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Conserved domains on  [gi|1308984715|gb|PKO90033|]
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secretion system protein E [Betaproteobacteria bacterium HGW-Betaproteobacteria-12]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PulE COG2804
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ...
173-742 0e+00

Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


:

Pssm-ID: 442055 [Multi-domain]  Cd Length: 561  Bit Score: 731.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 173 AATHRSRLGIVLHNKGALSAPQLQELTLLQERRKEPLIRLLLEKDWVPERRIREILRTDMLIEEVQLAEFRVDPALAELI 252
Cdd:COG2804     2 ALSLLLRLGDLLVEAGLISEEQLLAALAEQKKTGKPLGELLVELGLVTEELLAEALAEQLGLPFVDLDELEIDPEVLELL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 253 PHSFCVRQMVLPLRLDGKRLLLAMADPLDEGLIDEVRFTAGLDLTVVMADAEAIKRKIEAVYGGDGAVDfKELETLvsgv 332
Cdd:COG2804    82 PEELARRHRVLPLRLEGGTLTVAMADPLDLEALDELRRLTGRPVEPVVATESDIERALDRLYGSESSIE-ELLEEL---- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 333 dpyeGIEVVIEDDDitgLEDLLRETEAPPAIRLANAIILEAIRLGASDIHIQPRTKSVIVRYRIDGVLVDKIHIPHHLHH 412
Cdd:COG2804   157 ----AEDLTSEEED---LEDLLEEADDAPVVRLVNAILEDAIKEGASDIHIEPYEKRLRVRFRIDGVLREVLRLPKSLAP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 413 SLVSRLKIMSELDISERRRPQDGRITVKTPMRMVDLRISTLPTINGEKVVMRILDRNAAVQSLEGLGFPAADLTRIADMV 492
Cdd:COG2804   230 ALVSRIKIMANLDIAERRLPQDGRIKLRLGGREIDLRVSTLPTVYGEKVVLRILDKSAALLDLEQLGFSPDQLERLRRLI 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 493 AKPQGIILATGPTGSGKTTTLYSLLQHDATPGKNYITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDPDVILLG 572
Cdd:COG2804   310 RRPHGIILVTGPTGSGKTTTLYAALNELNTPERNIITVEDPVEYQLPGINQVQVNPKIGLTFASALRSILRQDPDVIMVG 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 573 EIRDFDTAEVAFHAALTGHQVFSTLHTNSAVATIARLFDLGMKPYVVASALEGIIAQRLVRKICAACSEPVAPDAELYRR 652
Cdd:COG2804   390 EIRDLETAEIAVQAALTGHLVLSTLHTNDAPSAITRLLDMGVEPFLLASSLLGVLAQRLVRRLCPHCKEPYEPDPEELER 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 653 LGPRFDPARPA--FRGKGCPTCHGLGYKGRVGVYEILTLDDELRDRIGGGASILEISRLIRHKGMRPIASHGAELVAAGR 730
Cdd:COG2804   470 LGLPPEELAPLtfYRGVGCEHCNGTGYKGRTGIYELLVIDDELRELIAEGASAAELREAARKEGMRTLREDGLEKVLQGI 549
                         570
                  ....*....|..
gi 1308984715 731 TTAEEILRVIGP 742
Cdd:COG2804   550 TTLEEVLRVTGE 561
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
27-144 1.45e-55

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


:

Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 185.68  E-value: 1.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  27 YRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTG 106
Cdd:cd17569     1 PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTG 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984715 107 HANTDAVMGAINEGAVYKFILKPWNDDDLRVTVALALE 144
Cdd:cd17569    81 YADLDAAIEAINEGEIYRFLTKPWDDEELKETIRQALE 118
 
Name Accession Description Interval E-value
PulE COG2804
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ...
173-742 0e+00

Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442055 [Multi-domain]  Cd Length: 561  Bit Score: 731.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 173 AATHRSRLGIVLHNKGALSAPQLQELTLLQERRKEPLIRLLLEKDWVPERRIREILRTDMLIEEVQLAEFRVDPALAELI 252
Cdd:COG2804     2 ALSLLLRLGDLLVEAGLISEEQLLAALAEQKKTGKPLGELLVELGLVTEELLAEALAEQLGLPFVDLDELEIDPEVLELL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 253 PHSFCVRQMVLPLRLDGKRLLLAMADPLDEGLIDEVRFTAGLDLTVVMADAEAIKRKIEAVYGGDGAVDfKELETLvsgv 332
Cdd:COG2804    82 PEELARRHRVLPLRLEGGTLTVAMADPLDLEALDELRRLTGRPVEPVVATESDIERALDRLYGSESSIE-ELLEEL---- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 333 dpyeGIEVVIEDDDitgLEDLLRETEAPPAIRLANAIILEAIRLGASDIHIQPRTKSVIVRYRIDGVLVDKIHIPHHLHH 412
Cdd:COG2804   157 ----AEDLTSEEED---LEDLLEEADDAPVVRLVNAILEDAIKEGASDIHIEPYEKRLRVRFRIDGVLREVLRLPKSLAP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 413 SLVSRLKIMSELDISERRRPQDGRITVKTPMRMVDLRISTLPTINGEKVVMRILDRNAAVQSLEGLGFPAADLTRIADMV 492
Cdd:COG2804   230 ALVSRIKIMANLDIAERRLPQDGRIKLRLGGREIDLRVSTLPTVYGEKVVLRILDKSAALLDLEQLGFSPDQLERLRRLI 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 493 AKPQGIILATGPTGSGKTTTLYSLLQHDATPGKNYITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDPDVILLG 572
Cdd:COG2804   310 RRPHGIILVTGPTGSGKTTTLYAALNELNTPERNIITVEDPVEYQLPGINQVQVNPKIGLTFASALRSILRQDPDVIMVG 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 573 EIRDFDTAEVAFHAALTGHQVFSTLHTNSAVATIARLFDLGMKPYVVASALEGIIAQRLVRKICAACSEPVAPDAELYRR 652
Cdd:COG2804   390 EIRDLETAEIAVQAALTGHLVLSTLHTNDAPSAITRLLDMGVEPFLLASSLLGVLAQRLVRRLCPHCKEPYEPDPEELER 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 653 LGPRFDPARPA--FRGKGCPTCHGLGYKGRVGVYEILTLDDELRDRIGGGASILEISRLIRHKGMRPIASHGAELVAAGR 730
Cdd:COG2804   470 LGLPPEELAPLtfYRGVGCEHCNGTGYKGRTGIYELLVIDDELRELIAEGASAAELREAARKEGMRTLREDGLEKVLQGI 549
                         570
                  ....*....|..
gi 1308984715 731 TTAEEILRVIGP 742
Cdd:COG2804   550 TTLEEVLRVTGE 561
type_II_gspE TIGR02533
type II secretion system protein E; This family describes GspE, the E protein of the type II ...
252-739 7.48e-176

type II secretion system protein E; This family describes GspE, the E protein of the type II secretion system, also called the main terminal branch of the general secretion pathway. This model separates GspE from the PilB protein of type IV pilin biosynthesis. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 131585 [Multi-domain]  Cd Length: 486  Bit Score: 512.69  E-value: 7.48e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 252 IPHSFCVRQMVLPLRLDGKRLLLAMADPLDEGLIDEVRFTAGLDLTVVMADAEAIKRKIEAVYGGDGAvdfkELETLVSG 331
Cdd:TIGR02533   4 LPIGFAKQSRVLPLSEHDGTLVVAVSDPLDLAALDEVRRLFGAPVQLIIATASEIDDAINSVYARTGS----AAAQIVEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 332 VDPYEGIEVVIEDDDItgLEDLLRETEAPPAIRLANAIILEAIRLGASDIHIQPRTKSVIVRYRIDGVLVDKIHIPHHLH 411
Cdd:TIGR02533  80 IEGEDDLSALELDEPK--IEDLLDLEDDAPVIRLVNSLLSRAVKERASDIHIEPFEKALVVRFRVDGVLRDVLSPPKKLH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 412 HSLVSRLKIMSELDISERRRPQDGRITVKTPMRMVDLRISTLPTINGEKVVMRILDRNAAVQSLEGLGFPAADLTRIADM 491
Cdd:TIGR02533 158 AALVSRVKIMAKLNIAEKRLPQDGRISLRVGGRDIDIRVSTVPTSHGERVVMRLLDKTAVRLDLETLGMSPELLSRFERL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 492 VAKPQGIILATGPTGSGKTTTLYSLLQHDATPGKNYITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDPDVILL 571
Cdd:TIGR02533 238 IRRPHGIILVTGPTGSGKTTTLYAALSRLNTPERNILTVEDPVEYQIEGIGQIQVNPKIGLTFAAGLRAILRQDPDIIMV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 572 GEIRDFDTAEVAFHAALTGHQVFSTLHTNSAVATIARLFDLGMKPYVVASALEGIIAQRLVRKICAACSEPVAPDAELYR 651
Cdd:TIGR02533 318 GEIRDLETAQIAIQASLTGHLVLSTLHTNDAAGAVTRLIDMGVEPFLLASSLLGVLAQRLVRRLCPHCKEPYEATPEEIA 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 652 RLGPRFDPARPAFRGKGCPTCHGLGYKGRVGVYEILTLDDELRDRIGGGASILEISRLIRHKGMRPIASHGAELVAAGRT 731
Cdd:TIGR02533 398 LFGISPEGPINLYRPVGCPHCNHTGYLGRTGIYELLIVDDDLRSLIHSRADEGEIKEIARAAGMRTLRDDGLRKVLAGIT 477

                  ....*...
gi 1308984715 732 TAEEILRV 739
Cdd:TIGR02533 478 TIEEVLRV 485
PRK10436 PRK10436
hypothetical protein; Provisional
254-741 1.56e-130

hypothetical protein; Provisional


Pssm-ID: 236694  Cd Length: 462  Bit Score: 395.45  E-value: 1.56e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 254 HSFCVRQMVLPLRLDGKRLLLAMADPLDEGLIDEVRFTAGLDLTVVMADAEaikrKIEavyggdgavdfKELETLVSGVD 333
Cdd:PRK10436   10 HALCQRYQAVLLDSDEETLHVAVVDAPSHELLDALRFATGKRIEIECWPRA----QME-----------QHLQRTQQTLP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 334 PYEgievviEDDDitgledllreteaPPAIRLANAIILEAIRLGASDIHIQPRTKSVIVRYRIDGVLVDKIHIPHHLHHS 413
Cdd:PRK10436   75 VAD------QEKD-------------TPVAQLINQTLQSALQKRASDIHFEPAQNHYRIRLRIDGVLHPLPDPSPELGAA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 414 LVSRLKIMSELDISERRRPQDGRITVKTPMRMVDLRISTLPTINGEKVVMRILDRNAAVQSLEGLGFPAADLTRIADMVA 493
Cdd:PRK10436  136 LTARLKVLGNLDIAERRLPQDGQFTVELAGNAYSFRIATLPCRGGEKVVLRLLQQVQQALDLETLGMTPAQLAQFRQALQ 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 494 KPQGIILATGPTGSGKTTTLYSLLQHDATPGKNYITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDPDVILLGE 573
Cdd:PRK10436  216 QPQGLILVTGPTGSGKTVTLYSALQTLNTAQINICSVEDPVEIPLAGINQTQIHPKAGLTFQRVLRALLRQDPDVIMVGE 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 574 IRDFDTAEVAFHAALTGHQVFSTLHTNSAVATIARLFDLGMKPYVVASALEGIIAQRLVRKICAACSEPVAPDAELYRRL 653
Cdd:PRK10436  296 IRDGETAEIAIKAAQTGHLVLSTLHTNSTSETLVRLQQMGIARWMLASALKLVIAQRLVRKLCPHCRQQASEPIHLPPNI 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 654 GPRFdpaRPAFRGKGCPTCHGlGYKGRVGVYEILTLDDELRDRIGGGASILEISRLIRHKGMRPIASHGAELVAAGRTTA 733
Cdd:PRK10436  376 WPGP---LPHWQAVGCEHCYH-GYYGRTALFEVLPITPVLQQAIASNASPEELETHARQQGMTTLFENGLLAVEQGLTTL 451

                  ....*...
gi 1308984715 734 EEILRVIG 741
Cdd:PRK10436  452 EELYRVLG 459
T2SSE pfam00437
Type II/IV secretion system protein; This family contains components of both the Type II ...
367-634 3.58e-105

Type II/IV secretion system protein; This family contains components of both the Type II protein secretion system (T2SS), including Type 4 pilus (T4P), and Type IV protein secretion system (T4SS) from Gram-negative bacteria. VirB11 ATPase is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) transfer system, a type IV secretion pathway required for delivery of T-DNA and effector proteins to plant cells during infection. The cytoplasmic T2S E ATPase is a Zn-containing protein thought to provide the mechanical force for the secretion process. T2S-E contains Walker A and B motifs, that are essential for secretion and ATPase activity. ATPase PulE and XcpR from Klebsiella oxytoca and Pseudomonas aeruginosa respectively are required for protein secretion via the T2SS. ATPase PilB is required for T4P extension.


