSVVFVDLPSGTSPKDLLRalLRALGLPLSGRLSKEELLAALQQLLLAl 82
|
90 100
....*....|....*....|....*..
gi 515712161 204 ---GVLFLDEVHCLPPECQEKLFLFMD 227
Cdd:pfam13401 83 avaVVLIIDEAQHLSLEALEELRDLLN 109
|
|
| DnaC |
COG1484 |
DNA replication protein DnaC [Replication, recombination and repair]; |
127-167 |
1.26e-03 |
|
DNA replication protein DnaC [Replication, recombination and repair];
Pssm-ID: 441093 [Multi-domain] Cd Length: 242 Bit Score: 41.30 E-value: 1.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 515712161 127 LLLYGPTGTGKSFMAQlmyeyALNHQLIEADKKFLIVNCSE 167
Cdd:COG1484 102 LILLGPPGTGKTHLAI-----ALGHEACRAGYRVRFTTAPD 137
|
|
| RecA-like_CDC48_r1-like |
cd19519 |
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ... |
121-217 |
2.69e-03 |
|
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410927 [Multi-domain] Cd Length: 166 Bit Score: 39.73 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515712161 121 PPNGLplLLYGPTGTGKSFMAQLMYEyalnhqliEADKKFLIVN----CSEYANNPElltANLfghkKGAFTGADKDNPG 196
Cdd:cd19519 33 PPRGI--LLYGPPGTGKTLIARAVAN--------ETGAFFFLINgpeiMSKLAGESE---SNL----RKAFEEAEKNAPA 95
|
90 100
....*....|....*....|.
gi 515712161 197 LIklaeggvlFLDEVHCLPPE 217
Cdd:cd19519 96 II--------FIDEIDAIAPK 108
|
|
| |