Pssm-ID: 425681 [Multi-domain]  Cd Length: 269  Bit Score: 322.31  E-value: 3.58e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 367 NAIILEAIRLGASDIHIQPRTKSVIVRYRIDGVLVDKIHIPHHLHHSLVSRLKIMSELDISERRRPQDGRITVKTPMRMV 446
Cdd:pfam00437   1 NLIPLEALDEGASDIHVEPPERIVWIRFRVDGVLREIPFPDADALARLISRIKVMARLDISERRPPQDGRLPLRIGGKGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 447 DLRISTLPTINGEKVVMRILDRNAAVQSLEGLGFPAADLTRIADMVAKPQGIILATGPTGSGKTTTLYSLLQHDATPGKN 526
Cdd:pfam00437  81 RVRVSTLPTAGGEKLVIRLLDPSNVALSLDELGMTGAQDEALLEFLRQPRGNILVTGPTGSGKTTTLYAALGELNTRDEN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 527 YITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDPDVILLGEIRDFDTAEVAFHAALTGHQVFSTLHTNSAVATI 606
Cdd:pfam00437 161 IVTVEDPVEIQLEGINQVQLNARAGVTFADLLRAILRQDPDRIMVGEIRDLETAEIALQAANTGHLVLSTLHTNSAAGAL 240
                         250       260
                  ....*....|....*....|....*...
gi 1308984715 607 ARLFDLGMKPYVVASALEGIIAQRLVRK 634
Cdd:pfam00437 241 TRLQDMGVPPFELASSLLLVIAQRLVRK 268
ATPase_ComGA NF041000
competence type IV pilus ATPase ComGA;
367-632 8.90e-93

competence type IV pilus ATPase ComGA;


Pssm-ID: 468930 [Multi-domain]  Cd Length: 265  Bit Score: 290.12  E-value: 8.90e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 367 NAIILEAIRLGASDIHIQPRTKSVIVRYRIDGVLVDKIHIPHHLHHSLVSRLKIMSELDISERRRPQDGRITVKTPMRMV 446
Cdd:NF041000    1 EELIEEAIELRASDIHFLPREDGYQIKFRIGGGLIPYRELSLEEGQRLISYFKFLAGMDIGEKRRPQSGAFTYELNEQQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 447 DLRISTLPTING-EKVVMRILDRNAAVQSLEglgFPAADLTRIADMVAKPQGIILATGPTGSGKTTTLYSLLqHDATPGK 525
Cdd:NF041000   81 SLRLSTVGDFLGrESLVIRLLYQLEQIKPQL---FFPEQFQLLKQLLQRRSGLILFSGPTGSGKTTTMYSLA-RKLALNK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 526 NYITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDPDVILLGEIRDFDTAEVAFHAALTGHQVFSTLHTNSAVAT 605
Cdd:NF041000  157 QVITIEDPVEIKEPNFLQLQVNEKAGMTYDTLLKAALRHRPDILIIGEIRDAETAKAAIRAALTGHLVLSTVHAKSAAGV 236
                         250       260
                  ....*....|....*....|....*..
gi 1308984715 606 IARLFDLGMKPYVVASALEGIIAQRLV 632
Cdd:NF041000  237 IYRLLELGISKEELEQTLIGISYQRLI 263
PulE-GspE-like cd01129
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ...
487-635 5.36e-74

PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II secretory pathway, the main terminal branch of the general secretory pathway (GSP). PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PilB, a type IV pilus assembly ATPase, DotB, an ATPase of the type IVb secretion system, also known as the dot/icm system, Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ, and HofB.


Pssm-ID: 410873 [Multi-domain]  Cd Length: 159  Bit Score: 236.61  E-value: 5.36e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 487 RIADMVAKPQGIILATGPTGSGKTTTLYSLLQHDATPGKNYITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDP 566
Cdd:cd01129     2 RLRRLIKRPHGLILVTGPTGSGKTTTLYAMLRELNGPERNIITIEDPVEYQIPGINQSQVNEKIGLTFADALRAILRQDP 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308984715 567 DVILLGEIRDFDTAEVAFHAALTGHQVFSTLHTNSAVATIARLFDLGMKPYVVASALEGIIAQRLVRKI 635
Cdd:cd01129    82 DIIMVGEIRDAETAEIAIRAALTGHLVLSTLHTNDALGAITRLLDMGIEPFLLASALRGVIAQRLVGRT 150
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
27-144 1.45e-55

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 185.68  E-value: 1.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  27 YRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTG 106
Cdd:cd17569     1 PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTG 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984715 107 HANTDAVMGAINEGAVYKFILKPWNDDDLRVTVALALE 144
Cdd:cd17569    81 YADLDAAIEAINEGEIYRFLTKPWDDEELKETIRQALE 118
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
28-180 1.17e-33

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: 133.94  E-value: 1.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGH 107
Cdd:COG2204     4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGY 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308984715 108 ANTDAVMGAINEGAvYKFILKPWNDDDLRVTVALALERFDLIARNRA---LKSENEKKSKEISALAKLAATHRSRL 180
Cdd:COG2204    84 GDVETAVEAIKAGA-FDYLTKPFDLEELLAAVERALERRRLRRENAEdsgLIGRSPAMQEVRRLIEKVAPSDATVL 158
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
30-140 5.53e-25

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 99.92  E-value: 5.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHAN 109
Cdd:pfam00072   2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHGD 81
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308984715 110 TDAVMGAINEGAVYkFILKPWNDDDLRVTVA 140
Cdd:pfam00072  82 EDDAVEALEAGADD-FLSKPFDPDELLAAIR 111
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
25-158 2.56e-20

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 94.53  E-value: 2.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  25 PRYRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIML 104
Cdd:PRK11361    3 AINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILM 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1308984715 105 TGHANTDAVMGAINEGAvYKFILKPWNDDDLRVTVALALERFDLIARNRALKSE 158
Cdd:PRK11361   83 TAYAEVETAVEALRCGA-FDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQA 135
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
27-81 2.84e-10

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 56.04  E-value: 2.84e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1308984715   27 YRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMP 81
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
495-574 4.00e-03

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: 38.51  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  495 PQGIILATGPTGSGKTTTLYSLLQHDATPGKN--YITIEDPVEYYLDMAGQVLVREKIGLTFPA-----VLRAILRQDPD 567
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGviYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrlALALARKLKPD 80

                   ....*..
gi 1308984715  568 VILLGEI 574
Cdd:smart00382  81 VLILDEI 87
 
Name Accession Description Interval E-value
PulE COG2804
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ...
173-742 0e+00

Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442055 [Multi-domain]  Cd Length: 561  Bit Score: 731.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 173 AATHRSRLGIVLHNKGALSAPQLQELTLLQERRKEPLIRLLLEKDWVPERRIREILRTDMLIEEVQLAEFRVDPALAELI 252
Cdd:COG2804     2 ALSLLLRLGDLLVEAGLISEEQLLAALAEQKKTGKPLGELLVELGLVTEELLAEALAEQLGLPFVDLDELEIDPEVLELL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 253 PHSFCVRQMVLPLRLDGKRLLLAMADPLDEGLIDEVRFTAGLDLTVVMADAEAIKRKIEAVYGGDGAVDfKELETLvsgv 332
Cdd:COG2804    82 PEELARRHRVLPLRLEGGTLTVAMADPLDLEALDELRRLTGRPVEPVVATESDIERALDRLYGSESSIE-ELLEEL---- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 333 dpyeGIEVVIEDDDitgLEDLLRETEAPPAIRLANAIILEAIRLGASDIHIQPRTKSVIVRYRIDGVLVDKIHIPHHLHH 412
Cdd:COG2804   157 ----AEDLTSEEED---LEDLLEEADDAPVVRLVNAILEDAIKEGASDIHIEPYEKRLRVRFRIDGVLREVLRLPKSLAP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 413 SLVSRLKIMSELDISERRRPQDGRITVKTPMRMVDLRISTLPTINGEKVVMRILDRNAAVQSLEGLGFPAADLTRIADMV 492
Cdd:COG2804   230 ALVSRIKIMANLDIAERRLPQDGRIKLRLGGREIDLRVSTLPTVYGEKVVLRILDKSAALLDLEQLGFSPDQLERLRRLI 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 493 AKPQGIILATGPTGSGKTTTLYSLLQHDATPGKNYITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDPDVILLG 572
Cdd:COG2804   310 RRPHGIILVTGPTGSGKTTTLYAALNELNTPERNIITVEDPVEYQLPGINQVQVNPKIGLTFASALRSILRQDPDVIMVG 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 573 EIRDFDTAEVAFHAALTGHQVFSTLHTNSAVATIARLFDLGMKPYVVASALEGIIAQRLVRKICAACSEPVAPDAELYRR 652
Cdd:COG2804   390 EIRDLETAEIAVQAALTGHLVLSTLHTNDAPSAITRLLDMGVEPFLLASSLLGVLAQRLVRRLCPHCKEPYEPDPEELER 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 653 LGPRFDPARPA--FRGKGCPTCHGLGYKGRVGVYEILTLDDELRDRIGGGASILEISRLIRHKGMRPIASHGAELVAAGR 730
Cdd:COG2804   470 LGLPPEELAPLtfYRGVGCEHCNGTGYKGRTGIYELLVIDDELRELIAEGASAAELREAARKEGMRTLREDGLEKVLQGI 549
                         570
                  ....*....|..
gi 1308984715 731 TTAEEILRVIGP 742
Cdd:COG2804   550 TTLEEVLRVTGE 561
type_II_gspE TIGR02533
type II secretion system protein E; This family describes GspE, the E protein of the type II ...
252-739 7.48e-176

type II secretion system protein E; This family describes GspE, the E protein of the type II secretion system, also called the main terminal branch of the general secretion pathway. This model separates GspE from the PilB protein of type IV pilin biosynthesis. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 131585 [Multi-domain]  Cd Length: 486  Bit Score: 512.69  E-value: 7.48e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 252 IPHSFCVRQMVLPLRLDGKRLLLAMADPLDEGLIDEVRFTAGLDLTVVMADAEAIKRKIEAVYGGDGAvdfkELETLVSG 331
Cdd:TIGR02533   4 LPIGFAKQSRVLPLSEHDGTLVVAVSDPLDLAALDEVRRLFGAPVQLIIATASEIDDAINSVYARTGS----AAAQIVEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 332 VDPYEGIEVVIEDDDItgLEDLLRETEAPPAIRLANAIILEAIRLGASDIHIQPRTKSVIVRYRIDGVLVDKIHIPHHLH 411
Cdd:TIGR02533  80 IEGEDDLSALELDEPK--IEDLLDLEDDAPVIRLVNSLLSRAVKERASDIHIEPFEKALVVRFRVDGVLRDVLSPPKKLH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 412 HSLVSRLKIMSELDISERRRPQDGRITVKTPMRMVDLRISTLPTINGEKVVMRILDRNAAVQSLEGLGFPAADLTRIADM 491
Cdd:TIGR02533 158 AALVSRVKIMAKLNIAEKRLPQDGRISLRVGGRDIDIRVSTVPTSHGERVVMRLLDKTAVRLDLETLGMSPELLSRFERL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 492 VAKPQGIILATGPTGSGKTTTLYSLLQHDATPGKNYITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDPDVILL 571
Cdd:TIGR02533 238 IRRPHGIILVTGPTGSGKTTTLYAALSRLNTPERNILTVEDPVEYQIEGIGQIQVNPKIGLTFAAGLRAILRQDPDIIMV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 572 GEIRDFDTAEVAFHAALTGHQVFSTLHTNSAVATIARLFDLGMKPYVVASALEGIIAQRLVRKICAACSEPVAPDAELYR 651
Cdd:TIGR02533 318 GEIRDLETAQIAIQASLTGHLVLSTLHTNDAAGAVTRLIDMGVEPFLLASSLLGVLAQRLVRRLCPHCKEPYEATPEEIA 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 652 RLGPRFDPARPAFRGKGCPTCHGLGYKGRVGVYEILTLDDELRDRIGGGASILEISRLIRHKGMRPIASHGAELVAAGRT 731
Cdd:TIGR02533 398 LFGISPEGPINLYRPVGCPHCNHTGYLGRTGIYELLIVDDDLRSLIHSRADEGEIKEIARAAGMRTLRDDGLRKVLAGIT 477

                  ....*...
gi 1308984715 732 TAEEILRV 739
Cdd:TIGR02533 478 TIEEVLRV 485
type_IV_pilB TIGR02538
type IV-A pilus assembly ATPase PilB; This model describes a protein of type IV pilus ...
179-739 1.14e-169

type IV-A pilus assembly ATPase PilB; This model describes a protein of type IV pilus biogenesis designated PilB in Pseudomonas aeruginosa but PilF in Neisseria gonorrhoeae; the more common usage, reflected here, is PilB. This protein is an ATPase involved in protein export for pilin assembly and is closely related to GspE (TIGR02533) of type II secretion, also called the main terminal branch of the general secretion pathway. Note that type IV pilus systems are often divided into type IV-A and IV-B, with the latter group including bundle-forming pilus, mannose-sensitive hemagglutinin, etc. Members of this family are found in type IV-A systems. [Cell envelope, Surface structures, Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274186 [Multi-domain]  Cd Length: 564  Bit Score: 499.54  E-value: 1.14e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 179 RLGIVLHNKGALSAPQLQELTLLQERRKEPLIRLLLEKDWVPERRIREILRTDMLIEEVQLAEFRVDPALAELIPHSFCV 258
Cdd:TIGR02538   1 GLGRILVKAGLLTETQAQAALEEAQASGQPLVQYLIQNGLLDPKQLAEFLSREFGVPLLDLNAFDPDALPVQLVSEELIQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 259 RQMVLPLRLDGKRLLLAMADPLDEGLIDEVRFTAGLDLTVVMADAEAIKRKIEAVYGGDGAVDfKELETLVSGVDpyEGI 338
Cdd:TIGR02538  81 KHQALPLFKRGNTLFVAVSDPTNISALDDIRFATGLNVEVVIVEEDKLSALIEKYYGGSDSLA-KELGDEDIGDL--EEL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 339 EVVIEDDDITGLEDLLRETEAPPAIRLANAIILEAIRLGASDIHIQPRTKSVIVRYRIDGVLVDKIHIPHHLHHSLVSRL 418
Cdd:TIGR02538 158 DVDAIDDEGPDDIEQDAVDDDAPIVKFVNKILLDAIRKGASDIHFEPYEKSYRVRFRIDGILHEVAQPPLALANRIAARI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 419 KIMSELDISERRRPQDGRITVKTPM-RMVDLRISTLPTINGEKVVMRILDRNAAVQSLEGLGFPAADLTRIADMVAKPQG 497
Cdd:TIGR02538 238 KVMSRLDIAEKRIPQDGRIKLKLSKsKAIDFRVSTLPTLFGEKVVLRILDSSAAQLDIDKLGFEPDQKALFLEAIHKPQG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 498 IILATGPTGSGKTTTLYSLLQHDATPGKNYITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDPDVILLGEIRDF 577
Cdd:TIGR02538 318 MVLVTGPTGSGKTVSLYTALNILNTEEVNISTAEDPVEINLPGINQVNVNPKIGLTFAAALRSFLRQDPDIIMVGEIRDL 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 578 DTAEVAFHAALTGHQVFSTLHTNSAVATIARLFDLGMKPYVVASALEGIIAQRLVRKICAACSEPVAPDAELYRRLGprF 657
Cdd:TIGR02538 398 ETAEIAIKAAQTGHLVLSTLHTNDAPETLARLVNMGIAPFNIASSVNLIMAQRLARRLCSHCKAPEEVPAEALLELG--F 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 658 DPARPA----FRGKGCPTCHGLGYKGRVGVYEILTLDDELRDRIGGGASILEISRLIRHKGMRPIASHGAELVAAGRTTA 733
Cdd:TIGR02538 476 TQEDLAdlklYGPVGCDECSNTGYKGRVGIYEVMPMSEEIAELILKGGNALQIAELAQKEGMRTLRRSGLLKVKQGVTSL 555

                  ....*.
gi 1308984715 734 EEILRV 739
Cdd:TIGR02538 556 EEVLRV 561
PRK10436 PRK10436
hypothetical protein; Provisional
254-741 1.56e-130

hypothetical protein; Provisional


Pssm-ID: 236694  Cd Length: 462  Bit Score: 395.45  E-value: 1.56e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 254 HSFCVRQMVLPLRLDGKRLLLAMADPLDEGLIDEVRFTAGLDLTVVMADAEaikrKIEavyggdgavdfKELETLVSGVD 333
Cdd:PRK10436   10 HALCQRYQAVLLDSDEETLHVAVVDAPSHELLDALRFATGKRIEIECWPRA----QME-----------QHLQRTQQTLP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 334 PYEgievviEDDDitgledllreteaPPAIRLANAIILEAIRLGASDIHIQPRTKSVIVRYRIDGVLVDKIHIPHHLHHS 413
Cdd:PRK10436   75 VAD------QEKD-------------TPVAQLINQTLQSALQKRASDIHFEPAQNHYRIRLRIDGVLHPLPDPSPELGAA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 414 LVSRLKIMSELDISERRRPQDGRITVKTPMRMVDLRISTLPTINGEKVVMRILDRNAAVQSLEGLGFPAADLTRIADMVA 493
Cdd:PRK10436  136 LTARLKVLGNLDIAERRLPQDGQFTVELAGNAYSFRIATLPCRGGEKVVLRLLQQVQQALDLETLGMTPAQLAQFRQALQ 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 494 KPQGIILATGPTGSGKTTTLYSLLQHDATPGKNYITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDPDVILLGE 573
Cdd:PRK10436  216 QPQGLILVTGPTGSGKTVTLYSALQTLNTAQINICSVEDPVEIPLAGINQTQIHPKAGLTFQRVLRALLRQDPDVIMVGE 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 574 IRDFDTAEVAFHAALTGHQVFSTLHTNSAVATIARLFDLGMKPYVVASALEGIIAQRLVRKICAACSEPVAPDAELYRRL 653
Cdd:PRK10436  296 IRDGETAEIAIKAAQTGHLVLSTLHTNSTSETLVRLQQMGIARWMLASALKLVIAQRLVRKLCPHCRQQASEPIHLPPNI 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 654 GPRFdpaRPAFRGKGCPTCHGlGYKGRVGVYEILTLDDELRDRIGGGASILEISRLIRHKGMRPIASHGAELVAAGRTTA 733
Cdd:PRK10436  376 WPGP---LPHWQAVGCEHCYH-GYYGRTALFEVLPITPVLQQAIASNASPEELETHARQQGMTTLFENGLLAVEQGLTTL 451

                  ....*...
gi 1308984715 734 EEILRVIG 741
Cdd:PRK10436  452 EELYRVLG 459
T2SSE pfam00437
Type II/IV secretion system protein; This family contains components of both the Type II ...
367-634 3.58e-105

Type II/IV secretion system protein; This family contains components of both the Type II protein secretion system (T2SS), including Type 4 pilus (T4P), and Type IV protein secretion system (T4SS) from Gram-negative bacteria. VirB11 ATPase is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) transfer system, a type IV secretion pathway required for delivery of T-DNA and effector proteins to plant cells during infection. The cytoplasmic T2S E ATPase is a Zn-containing protein thought to provide the mechanical force for the secretion process. T2S-E contains Walker A and B motifs, that are essential for secretion and ATPase activity. ATPase PulE and XcpR from Klebsiella oxytoca and Pseudomonas aeruginosa respectively are required for protein secretion via the T2SS. ATPase PilB is required for T4P extension.


Pssm-ID: 425681 [Multi-domain]  Cd Length: 269  Bit Score: 322.31  E-value: 3.58e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 367 NAIILEAIRLGASDIHIQPRTKSVIVRYRIDGVLVDKIHIPHHLHHSLVSRLKIMSELDISERRRPQDGRITVKTPMRMV 446
Cdd:pfam00437   1 NLIPLEALDEGASDIHVEPPERIVWIRFRVDGVLREIPFPDADALARLISRIKVMARLDISERRPPQDGRLPLRIGGKGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 447 DLRISTLPTINGEKVVMRILDRNAAVQSLEGLGFPAADLTRIADMVAKPQGIILATGPTGSGKTTTLYSLLQHDATPGKN 526
Cdd:pfam00437  81 RVRVSTLPTAGGEKLVIRLLDPSNVALSLDELGMTGAQDEALLEFLRQPRGNILVTGPTGSGKTTTLYAALGELNTRDEN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 527 YITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDPDVILLGEIRDFDTAEVAFHAALTGHQVFSTLHTNSAVATI 606
Cdd:pfam00437 161 IVTVEDPVEIQLEGINQVQLNARAGVTFADLLRAILRQDPDRIMVGEIRDLETAEIALQAANTGHLVLSTLHTNSAAGAL 240
                         250       260
                  ....*....|....*....|....*...
gi 1308984715 607 ARLFDLGMKPYVVASALEGIIAQRLVRK 634
Cdd:pfam00437 241 TRLQDMGVPPFELASSLLLVIAQRLVRK 268
ATPase_ComGA NF041000
competence type IV pilus ATPase ComGA;
367-632 8.90e-93

competence type IV pilus ATPase ComGA;


Pssm-ID: 468930 [Multi-domain]  Cd Length: 265  Bit Score: 290.12  E-value: 8.90e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 367 NAIILEAIRLGASDIHIQPRTKSVIVRYRIDGVLVDKIHIPHHLHHSLVSRLKIMSELDISERRRPQDGRITVKTPMRMV 446
Cdd:NF041000    1 EELIEEAIELRASDIHFLPREDGYQIKFRIGGGLIPYRELSLEEGQRLISYFKFLAGMDIGEKRRPQSGAFTYELNEQQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 447 DLRISTLPTING-EKVVMRILDRNAAVQSLEglgFPAADLTRIADMVAKPQGIILATGPTGSGKTTTLYSLLqHDATPGK 525
Cdd:NF041000   81 SLRLSTVGDFLGrESLVIRLLYQLEQIKPQL---FFPEQFQLLKQLLQRRSGLILFSGPTGSGKTTTMYSLA-RKLALNK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 526 NYITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDPDVILLGEIRDFDTAEVAFHAALTGHQVFSTLHTNSAVAT 605
Cdd:NF041000  157 QVITIEDPVEIKEPNFLQLQVNEKAGMTYDTLLKAALRHRPDILIIGEIRDAETAKAAIRAALTGHLVLSTVHAKSAAGV 236
                         250       260
                  ....*....|....*....|....*..
gi 1308984715 606 IARLFDLGMKPYVVASALEGIIAQRLV 632
Cdd:NF041000  237 IYRLLELGISKEELEQTLIGISYQRLI 263
PulE-GspE-like cd01129
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ...
487-635 5.36e-74

PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II secretory pathway, the main terminal branch of the general secretory pathway (GSP). PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PilB, a type IV pilus assembly ATPase, DotB, an ATPase of the type IVb secretion system, also known as the dot/icm system, Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ, and HofB.


Pssm-ID: 410873 [Multi-domain]  Cd Length: 159  Bit Score: 236.61  E-value: 5.36e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 487 RIADMVAKPQGIILATGPTGSGKTTTLYSLLQHDATPGKNYITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDP 566
Cdd:cd01129     2 RLRRLIKRPHGLILVTGPTGSGKTTTLYAMLRELNGPERNIITIEDPVEYQIPGINQSQVNEKIGLTFADALRAILRQDP 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308984715 567 DVILLGEIRDFDTAEVAFHAALTGHQVFSTLHTNSAVATIARLFDLGMKPYVVASALEGIIAQRLVRKI 635
Cdd:cd01129    82 DIIMVGEIRDAETAEIAIRAALTGHLVLSTLHTNDALGAITRLLDMGIEPFLLASALRGVIAQRLVGRT 150
PilT COG2805
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ...
367-738 1.66e-66

Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];


Pssm-ID: 442056  Cd Length: 342  Bit Score: 223.43  E-value: 1.66e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 367 NAIILEAIRLGASDIHIQPRTKsviVRYRIDGVLVdKIHIPHHLHHSLVSRLKIMseldISERRRPQ-------DGRITV 439
Cdd:COG2805     6 DELLKLAVEQGASDLHLTVGSP---PMLRIDGELV-PLDDPPLTPEDLEALLKEI----LTEEQRERleeegelDFSYSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 440 KTPMRmvdLRISTLPTINGEKVVMRILdrNAAVQSLEGLGFPAAdltrIADMVAKPQGIILATGPTGSGKTTTLYSLLQH 519
Cdd:COG2805    78 PGLGR---FRVNIFRQRGGVAAVLRLI--PSEIPTLEELGLPPV----LKELAELPRGLVLVTGPTGSGKSTTLAAMIDY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 520 -DATPGKNYITIEDPVEYYLDmAGQVLV--REkIG---LTFPAVLRAILRQDPDVILLGEIRDFDTAEVAFHAALTGHQV 593
Cdd:COG2805   149 iNETRAKHIITIEDPIEFVHK-HKKSLInqRE-VGrdtPSFANALRAALREDPDVILVGEMRDLETIEAALTAAETGHLV 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 594 FSTLHTNSAVATIARLFDL---GMKPYV---VASALEGIIAQRLVrkicaacsepvapdaelyrrlgprfdparpafrgk 667
Cdd:COG2805   227 FATLHTNSAAQTIDRIIDVfppEEQAQIrsqLAESLRGVISQRLL----------------------------------- 271
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308984715 668 gcPTCHGlgyKGRVGVYEILTLDDELRDRIGGGAsILEISRLI---RHKGMRPIASHGAELVAAGRTTAEEILR 738
Cdd:COG2805   272 --PRADG---GGRVAAREILVNTPAVRNLIREGK-THQIPSLIqtgKKLGMQTMDQSLAELVKEGLITEETALA 339
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
27-144 1.45e-55

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 185.68  E-value: 1.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  27 YRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTG 106
Cdd:cd17569     1 PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTG 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984715 107 HANTDAVMGAINEGAVYKFILKPWNDDDLRVTVALALE 144
Cdd:cd17569    81 YADLDAAIEAINEGEIYRFLTKPWDDEELKETIRQALE 118
pilT_fam TIGR01420
pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to ...
367-737 1.22e-49

pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to GspE, a protein involved in type II secretion (also called the General Secretion Pathway). PilT is an apparent cytosolic ATPase associated with type IV pilus systems. It is not required for pilin biogenesis, but is required for twitching motility and social gliding behaviors, shown in some species, powered by pilus retraction. Members of this family may be found in some species that type IV pili but have related structures for DNA uptake and natural transformation. [Cell envelope, Surface structures, Cellular processes, Chemotaxis and motility]


Pssm-ID: 273613  Cd Length: 343  Bit Score: 177.51  E-value: 1.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 367 NAIILEAIRLGASDIHIQPRTKsviVRYRIDGVLVDKIHIPHHLHHSLVSRLKIMSE--LDISERRRPQDGRITVKTPMR 444
Cdd:TIGR01420   3 EEILREAVKLGASDIHLTAGAP---PAMRIDGDLVRIEFEPLTPEDTQKLAREILSEkqREEFEENGELDFSFSLPGVGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 445 mvdLRISTLPTINGEKVVMRILDrnAAVQSLEGLGFPaadlTRIADMVAKPQGIILATGPTGSGKTTTLYSLLQH-DATP 523
Cdd:TIGR01420  80 ---FRVNAFYQRGGVALVLRLIP--SKIPTFEELGLP----PVLRELAERPRGLILVTGPTGSGKSTTLASMIDYiNKNK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 524 GKNYITIEDPVEY-YLDMAGQVLVREkIG---LTFPAVLRAILRQDPDVILLGEIRDFDTAEVAFHAALTGHQVFSTLHT 599
Cdd:TIGR01420 151 AYHIITIEDPIEYvHTNKRSLINQRE-VGedtLSFANALRAALREDPDVILIGEMRDLETVELALTAAETGHLVFGTLHT 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 600 NSAVATIARL---FDLGMKPYV---VASALEGIIAQRLVRKIcaacsepvapdaelyrrlgprfdparpafrgkgcptch 673
Cdd:TIGR01420 230 NSAAQTIERIidvFPAEEQEQIrtqLAESLVAIISQRLLPKA-------------------------------------- 271
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308984715 674 glGYKGRVGVYEILTLDDELRDRIGGGaSILEISRLIR---HKGMRPIASHGAELVAAGRTTAEEIL 737
Cdd:TIGR01420 272 --DGGGRVLAVEILINTPAVRNLIREG-KTHQIKSLIQtgqQLGMQTFDQHLAQLYKKGLITLEDAL 335
PilT cd01131
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ...
474-635 3.65e-48

Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein responsible for the retraction of type IV pili, likely by pili disassembly. This retraction provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility.


Pssm-ID: 410875 [Multi-domain]  Cd Length: 223  Bit Score: 169.64  E-value: 3.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 474 SLEGLGFPaadlTRIADMVAKPQGIILATGPTGSGKTTTLYSLLQH-DATPGKNYITIEDPVEYYLDMAGQVLVREKIGL 552
Cdd:cd01131     3 TFEELGLP----PVLKDLALKPRGLVLVTGPTGSGKSTTLAAMIDYiNETRSKHIITIEDPIEFVHKHKKSLINQREVGR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 553 ---TFPAVLRAILRQDPDVILLGEIRDFDTAEVAFHAALTGHQVFSTLHTNSAVATIARLFDL---GMKPYV---VASAL 623
Cdd:cd01131    79 dteSFAAALRAALREDPDVILVGEMRDLETIELALTAAETGHLVFSTLHTNSAAQTIDRIIDVfppEQQEQVriqLASSL 158
                         170
                  ....*....|..
gi 1308984715 624 EGIIAQRLVRKI 635
Cdd:cd01131   159 RGVISQRLLPKK 170
DotB_TraJ cd19516
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ...
488-634 5.76e-34

dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of the type IVb secretion (T4bS) system, also known as the dot/icm system, and is the main energy supplier of the secretion system. It is an ATPase, similar to the VirB11 component of the T4aS systems. This family also includes Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ encoded on the tra (transfer) operon.


Pssm-ID: 410924 [Multi-domain]  Cd Length: 179  Bit Score: 128.26  E-value: 5.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 488 IADMVAKPQGIILATGPTGSGKTTTLYSLLQH---DATPGKNYITIEDPVEYYLD---MAGQVLVREKIG---LTFPAVL 558
Cdd:cd19516     3 LVEALFPREGLVYVAGATGSGKSTLLAAIYRYileNDPPDRKIITYEDPIEFVYDgikSKHSIIVQSQIPrhfKSFAKAV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 559 RAILRQDPDVILLGEIRDFDTAEVAFHAALTGHQVFSTLHTNSAVATIARLFDL------GMKPYVVASALEGIIAQRLV 632
Cdd:cd19516    83 REALRRKPSLIGVGELRDQETISAAVEASLTGHPVYSTVHTKSVAETIRRLISLfppeerDAAAYDLLSTLRFIIVQRLV 162

                  ..
gi 1308984715 633 RK 634
Cdd:cd19516   163 RT 164
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
28-180 1.17e-33

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: 133.94  E-value: 1.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGH 107
Cdd:COG2204     4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGY 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308984715 108 ANTDAVMGAINEGAvYKFILKPWNDDDLRVTVALALERFDLIARNRA---LKSENEKKSKEISALAKLAATHRSRL 180
Cdd:COG2204    84 GDVETAVEAIKAGA-FDYLTKPFDLEELLAAVERALERRRLRRENAEdsgLIGRSPAMQEVRRLIEKVAPSDATVL 158
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
28-158 8.09e-33

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 123.25  E-value: 8.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRqENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGH 107
Cdd:cd17596     2 TILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGY 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1308984715 108 ANTDAVMGAINEGAVYKFILKPWNDDDLRVTVALALERFDLIARNRALKSE 158
Cdd:cd17596    81 TDSEDIIAGINEAGIYQYLTKPWHPDQLLLTVRNAARLFELQRENERLSLE 131
type_II_IV_secretion_ATPases cd19477
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP ...
488-635 3.61e-32

type II/type IV hexameric secretion ATPases; 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: 410885 [Multi-domain]  Cd Length: 168  Bit Score: 122.50  E-value: 3.61e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 488 IADMVAKPqGIILATGPTGSGKTTTLYSLLQhDATPGKNYITIEDPVEY---YLDMAGQVLVREKIglTFPAVLRAILRQ 564
Cdd:cd19477     3 IKDGIAIG-KNVIVCGGTGSGKTTYIKSILE-FIPKEERIISIEDTEEIvfkHHKNYTQLFFGGNI--TSADCLKSCLRQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 565 DPDVILLGEIRDfDTAEVAFHAALTGHQ-VFSTLHTNSAVATIARLFDLG------------MKPYVVASALEGIIAQRL 631
Cdd:cd19477    79 RPDRIILGELRS-SEAYDFYNVLCSGHKgTLTTLHAGSSEEAFIRLAN*SssnsaarnikfeSLIEGFKDLIDGIVHINH 157

                  ....
gi 1308984715 632 VRKI 635
Cdd:cd19477   158 HKQC 161
PilU COG5008
Type IV pilus assembly protein, ATPase PilU [Cell motility, Extracellular structures];
461-635 7.34e-32

Type IV pilus assembly protein, ATPase PilU [Cell motility, Extracellular structures];


Pssm-ID: 444032  Cd Length: 370  Bit Score: 127.91  E-value: 7.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 461 VVMRIldrNAAVQSLEGLGFPAAdltrIADMVAKPQGIILATGPTGSGKTTTLYSLLQHDATPGKNYI-TIEDPVEYyLD 539
Cdd:COG5008    95 VLRRI---ETEIPTLDELGLPPV----LKDLIMEKRGLVLFVGATGSGKSTTLAAMIDHRNENSSGHIlTIEDPIEF-VH 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 540 MAGQVLV--REkIGL---TFPAVLRAILRQDPDVILLGEIRDFDTAEVAFHAALTGHQVFSTLHTNSAVATIAR------ 608
Cdd:COG5008   167 KHKKSIVtqRE-VGVdteSYEVALKNALRQAPDVILIGEIRDRETMEHAIAFAETGHLCLATLHANNANQALDRiinffp 245
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1308984715 609 -------LFDLgmkpyvvASALEGIIAQRLVRKI 635
Cdd:COG5008   246 eerrpqlLMDL-------SLNLRAIVSQRLVPTK 272
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
23-161 9.35e-30

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 117.57  E-value: 9.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  23 TPPRYRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSP--ETI 100
Cdd:COG3437     3 TGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPStrDIP 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308984715 101 RIMLTGHANTDAVMGAINEGAVYkFILKPWNDDDLRVTVALALERFDLIARNRALKSENEK 161
Cdd:COG3437    83 VIFLTALADPEDRERALEAGADD-YLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKL 142
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
28-129 5.42e-27

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 105.24  E-value: 5.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQE-NYQVV-TADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLT 105
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEaGFEVVgEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILS 80
                          90       100
                  ....*....|....*....|....
gi 1308984715 106 GHANTDAVMGAINEGAVYkFILKP 129
Cdd:COG4753    81 GYSDFEYAQEAIKLGADD-YLLKP 103
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
24-145 1.53e-26

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 104.93  E-value: 1.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  24 PPRYRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARS--PETIR 101
Cdd:COG0784     3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPrlPDIPI 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1308984715 102 IMLTGHANTDAVMGAINEGAVYkFILKPWNDDDLRVTVALALER 145
Cdd:COG0784    83 IALTAYADEEDRERALEAGADD-YLTKPVDPEELLEALRRLLAR 125
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
30-140 5.53e-25

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 99.92  E-value: 5.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHAN 109
Cdd:pfam00072   2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHGD 81
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308984715 110 TDAVMGAINEGAVYkFILKPWNDDDLRVTVA 140
Cdd:pfam00072  82 EDDAVEALEAGADD-FLSKPFDPDELLAAIR 111
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
30-158 7.38e-24

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 97.56  E-value: 7.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHAN 109
Cdd:cd17549     2 LLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHGD 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1308984715 110 TDAVMGAINEGAvYKFILKPWNDDDLRVTVALALERFDLIARNRALKSE 158
Cdd:cd17549    82 VPMAVEAMRAGA-YDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQ 129
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
29-144 8.88e-24

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 96.80  E-value: 8.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHA 108
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1308984715 109 NTDAVMGAINEGAvYKFILKPWNDDDLRVTVALALE 144
Cdd:cd17550    81 TIETAVKATKLGA-YDFIEKPLSLDRLLLTIERALE 115
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
30-129 9.40e-24

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 96.14  E-value: 9.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHAN 109
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                          90       100
                  ....*....|....*....|
gi 1308984715 110 TDAVMGAINEGAVYkFILKP 129
Cdd:cd00156    81 EEDAVRALELGADD-YLVKP 99
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
26-151 4.29e-23

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 96.90  E-value: 4.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  26 RYRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKA--RSPETIRIM 103
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRAdpRTADIPIIF 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1308984715 104 LTGHANTDAVMGAINEGAVyKFILKPWNDDDLRVTValalerfDLIAR 151
Cdd:COG3706    81 LTALDDEEDRARALEAGAD-DYLTKPFDPEELLARV-------DLVAR 120
plasmid_TraJ TIGR02525
plasmid transfer ATPase TraJ; Members of this protein family are predicted ATPases associated ...
497-654 8.18e-23

plasmid transfer ATPase TraJ; Members of this protein family are predicted ATPases associated with plasmid transfer loci in bacteria. This family is most similar to the DotB ATPase of a type-IV secretion-like system of obligate intracellular pathogens Legionella pneumophila and Coxiella burnetii (TIGR02524). [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 131577 [Multi-domain]  Cd Length: 372  Bit Score: 101.03  E-value: 8.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 497 GIILATGPTGSGKTTTLYSLLQH--DATPGKNYITIEDPVEYYLDMAGQVL--VREKIGL---TFPAVLRAILRQDPDVI 569
Cdd:TIGR02525 150 GLGLICGETGSGKSTLAASIYQHcgETYPDRKIVTYEDPIEYILGSPDDLLppAQSQIGRdvdSFANGIRLALRRAPKII 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 570 LLGEIRDFDTAEVAFHAALTGHQVFSTLHTNSAVATIARLfdLGMKP--------YVVASALEGIIAQRLVRKICA---A 638
Cdd:TIGR02525 230 GVGEIRDLETFQAAVLAGQSGHFCLGTLHVKSPGEAISRC--LQMYPpemreaaaFDLLSILQYIIVQRLLRTTDGkrqA 307
                         170
                  ....*....|....*.
gi 1308984715 639 CSEPVAPDAELYRRLG 654
Cdd:TIGR02525 308 VREYIVFDDSLRRKLY 323
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
26-145 1.98e-22

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 95.79  E-value: 1.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  26 RYRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLT 105
Cdd:COG0745     1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1308984715 106 GHANTDAVMGAINEGAVyKFILKPWNDDDLRVTVALALER 145
Cdd:COG0745    81 ARDDEEDRVRGLEAGAD-DYLTKPFDPEELLARIRALLRR 119
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
29-131 2.59e-22

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 93.17  E-value: 2.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFR---QENYQVVTADSGAEGLQRLAE-----AETHLVISDFMMPAMNGAEFLREVKARSPETI 100
Cdd:cd17595     3 ILTVDDDPQVLRAVARDLRrqyGKDYRVLRADSGAEALDALKElklrgEAVALFLVDQRMPEMDGVEFLEKAMELFPEAK 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308984715 101 RIMLTGHANTDAVMGAINEGAVYKFILKPWN 131
Cdd:cd17595    83 RVLLTAYADTDAAIRAINDVQLDYYLLKPWD 113
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
25-158 2.56e-20

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 94.53  E-value: 2.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  25 PRYRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIML 104
Cdd:PRK11361    3 AINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILM 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1308984715 105 TGHANTDAVMGAINEGAvYKFILKPWNDDDLRVTVALALERFDLIARNRALKSE 158
Cdd:PRK11361   83 TAYAEVETAVEALRCGA-FDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQA 135
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
29-149 2.63e-20

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


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 86.87  E-value: 2.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHA 108
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1308984715 109 NTDAVMGAINEGAvYKFILKPWNDDDLRVTVALALERFDLI 149
Cdd:cd17572    81 SVDIAVEAMRLGA-YDFLEKPFDADRLRVTVRNALKHRKLT 120
T2SSE_N pfam05157
Type II secretion system (T2SS), protein E, N-terminal domain; This domain is found at the ...
213-319 9.90e-20

Type II secretion system (T2SS), protein E, N-terminal domain; This domain is found at the N-terminus of members of the Type II secretion system protein E. Proteins in this subfamily are typically involved in Type 4 pilus biogenesis, though some are involved in other processes; for instance aggregation in Myxococcus xanthus. The structure of this domain is now known.


Pssm-ID: 428339 [Multi-domain]  Cd Length: 108  Bit Score: 85.08  E-value: 9.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 213 LLEKDWVPERRIREILRTDMLIEEVQLAEFRVDPALAELIPHSFCVRQMVLPLRLDGKRLLLAMADPLDEGLIDEVRFTA 292
Cdd:pfam05157   1 LVELGLLSEEQLAQALAEQLGLPFVDLEALEIDPELLRLLPREFARRHRVLPLREDGGTLVVAVADPLDLALLDELRFLT 80
                          90       100
                  ....*....|....*....|....*..
gi 1308984715 293 GLDLTVVMADAEAIKRKIEAVYGGDGA 319
Cdd:pfam05157  81 GKRVEPVLATPSDIRRALERLYGSEES 107
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
29-147 1.70e-19

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 84.70  E-value: 1.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENY---QVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLT 105
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIDWEELgfeVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1308984715 106 GHANTDAVMGAINEGAVYkFILKPWNDDDLRVTVALALERFD 147
Cdd:cd17536    81 GYDDFEYAQKAIRLGVVD-YLLKPVDEEELEEALEKAKEELD 121
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
24-154 1.83e-19

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 85.02  E-value: 1.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  24 PPRYRLLFVDDEPGILKALTRVFRQ-ENYQVV-TADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIR 101
Cdd:COG4565     1 MKMIRVLIVEDDPMVAELLRRYLERlPGFEVVgVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1308984715 102 IMLTGHANTDAVMGAINEGAVYkFILKPWNDDDLRVTVALALERFDLIARNRA 154
Cdd:COG4565    81 IVITAARDPETVREALRAGVVD-YLIKPFTFERLREALERYLEYRRLLREDQE 132
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
30-105 3.31e-18

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 80.14  E-value: 3.31e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308984715  30 LFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLT 105
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLT 76
VirB11-like_ATPase cd01130
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...
488-618 3.37e-18

Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.


Pssm-ID: 410874 [Multi-domain]  Cd Length: 177  Bit Score: 82.97  E-value: 3.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 488 IADMVAKPQGIILAtGPTGSGKTTTLYSLLQHdATPGKNYITIEDPVEYYLDMAGQV--LVREKIG----LTFPAVLRAI 561
Cdd:cd01130     5 LRLAVRARKNILIS-GGTGSGKTTLLNALLSF-IPPDERIVTIEDTRELQLPHPNVVhlLTRPGGGekgeVTMADLLKAA 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1308984715 562 LRQDPDVILLGEIRDfDTAEVAFHAALTGHQ-VFSTLHTNSAVATIARLFDLGMKPYV 618
Cdd:cd01130    83 LRMRPDRIIVGEVRG-GEAYDMLQAMNTGHPgSITTIHANSAEDAIDRLATLVLEAGV 139
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
32-158 1.32e-17

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 81.69  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  32 VDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHANTD 111
Cdd:COG4566     5 VDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHGDVP 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1308984715 112 AVMGAINEGAVYkFILKPWNDDDLRVTVALALERFDLIARNRALKSE 158
Cdd:COG4566    85 MAVRAMKAGAVD-FLEKPFDDQALLDAVRRALARDRARRAERARRAE 130
PRK15115 PRK15115
response regulator GlrR; Provisional
28-144 6.52e-17

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 84.12  E-value: 6.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGH 107
Cdd:PRK15115    7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAH 86
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1308984715 108 ANTDAVMGAINEGaVYKFILKPWNDDDLRVTVALALE 144
Cdd:PRK15115   87 GSIPDAVAATQQG-VFSFLTKPVDRDALYKAIDDALE 122
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
23-145 7.45e-17

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 78.80  E-value: 7.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  23 TPPRYRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRI 102
Cdd:COG4567     1 SAEDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1308984715 103 MLTGHANTDAVMGAINEGAVYkFILKPWNDDDLrvtvALALER 145
Cdd:COG4567    81 VLTGYASIATAVEAIKLGADD-YLAKPADADDL----LAALER 118
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
28-129 1.15e-16

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


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 76.00  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARsPETIRI---ML 104
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKED-PETRHIpviMI 79
                          90       100
                  ....*....|....*....|....*
gi 1308984715 105 TGHANTDAVMGAINEGAVyKFILKP 129
Cdd:cd17538    80 TALDDREDRIRGLEAGAD-DFLSKP 103
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
28-139 2.92e-16

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


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 75.34  E-value: 2.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGH 107
Cdd:cd17554     2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAY 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984715 108 ANTDAVMGAINEGAvykFILKPWNDDDLRVTV 139
Cdd:cd17554    82 SEYKSDFSSWAADA---YVVKSSDLTELKETI 110
VirB11 COG0630
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ...
503-633 6.33e-16

Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440395 [Multi-domain]  Cd Length: 462  Bit Score: 80.89  E-value: 6.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 503 GPTGSGKTTTLYSLLQHdATPGKNYITIEDPVEYYL--DMAGQVLVREKIGLTFPAV-----LRAILRQDPDVILLGEIR 575
Cdd:COG0630   297 GGTASGKTTLLNALLSF-IPPDAKIVTIEDTRELNLphENWISLVTRESFGGEEGDVtmfdlLKAALRQRPDYIVVGEVR 375
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1308984715 576 DfDTAEVAFHAALTGHQVFSTLHTNSAVATIARLFDLGMK-PYVVASALEGIIAQRLVR 633
Cdd:COG0630   376 G-EEAYTLFQAMATGHGVLSTFHADSVESAINRLTSPPINvPRTLLQALDLVVFQKRVR 433
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
30-136 5.66e-15

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 71.51  E-value: 5.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEA--ETHLVISDFMMPAMNGAEFLREVkaRSPETIR-IMLTG 106
Cdd:cd17584     2 LVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENkdEFDLVITDVHMPDMDGFEFLELI--RLEMDLPvIMMSA 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 1308984715 107 HANTDAVMGAINEGAVYkFILKPWNDDDLR 136
Cdd:cd17584    80 DGSTSTVMKGLAHGACD-YLLKPVSIEDLK 108
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
29-129 9.56e-15

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 70.62  E-value: 9.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKArSPETIR---IMLT 105
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKA-DPATRHipvIFLT 79
                          90       100
                  ....*....|....*....|....
gi 1308984715 106 GHANTDAVMGAINEGAVyKFILKP 129
Cdd:cd19920    80 ALTDTEDKVKGFELGAV-DYITKP 102
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
30-135 2.08e-14

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 69.85  E-value: 2.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVF-RQENYQVV-TADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGH 107
Cdd:cd17535     2 LIVDDHPLVREGLRRLLeSEPDIEVVgEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTAH 81
                          90       100
                  ....*....|....*....|....*...
gi 1308984715 108 ANTDAVMGAINEGAVyKFILKPWNDDDL 135
Cdd:cd17535    82 DDPEYVLRALKAGAA-GYLLKDSSPEEL 108
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
25-161 2.74e-14

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 71.91  E-value: 2.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  25 PRYRLLFVDDEPGILKALTRVFRQENYQVVT-ADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIrIM 103
Cdd:COG3707     2 RGLRVLVVDDEPLRRADLREGLREAGYEVVAeAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPAPV-IL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1308984715 104 LTGHANTDAVMGAINEGaVYKFILKPWNDDDLRVTVALALERFdliARNRALKSENEK 161
Cdd:COG3707    81 LTAYSDPELIERALEAG-VSAYLVKPLDPEDLLPALELALARF---RELRALRRELAK 134
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
28-132 3.86e-14

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 69.15  E-value: 3.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGH 107
Cdd:cd17555     2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGA 81
                          90       100
                  ....*....|....*....|....*
gi 1308984715 108 ANTDAVMGAINEGAvYKFILKPWND 132
Cdd:cd17555    82 GVMSDAVEALRLGA-WDYLTKPIED 105
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
32-134 3.93e-14

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


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 69.22  E-value: 3.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  32 VDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHANTD 111
Cdd:cd19919     6 VDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAHSDLD 85
                          90       100
                  ....*....|....*....|...
gi 1308984715 112 AVMGAINEGAvYKFILKPWNDDD 134
Cdd:cd19919    86 SAVSAYQGGA-FEYLPKPFDIDE 107
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
30-138 6.41e-14

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 68.70  E-value: 6.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAE-AETHLVISDFMMPAMNGAEFLREVKAR-SPETIRIM-LTG 106
Cdd:cd17544     4 LVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQhPDIKLVITDYNMPEMDGFELVREIRKKySRDQLAIIgISA 83
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1308984715 107 HAntDAVMGA--INEGAvYKFILKPWNDDDL--RVT 138
Cdd:cd17544    84 SG--DNALSArfIKAGA-NDFLTKPFLPEEFycRVT 116
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
28-130 1.01e-13

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 67.53  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRL-AEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTG 106
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLqQGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80
                          90       100
                  ....*....|....*....|....
gi 1308984715 107 HAnTDAVMGAINEGAVYKFILKPW 130
Cdd:cd18160    81 GA-AAAPELLSDAVGDNATLKKPF 103
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
28-135 1.21e-13

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


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 67.71  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVK--ARSPETIRIMLT 105
Cdd:cd17562     2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRklPAYKFTPILMLT 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1308984715 106 GHANTDAVMGAINEGAVyKFILKPWNDDDL 135
Cdd:cd17562    82 TESSDEKKQEGKAAGAT-GWLVKPFDPEQL 110
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
28-139 1.67e-13

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 67.58  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGH 107
Cdd:cd17553     2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAY 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984715 108 ANTDAVMGAINEGAVYKFIlKPWNDDDLRVTV 139
Cdd:cd17553    82 GELDMIQESKELGALTHFA-KPFDIDEIRDAV 112
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
28-135 4.27e-13

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 65.93  E-value: 4.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGH 107
Cdd:cd17563     2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGY 81
                          90       100
                  ....*....|....*....|....*...
gi 1308984715 108 ANTDAVMGAINEGAVYkFILKPWNDDDL 135
Cdd:cd17563    82 ASIATAVEAIKLGADD-YLAKPADADEI 108
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
32-135 5.24e-13

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 66.08  E-value: 5.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  32 VDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHAntD 111
Cdd:cd17537     6 VDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHG--D 83
                          90       100
                  ....*....|....*....|....*.
gi 1308984715 112 AVMG--AINEGAVyKFILKPWNDDDL 135
Cdd:cd17537    84 VPMAveAMKAGAV-DFLEKPFRDQVL 108
fixJ PRK09390
response regulator FixJ; Provisional
24-158 7.10e-13

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 68.11  E-value: 7.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  24 PPRYRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIM 103
Cdd:PRK09390    1 SDKGVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1308984715 104 LTGHANTDAVMGAINEGAVyKFILKPWNDDDLRVTVALALERFDLIARNRALKSE 158
Cdd:PRK09390   81 MTGHGDVPLAVEAMKLGAV-DFIEKPFEDERLIGAIERALAQAPEAAKSEAVAAD 134
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
28-136 1.24e-12

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 65.05  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVT-ADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKA--RSPETIRIML 104
Cdd:cd19923     2 KVLVVDDFSTMRRIIKNLLKELGFNNVEeAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRAdgALSHLPVLMV 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984715 105 TGHANTDAVMGAINEGaVYKFILKPWNDDDLR 136
Cdd:cd19923    82 TAEAKKENVIAAAQAG-VNNYIVKPFTAATLK 112
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
27-161 1.37e-12

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 67.92  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  27 YRLLFVDDEPGILKALTRVFRQ-ENYQVV-TADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIML 104
Cdd:COG3279     2 MKILIVDDEPLARERLERLLEKyPDLEVVgEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFT 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1308984715 105 TGHANtDAVMgAINEGAVYkFILKPWNDDDLRVTVALALERFDLIARNRALKSENEK 161
Cdd:COG3279    82 TAYDE-YALE-AFEVNAVD-YLLKPIDEERLAKALEKAKERLEAKAAAEASPEEKDR 135
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
29-139 1.37e-12

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


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 64.80  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIR---IMLT 105
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRRtpiIALT 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1308984715 106 GHANTDAVMGAINEGAVYkFILKPWNDDDLRVTV 139
Cdd:cd17546    81 ANALEEDREKCLEAGMDD-YLSKPVKLDQLKEVL 113
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
27-129 3.73e-12

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 63.95  E-value: 3.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  27 YRLLFVDDEPGILKALTRVFRQE-NYQVV-TADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPeTIRIML 104
Cdd:cd17541     1 IRVLIVDDSAVMRKLLSRILESDpDIEVVgTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERP-TPVVMV 79
                          90       100
                  ....*....|....*....|....*..
gi 1308984715 105 TGH--ANTDAVMGAINEGAVYkFILKP 129
Cdd:cd17541    80 SSLteEGAEITLEALELGAVD-FIAKP 105
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
28-129 7.87e-12

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


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 62.84  E-value: 7.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENY-QVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPET---IrIM 103
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEdvpI-VM 80
                          90       100
                  ....*....|....*....|....*.
gi 1308984715 104 LTGHANTDAVMGAINEGAVyKFILKP 129
Cdd:cd17551    81 ITADTDREVRLRALEAGAT-DFLTKP 105
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
30-108 8.84e-12

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 62.48  E-value: 8.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSP--ETIRIMLTGH 107
Cdd:cd17580     2 LVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWlaNTPAIALTGY 81

                  .
gi 1308984715 108 A 108
Cdd:cd17580    82 G 82
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
27-143 9.07e-12

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 62.68  E-value: 9.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  27 YRLLFVDDEPGILKALTRVFRQENYQVV-TADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLT 105
Cdd:cd17542     1 KKVLIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCS 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984715 106 GHANTDAVMGAINEGAVyKFILKPWNDDDLRVTVALAL 143
Cdd:cd17542    81 AMGQEEMVKEAIKAGAK-DFIVKPFQPERVLEAVEKVL 117
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
28-155 1.15e-11

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


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 62.37  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGH 107
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1308984715 108 ANTDAVMGAINEGAvykfilkpwndDDLrVTVALALErfDLIARNRAL 155
Cdd:cd17615    81 DSVEDRIAGLTAGG-----------DDY-VTKPFSLE--EVVARLRAL 114
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
29-135 1.43e-11

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 61.96  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARspETIR----IML 104
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSD--PDLKdipvILL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308984715 105 TGHANTDAVMGAINEGAvYKFILKPWNDDDL 135
Cdd:cd17598    79 TTLSDPRDVIRGLECGA-DNFITKPYDEKYL 108
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
30-115 1.53e-11

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 61.91  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKaRSPETIR---IMLTG 106
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILR-SDPKTSSipiIMLTA 79
                          90
                  ....*....|
gi 1308984715 107 HAN-TDAVMG 115
Cdd:cd19937    80 KGEeFDKVLG 89
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
30-145 1.53e-11

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


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 61.85  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGH-A 108
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALdA 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1308984715 109 NTDAVMGaINEGAvYKFILKPWNDDDLRVTVALALER 145
Cdd:cd17625    81 VEDRVKG-LDLGA-DDYLPKPFSLAELLARIRALLRR 115
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
29-121 1.83e-11

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 60.92  E-value: 1.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHA 108
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80
                          90
                  ....*....|....
gi 1308984715 109 N-TDAVMGaINEGA 121
Cdd:cd19935    81 SvEDRVKG-LDLGA 93
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
27-139 3.45e-11

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 60.86  E-value: 3.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  27 YRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIrIMLTG 106
Cdd:cd17619     1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSEVGI-ILVTG 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1308984715 107 HAN-TDAVMGAinEGAVYKFILKPWNDDDLRVTV 139
Cdd:cd17619    80 RDDeVDRIVGL--EIGADDYVTKPFNPRELLVRA 111
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
29-155 3.67e-11

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 60.86  E-value: 3.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHA 108
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1308984715 109 NTDAVMGAINEGAvykfilkpwnDDDLRVTVALAlerfDLIARNRAL 155
Cdd:cd17627    81 SVSDRVAGLDAGA----------DDYLVKPFALE----ELLARVRAL 113
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
28-143 8.90e-11

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 59.87  E-value: 8.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGIlKALTRVFRQE--NYQVVTADSGAEGLQrLAEAET-HLVISDFMMPAMNGAEFLREVKArSPETIRI-- 102
Cdd:cd17552     3 RILVIDDEEDI-REVVQACLEKlaGWEVLTASSGQEGLE-KAATEQpDAILLDVMMPDMDGLATLKKLQA-NPETQSIpv 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1308984715 103 -MLTGHANTDAVMGAINEGaVYKFILKPWNDDDLRVTVALAL 143
Cdd:cd17552    80 iLLTAKAQPSDRQRFASLG-VAGVIAKPFDPLTLAEQIAKLL 120
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
29-135 1.53e-10

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 58.86  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIrIMLTGHA 108
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQVPV-LMLTARG 79
                          90       100
                  ....*....|....*....|....*...
gi 1308984715 109 N-TDAVMGAinEGAVYKFILKPWNDDDL 135
Cdd:cd17623    80 DdIDRILGL--ELGADDYLPKPFNPREL 105
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
499-614 1.64e-10

Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443988 [Multi-domain]  Cd Length: 386  Bit Score: 63.65  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 499 ILATGPTGSGKTTTLYSLLQHdATPGKNYITIEDPVEYYLDM---------------AGQVLVREkigltfpaVLRAILR 563
Cdd:COG4962   185 ILVSGGTGSGKTTLLNALSGF-IPPDERIVTIEDAAELQLQHphvvrletrppnvegAGEVTLRD--------LVRNALR 255
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1308984715 564 QDPDVILLGEIRDfdtAEVA--FHAALTGHQ-VFSTLHTNSAVATIARLFDLGM 614
Cdd:COG4962   256 MRPDRIIVGEVRG---AEALdmLQAMNTGHDgSMSTLHANSARDALARLETLAL 306
PRK13851 PRK13851
type IV secretion system protein VirB11; Provisional
499-612 1.86e-10

type IV secretion system protein VirB11; Provisional


Pssm-ID: 172375  Cd Length: 344  Bit Score: 62.99  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 499 ILATGPTGSGKTTTLYSLLQHdATPGKNYITIEDPVEYYLDMAGQV-LVREKIGLTFPAV-----LRAILRQDPDVILLG 572
Cdd:PRK13851  165 MLLCGPTGSGKTTMSKTLISA-IPPQERLITIEDTLELVIPHENHVrLLYSKNGAGLGAVtaehlLQASLRMRPDRILLG 243
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1308984715 573 EIRDfDTAEVAFHAALTGHQ-VFSTLHTNSAVATIARLFDL 612
Cdd:PRK13851  244 EMRD-DAAWAYLSEVVSGHPgSISTIHGANPVQGFKKLFSL 283
orf27 CHL00148
Ycf27; Reviewed
25-159 2.10e-10

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 61.66  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  25 PRYRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIrIML 104
Cdd:CHL00148    5 SKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKESDVPI-IML 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308984715 105 TGHAN-TDAVMGAinEGAVYKFILKPWNDDDLRVTVALALERFDLIARNRALKSEN 159
Cdd:CHL00148   84 TALGDvSDRITGL--ELGADDYVVKPFSPKELEARIRSVLRRTNKKSFSSKIPNSS 137
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
27-81 2.84e-10

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 56.04  E-value: 2.84e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1308984715   27 YRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMP 81
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
nfrB PRK11234
phage adsorption protein NrfB;
161-301 3.96e-10

phage adsorption protein NrfB;


Pssm-ID: 236884 [Multi-domain]  Cd Length: 727  Bit Score: 63.22  E-value: 3.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 161 KKSKEISALAKLAATHRsRLGIVLHNKGALSAPQLQELtLLQERRKEPLIRLLLEKDWVPERRIREILRTDMLIEEVQLA 240
Cdd:PRK11234  466 KTTHDFPSVTGDTRSLR-PLGQILLENGVITEEQLDTA-LRNRVRGLRLGQSLLMQGLISAEQLAQALAEQNGVAWESLD 543
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308984715 241 EFRVDPALAELIPHSFCVRQMVLPLRLDGKRLLLAMADPLDEGLIDEVRFTAGLDLTVVMA 301
Cdd:PRK11234  544 PWQIPSSLIAEMPASVALHYAVLPLREEGDELIVASEDGISPVSLAALTRKLGRKVRYVIV 604
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
28-143 4.09e-10

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 57.80  E-value: 4.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVV-TADSGAEGLQRLAEAETHLVISDFMMP-AMNGAEFLREVKARSPETIrIMLT 105
Cdd:cd17534     2 KILIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKFDIPV-IFLT 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984715 106 GHANtDAVMGAINEGAVYKFILKPWNDDDLRVTVALAL 143
Cdd:cd17534    81 AYSD-EETLERAKETNPYGYLVKPFNERELKAAIELAL 117
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
32-145 4.49e-10

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 62.58  E-value: 4.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  32 VDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHANTD 111
Cdd:PRK10923    9 VDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLD 88
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1308984715 112 AVMGAINEGAvYKFILKPWNDDDlrvTVALaLER 145
Cdd:PRK10923   89 AAVSAYQQGA-FDYLPKPFDIDE---AVAL-VER 117
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
22-143 4.64e-10

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 62.36  E-value: 4.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  22 LTPPRYRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIR 101
Cdd:PRK10365    1 MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1308984715 102 IMLTGHANTDAVMGAINEGAVyKFILKPWNDDDLRVTVALAL 143
Cdd:PRK10365   81 LIMTAYSSVETAVEALKTGAL-DYLIKPLDFDNLQATLEKAL 121
PLN03029 PLN03029
type-a response regulator protein; Provisional
23-166 7.22e-10

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 59.66  E-value: 7.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  23 TPPRYRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLA--------------------EAETHLVISDFMMPA 82
Cdd:PLN03029    5 TESQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGlheddrsnpdtpsvspnshqEVEVNLIITDYCMPG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  83 MNGAEFLREVKARSP-ETIRIMLTGHANTDA-VMGAINEGAvYKFILKPWNDDDLRvtvalALERFDLIARNRALKSENE 160
Cdd:PLN03029   85 MTGYDLLKKIKESSSlRNIPVVIMSSENVPSrITRCLEEGA-EEFFLKPVQLSDLN-----RLKPHMMKTKSKNQKQENQ 158

                  ....*.
gi 1308984715 161 KKSKEI 166
Cdd:PLN03029  159 EKQEKL 164
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
29-115 8.65e-10

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 56.44  E-value: 8.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIrIMLTGH- 107
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSNVPV-IMVTAKd 79

                  ....*...
gi 1308984715 108 ANTDAVMG 115
Cdd:cd17621    80 SEIDKVVG 87
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
28-145 1.13e-09

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 56.65  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTadSGAEGLQRLAEAETH---LVISDFMMPAMNGAEFLREVKARSPETIrIML 104
Cdd:cd19932     2 RVLIAEDEALIRMDLREMLEEAGYEVVG--EASDGEEAVELAKKHkpdLVIMDVKMPRLDGIEAAKIITSENIAPI-VLL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1308984715 105 TGHANTDAVMGAiNEGAVYKFILKPWNDDDLRVTVALALER 145
Cdd:cd19932    79 TAYSQQDLVERA-KEAGAMAYLVKPFSESDLIPAIEMAIAR 118
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
29-93 1.82e-09

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 55.46  E-value: 1.82e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVK 93
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLR 65
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
29-145 2.42e-09

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 55.51  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIrIMLTGH- 107
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSNVPI-IMLTAKd 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984715 108 ANTDAVMGAinEGAVYKFILKPWNDDDLRVTVALALER 145
Cdd:cd17614    80 SEVDKVLGL--ELGADDYVTKPFSNRELLARVKANLRR 115
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
28-135 2.58e-09

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 55.55  E-value: 2.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIrIMLTGH 107
Cdd:cd17626     2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAESGVPI-VMLTAK 80
                          90       100
                  ....*....|....*....|....*...
gi 1308984715 108 ANTDAVMGAINEGAvYKFILKPWNDDDL 135
Cdd:cd17626    81 SDTVDVVLGLESGA-DDYVAKPFKPKEL 107
VirB11 TIGR02788
P-type DNA transfer ATPase VirB11; The VirB11 protein is found in the vir locus of ...
483-621 2.73e-09

P-type DNA transfer ATPase VirB11; The VirB11 protein is found in the vir locus of Agrobacterium Ti plasmids where it is involved in the type IV secretion system for DNA transfer. VirB11 is believed to be an ATPase. VirB11 is a homolog of the P-like conjugation system TrbB protein and the Flp pilus sytem protein TadA.


Pssm-ID: 274301  Cd Length: 308  Bit Score: 59.29  E-value: 2.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 483 ADLTRIAdmVAKPQGIILAtGPTGSGKTTTLYSLLQHDATpGKNYITIEDPVEYYLDMAGQV-LVREKIG-----LTFPA 556
Cdd:TIGR02788 134 KEFLRLA--IASRKNIIIS-GGTGSGKTTFLKSLVDEIPK-DERIITIEDTREIFLPHPNYVhLFYSKGGqglakVTPKD 209
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308984715 557 VLRAILRQDPDVILLGEIRDfdtAEvAFH---AALTGHQ-VFSTLHTNSAVATIARLFDLGMKPYVVAS 621
Cdd:TIGR02788 210 LLQSCLRMRPDRIILGELRG---DE-AFDfirAVNTGHPgSITTLHAGSPEEAFEQLALMVKSSQAGLG 274
pleD PRK09581
response regulator PleD; Reviewed
28-132 3.51e-09

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 59.91  E-value: 3.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKArSPETIRI---ML 104
Cdd:PRK09581    4 RILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKS-DPATTHIpvvMV 82
                          90       100
                  ....*....|....*....|....*....
gi 1308984715 105 TG-HANTDAVMGaINEGAvYKFILKPWND 132
Cdd:PRK09581   83 TAlDDPEDRVRG-LEAGA-DDFLTKPIND 109
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
30-121 3.65e-09

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 54.48  E-value: 3.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIrIMLTGHAN 109
Cdd:cd17620     2 LVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSAVPV-IVLSARDE 80
                          90
                  ....*....|..
gi 1308984715 110 TDAVMGAINEGA 121
Cdd:cd17620    81 ESDKIAALDAGA 92
PRK13557 PRK13557
histidine kinase; Provisional
11-141 7.23e-09

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 58.91  E-value: 7.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  11 NTAAPQAPAAHLTPPRYRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRL-AEAETHLVISDFMMP-AMNGAEF 88
Cdd:PRK13557  400 NPEQEPKARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILdSHPEVDLLFTDLIMPgGMNGVML 479
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308984715  89 LREVKARSPeTIRIML-TGHAN-----TDAvmgainEGAVYKFILKPWNDDDL--RVTVAL 141
Cdd:PRK13557  480 AREARRRQP-KIKVLLtTGYAEasierTDA------GGSEFDILNKPYRRAELarRVRMVL 533
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
28-122 9.34e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 57.97  E-value: 9.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVF-RQENYQVV-TADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRI--M 103
Cdd:PRK12555    2 RIGIVNDSPLAVEALRRALaRDPDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERPCPILIvtS 81
                          90
                  ....*....|....*....
gi 1308984715 104 LTGhANTDAVMGAINEGAV 122
Cdd:PRK12555   82 LTE-RNASRVFEAMGAGAL 99
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
29-105 1.24e-08

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 53.64  E-value: 1.24e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLT 105
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILT 77
nfrB PRK15489
glycosyl transferase family protein;
177-304 1.27e-08

glycosyl transferase family protein;


Pssm-ID: 237974 [Multi-domain]  Cd Length: 703  Bit Score: 58.21  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 177 RSRLGIVLHNKGALSAPQLQELTLLQERRKEPLIRLLLEKDWVPERRIREILRTDMLIEEVQLAEFRVDpALAELIPHSF 256
Cdd:PRK15489  490 RRRLGELLLTWQAVTPEQLQAALAEQQTRGKPLGRILLSQGWLDDETLAEAIAFQADLPRVSLDNVVLG-ALADCLPRDL 568
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1308984715 257 CVRQMVLPL--RLDGkRLLLAMADPLDEGLIDEVRFTAGLDLTVVMA-DAE 304
Cdd:PRK15489  569 CVRWRVVPFsiGEDG-TLNIAVASPLPGEALQEVARAAGRKVAQFIArDSE 618
PRK13894 PRK13894
conjugal transfer ATPase TrbB; Provisional
499-609 1.46e-08

conjugal transfer ATPase TrbB; Provisional


Pssm-ID: 184377  Cd Length: 319  Bit Score: 57.06  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 499 ILATGPTGSGKTT----TLYSLLQHDatPGKNYITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDPDVILLGEI 574
Cdd:PRK13894  151 ILVIGGTGSGKTTlvnaIINEMVIQD--PTERVFIIEDTGEIQCAAENYVQYHTSIDVNMTALLKTTLRMRPDRILVGEV 228
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1308984715 575 RDFDTAEVaFHAALTGHQ-VFSTLHTNSAVATIARL 609
Cdd:PRK13894  229 RGPEALDL-LMAWNTGHEgGAATLHANNAKAGLDRL 263
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
30-129 2.51e-08

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 52.75  E-value: 2.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLA-----------EAETHLVISDFMMPAMNGAEFLREVKARS-- 96
Cdd:cd17581     2 LAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGledeedssnfnEPKVNMIITDYCMPGMTGYDLLKKVKESSal 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984715  97 -PETIRIMltghaNTDAVMGAIN----EGAvYKFILKP 129
Cdd:cd17581    82 kEIPVVIM-----SSENIPTRISrcleEGA-EDFLLKP 113
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
26-92 2.52e-08

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 52.97  E-value: 2.52e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308984715  26 RYRLLFVDDEPGILKALTRVF-RQENYQVV-TADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREV 92
Cdd:COG2197     1 MIRVLIVDDHPLVREGLRALLeAEPDIEVVgEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
28-129 2.66e-08

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


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 52.64  E-value: 2.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARS--PETIRIMLT 105
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEmtRDIPIIMLT 81
                          90       100
                  ....*....|....*....|....
gi 1308984715 106 GHANTDAVMGAINEGAvYKFILKP 129
Cdd:cd17618    82 ARGEEEDKVRGLEAGA-DDYITKP 104
PRK10766 PRK10766
two-component system response regulator TorR;
27-160 2.76e-08

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 55.04  E-value: 2.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  27 YRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIrIMLTG 106
Cdd:PRK10766    3 YHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRSTVGI-ILVTG 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308984715 107 HanTDAV-------MGAINegavykFILKPWNDDDLRVTVALALERFDLIARNRALKSENE 160
Cdd:PRK10766   82 R--TDSIdrivgleMGADD------YVTKPLELRELLVRVKNLLWRISLARQAQPHAQEED 134
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
29-135 3.31e-08

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 52.41  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHA 108
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                          90       100
                  ....*....|....*....|....*..
gi 1308984715 109 NTDAVMGAINEGAvYKFILKPWNDDDL 135
Cdd:cd17616    81 DIEDKVKGLGFGA-DDYMTKPFHKDEL 106
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
30-129 7.40e-08

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 51.00  E-value: 7.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHAN 109
Cdd:cd19926     2 LVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYGS 81
                          90       100
                  ....*....|....*....|
gi 1308984715 110 TDAVMGAINEGAvYKFILKP 129
Cdd:cd19926    82 LDTAIEALKAGA-FDFLTKP 100
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
32-129 7.81e-08

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 50.73  E-value: 7.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  32 VDDEPGILKALTRVFRQENYQVV--TADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHAN 109
Cdd:cd17565     4 VDDDKNIIKILSDIIEDDDLGEVvgEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQVSD 83
                          90       100
                  ....*....|....*....|
gi 1308984715 110 TDAVMGAINEGAVYkFILKP 129
Cdd:cd17565    84 KEMIGKAYQAGIEF-FINKP 102
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
30-109 1.04e-07

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 50.42  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAE-AETHLVISDFMMPA-MNGAEFLREVKARSPETIRIMLTGH 107
Cdd:cd18161     2 LVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESgPDIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLTSGY 81

                  ..
gi 1308984715 108 AN 109
Cdd:cd18161    82 AE 83
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
28-105 1.60e-07

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 50.45  E-value: 1.60e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIrIMLT 105
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFSDVPI-IMVT 77
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
28-145 1.79e-07

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 52.88  E-value: 1.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLaEAETHLVISDFMMPAMNGAEFLREVKARSpETIRIMLTGH 107
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLL-DDSIDLLLLDVMMPKKNGIDTLKELRQTH-QTPVIMLTAR 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1308984715 108 -ANTDAVMGAinEGAVYKFILKPWNDDDLRVTVALALER 145
Cdd:PRK10955   81 gSELDRVLGL--ELGADDYLPKPFNDRELVARIRAILRR 117
ompR PRK09468
osmolarity response regulator; Provisional
23-135 3.30e-07

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 51.90  E-value: 3.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  23 TPPRYRLLFVDDEPGILKALTRVFRQENYQVVTADSgAEGLQRLAEAET-HLVISDFMMPAMNGAEFLREVKARSPETIR 101
Cdd:PRK09468    2 MQENYKILVVDDDMRLRALLERYLTEQGFQVRSAAN-AEQMDRLLTRESfHLMVLDLMLPGEDGLSICRRLRSQNNPTPI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1308984715 102 IMLTghANTDAV-------MGAINegavykFILKPWNDDDL 135
Cdd:PRK09468   81 IMLT--AKGEEVdrivgleIGADD------YLPKPFNPREL 113
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
29-129 3.82e-07

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 48.65  E-value: 3.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPEtIRIMLTGHA 108
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPD-LPIIVMSAQ 79
                          90       100
                  ....*....|....*....|...
gi 1308984715 109 NTdaVMGAI--NEGAVYKFILKP 129
Cdd:cd19928    80 NT--LMTAVkaAERGAFEYLPKP 100
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
29-140 8.96e-07

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


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 48.05  E-value: 8.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHA 108
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISNVPIIFISSRDD 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984715 109 NTDAVMgAINEGAVyKFILKPWnddDLRVTVA 140
Cdd:cd18159    81 NMDQVM-AINMGGD-DYITKPF---DLDVLLA 107
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
32-115 1.78e-06

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 47.05  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  32 VDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHANTD 111
Cdd:cd19936     4 VDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKSTLPVIFLTSKDDEID 83

                  ....
gi 1308984715 112 AVMG 115
Cdd:cd19936    84 EVFG 87
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
28-115 2.09e-06

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 49.58  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTG- 106
Cdd:PRK11083    5 TILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTAr 84

                  ....*....
gi 1308984715 107 HANTDAVMG 115
Cdd:PRK11083   85 SDEVDRLVG 93
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
28-140 2.20e-06

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 47.15  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKArSPETIRI---ML 104
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKE-DPATRDIpviAL 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1308984715 105 TGHA---NTDAVMGAINEGavykFILKPWNDDDLRVTVA 140
Cdd:cd17548    80 TAYAmkgDREKILEAGCDG----YISKPIDTREFLETVA 114
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
28-121 2.91e-06

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 48.87  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQE-NYQVVT-ADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLT 105
Cdd:PRK10651    8 TILLIDDHPMLRTGVKQLISMApDITVVGeASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFS 87
                          90
                  ....*....|....*.
gi 1308984715 106 GHANTDAVMGAINEGA 121
Cdd:PRK10651   88 VSNHEEDVVTALKRGA 103
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
29-135 3.09e-06

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 46.57  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTAD--SGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTG 106
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLIELDPDFTVVGEasSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTV 80
                          90       100
                  ....*....|....*....|....*....
gi 1308984715 107 HANTDAVMGAINEGAvYKFILKPWNDDDL 135
Cdd:cd19931    81 SDAEDDVVTALRAGA-DGYLLKDMEPEDL 108
PRK11173 PRK11173
two-component response regulator; Provisional
27-164 3.15e-06

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 49.24  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  27 YRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSpETIRIMLTG 106
Cdd:PRK11173    4 PHILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQA-NVALMFLTG 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1308984715 107 HAN-TDAVMGAinEGAVYKFILKPWNDDDLRVTVAlalerfDLIARNRALKSENEKKSK 164
Cdd:PRK11173   83 RDNeVDKILGL--EIGADDYITKPFNPRELTIRAR------NLLSRTMNLGTVSEERRS 133
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
30-136 5.89e-06

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 45.72  E-value: 5.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVFRQENY-QVVTADSGAEGLQRLAEAETHLVISDFMMPA-MNGAEFLREVKAR---SPETIRIML 104
Cdd:cd17589     2 LIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELRHKkliSPSTVFIMV 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984715 105 TGHANTDAVMGAInEGAVYKFILKPWNDDDLR 136
Cdd:cd17589    82 TGESSRAMVLSAL-ELEPDDYLLKPFTVSELR 112
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
28-105 6.40e-06

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 46.26  E-value: 6.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQEN--YQVVTADSGAEGLQRL------AEAET-HLVISDFMMPAMNGAEFLREVKArSPE 98
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDFLrgegeyADAPRpDLILLDLNMPRMDGFEVLREIKA-DPD 79
                          90
                  ....*....|
gi 1308984715  99 TIRI---MLT 105
Cdd:cd17557    80 LRRIpvvVLT 89
PRK10610 PRK10610
chemotaxis protein CheY;
28-130 9.62e-06

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 45.74  E-value: 9.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQ-VVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARS--PETIRIML 104
Cdd:PRK10610    7 KFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGamSALPVLMV 86
                          90       100
                  ....*....|....*....|....*.
gi 1308984715 105 TGHANTDAVMGAINEGAVyKFILKPW 130
Cdd:PRK10610   87 TAEAKKENIIAAAQAGAS-GYVVKPF 111
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
28-150 1.08e-05

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 47.41  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVK--ARSPETIRIMLT 105
Cdd:PRK10161    4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKreSMTRDIPVVMLT 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1308984715 106 GHANTDAVMGAINEGAvYKFILKPWNDDDLRVTVALALERFDLIA 150
Cdd:PRK10161   84 ARGEEEDRVRGLETGA-DDYITKPFSPKELVARIKAVMRRISPMA 127
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
27-180 1.25e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 48.22  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  27 YRLLFVDDEPGILKALTRVFRQE-NYQVV-TADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPeTIRIM- 103
Cdd:PRK00742    4 IRVLVVDDSAFMRRLISEILNSDpDIEVVgTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRP-TPVVMv 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 104 --LTgHANTDAVMGAINEGAVyKFILKPWND--DDLRVTVALALERFDLIARNRALKSENEKKSKEISALAKLAATHRSR 179
Cdd:PRK00742   83 ssLT-ERGAEITLRALELGAV-DFVTKPFLGisLGMDEYKEELAEKVRAAARARVRALPPRAAAAARAAAAAPAALAAAP 160

                  .
gi 1308984715 180 L 180
Cdd:PRK00742  161 L 161
PRK15479 PRK15479
transcriptional regulator TctD;
28-211 1.38e-05

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 47.02  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGH 107
Cdd:PRK15479    2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTAR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 108 ANTDAVMGAINEGAvYKFILKPWNDDDLRvtvalalerfdliARNRALKSENEKKSKEISALAKLaathrsrlgiVLHNK 187
Cdd:PRK15479   82 SAVADRVKGLNVGA-DDYLPKPFELEELD-------------ARLRALLRRSAGQVQEVQQLGEL----------IFHDE 137
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1308984715 188 G---------ALSAPQLQELTLLQERRKEPLIR 211
Cdd:PRK15479  138 GyfllqgqplALTPREQALLTVLMYRRTRPVSR 170
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
29-94 2.07e-05

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 44.29  E-value: 2.07e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRL------AEAETH---LVISDFMMPAMNGAEFLREVKA 94
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLenlakeGNDLSKeldLIITDIEMPKMDGYELTFELRD 75
PRK13833 PRK13833
conjugal transfer protein TrbB; Provisional
499-612 2.46e-05

conjugal transfer protein TrbB; Provisional


Pssm-ID: 172360 [Multi-domain]  Cd Length: 323  Bit Score: 47.10  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 499 ILATGPTGSGKTTTLYSLLQH--DATPGKNYITIEDPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQDPDVILLGEIRD 576
Cdd:PRK13833  147 IVISGGTGSGKTTLANAVIAEivASAPEDRLVILEDTAEIQCAAENAVALHTSDTVDMARLLKSTMRLRPDRIIVGEVRD 226
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1308984715 577 fDTAEVAFHAALTGHQ-VFSTLHTNSAVATIARLFDL 612
Cdd:PRK13833  227 -GAALTLLKAWNTGHPgGVTTIHSNTAMSALRRLEQL 262
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
30-129 2.87e-05

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 43.97  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  30 LFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIrIMLTGHAN 109
Cdd:cd17594     3 LVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSDVPI-IIISGDRR 81
                          90       100
                  ....*....|....*....|
gi 1308984715 110 TDAVMGAINEGAVYKFILKP 129
Cdd:cd17594    82 DEIDRVVGLELGADDYLAKP 101
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
29-140 1.02e-04

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 42.03  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHA 108
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308984715 109 NTDAVMGAINEGAvYKFILKPWnddDLRVTVA 140
Cdd:cd17573    81 KTEQEIEAFKEGA-DDYIAKPF---DFKVLVA 108
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
32-109 1.02e-04

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 41.97  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  32 VDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARS--PETIRIMLTGHAN 109
Cdd:cd17602     4 VDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSalKDTPIIMLTGKDG 83
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
28-136 2.13e-04

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 41.37  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQ-ENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTG 106
Cdd:cd17593     2 KVLICDDSSMARKQLARALPAdWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVSG 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1308984715 107 HANTDAVMGAINEGAVYkFILKPWNDDDLR 136
Cdd:cd17593    82 DVQPEAKERVLELGALA-FLKKPFDPEKLA 110
PRK15347 PRK15347
two component system sensor kinase;
11-111 3.22e-04

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 44.25  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  11 NTAAPQAPAAHLTPPRYRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLR 90
Cdd:PRK15347  675 GAPNEPVINLPLQPWQLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQ 754
                          90       100
                  ....*....|....*....|....*
gi 1308984715  91 ----EVKARSPETIRIMLTGHANTD 111
Cdd:PRK15347  755 lwrdDPNNLDPDCMIVALTANAAPE 779
PRK10643 PRK10643
two-component system response regulator PmrA;
28-167 3.32e-04

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 42.72  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGH 107
Cdd:PRK10643    2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTAR 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308984715 108 -ANTDAVMGaINEGAvykfilkpwnDDDLRVTVALAlerfDLIARNRAL------KSENEKKSKEIS 167
Cdd:PRK10643   82 dTLEDRVAG-LDVGA----------DDYLVKPFALE----ELHARIRALirrhqgQGENELQVGNLT 133
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
6-97 5.68e-04

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 43.42  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715   6 KLFTGNTAAPQAPAAHLTPPRYR-------LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDF 78
Cdd:PRK10841  774 RIYRIELESDDSANALPSTDKAVsdnddmmILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDV 853
                          90       100
                  ....*....|....*....|..
gi 1308984715  79 MMPAMNGAEF---LREVKARSP 97
Cdd:PRK10841  854 NMPNMDGYRLtqrLRQLGLTLP 875
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
29-146 8.33e-04

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 41.71  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIrIMLTGHA 108
Cdd:PRK10529    4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWSAIPV-IVLSARS 82
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984715 109 NTDAVMGAINEGAvYKFILKPWNDDDLRVTVALALERF 146
Cdd:PRK10529   83 EESDKIAALDAGA-DDYLSKPFGIGELQARLRVALRRH 119
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
28-105 1.11e-03

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 39.28  E-value: 1.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIrIMLT 105
Cdd:cd17622     2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQGPI-LLLT 78
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
29-155 1.61e-03

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 38.80  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGHA 108
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1308984715 109 N-TDAVMGaINEGAvykfilkpwndDDLrVTVALALErfDLIARNRAL 155
Cdd:cd19934    81 SwQDKVEG-LDAGA-----------DDY-LTKPFHIE--ELLARLRAL 113
PRK10693 PRK10693
two-component system response regulator RssB;
56-95 1.73e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 41.13  E-value: 1.73e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1308984715  56 ADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKAR 95
Cdd:PRK10693    3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNR 42
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
24-163 1.94e-03

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 41.64  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715   24 PPRYRLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIM 103
Cdd:PRK09959   956 PEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWG 1035
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  104 LTGHANTDAVMGAINEGaVYKFILKPWNDDDLRVTVALALERFDLIARNRALKSENEKKS 163
Cdd:PRK09959  1036 LTANAQANEREKGLSCG-MNLCLFKPLTLDVLKTHLSQLHQVAHIAPQYRHLDIEALKNN 1094
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
494-574 2.11e-03

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: 39.44  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 494 KPQGIILATGPTGSGKTTTLYSLLQHDATPGKNYITIEDPveyylDMAGQVLVREKIGLTFPAVLRAILRQ-DPDVILLG 572
Cdd:cd00009    17 PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNAS-----DLLEGLVVAELFGHFLVRLLFELAEKaKPGVLFID 91

                  ..
gi 1308984715 573 EI 574
Cdd:cd00009    92 EI 93
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
28-111 3.19e-03

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 38.15  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEpGILKALTR-VFRQENYQVVTADSGAEGLQRLAEAET--HLVISDFMMPAMNGAEFLREVKARSPETIRIML 104
Cdd:cd19933     2 KVLLVDDN-AVNRMVTKgLLEKLGCEVTTVSSGEECLNLLASAEHsfQLVLLDLCMPEMDGFEVALRIRKLFGRRERPLI 80

                  ....*...
gi 1308984715 105 TG-HANTD 111
Cdd:cd19933    81 VAlTANTD 88
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
28-115 3.79e-03

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 37.74  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIrIMLTGH 107
Cdd:cd19939     1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHSHVPI-LMLTAR 79

                  ....*....
gi 1308984715 108 AN-TDAVMG 115
Cdd:cd19939    80 TEeMDRVLG 88
PRK15369 PRK15369
two component system response regulator;
27-121 3.83e-03

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 39.29  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  27 YRLLFVDDEP----GILKALTRVFRqenYQVV-TADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIR 101
Cdd:PRK15369    4 YKILLVDDHEliinGIKNMLAPYPR---YKIVgQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMNI 80
                          90       100
                  ....*....|....*....|
gi 1308984715 102 IMLTGHANTDAVMGAINEGA 121
Cdd:PRK15369   81 LVLTARQEEHMASRTLAAGA 100
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
495-574 4.00e-03

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: 38.51  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  495 PQGIILATGPTGSGKTTTLYSLLQHDATPGKN--YITIEDPVEYYLDMAGQVLVREKIGLTFPA-----VLRAILRQDPD 567
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGviYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrlALALARKLKPD 80

                   ....*..
gi 1308984715  568 VILLGEI 574
Cdd:smart00382  81 VLILDEI 87
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
28-145 7.36e-03

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 38.75  E-value: 7.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTGH 107
Cdd:PRK09836    2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTAL 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1308984715 108 ANTDAVMGAINEGAvYKFILKPWNDDDLRVTVALALER 145
Cdd:PRK09836   82 GTIEHRVKGLELGA-DDYLVKPFAFAELLARVRTLLRR 118
PRK11517 PRK11517
DNA-binding response regulator HprR;
28-214 7.71e-03

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 38.73  E-value: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  28 RLLFVDDEPGILKALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKArSPETIRIMLTGH 107
Cdd:PRK11517    2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRT-AKQTPVICLTAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 108 ANTDAVMGAINEGAvYKFILKPWNDDdlrvtvalalerfDLIARNRA-LKSENEKKSK-EISALAKLAATHR-SRLGIVL 184
Cdd:PRK11517   81 DSVDDRVRGLDSGA-NDYLVKPFSFS-------------ELLARVRAqLRQHHALNSTlEISGLRMDSVSQSvSRDNISI 146
                         170       180       190
                  ....*....|....*....|....*....|
gi 1308984715 185 hnkgALSAPQLQELTLLQERRKEPLIRLLL 214
Cdd:PRK11517  147 ----TLTRKEFQLLWLLASRAGEIIPRTVI 172
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
29-108 7.99e-03

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 36.87  E-value: 7.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715  29 LLFVDDEPGILKALTRVF-RQENYQVVT-ADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLREVKARSPETIRIMLTG 106
Cdd:cd19930     1 VLIAEDQEMVRGALAALLeLEDDLEVVAqASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80

                  ..
gi 1308984715 107 HA 108
Cdd:cd19930    81 FG 82
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
28-90 8.90e-03

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


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 37.04  E-value: 8.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308984715  28 RLLFVDDEPGILK-ALTRVFRQENYQVVTADSGAEGLQRLAEAETHLVISDFMMPAMNGAEFLR 90
Cdd:cd17530     2 RVLVLDDDPFQCMmAATILEDLGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLR 65
AAA_22 pfam13401
AAA domain;
496-574 9.52e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 36.94  E-value: 9.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308984715 496 QGIILATGPTGSGKTTTLYSLLQHDATPGKNYITIE-----DPVEYYLDMAGQVLVREKIGLTFPAVLRAILRQ-----D 565
Cdd:pfam13401   5 AGILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDlpsgtSPKDLLRALLRALGLPLSGRLSKEELLAALQQLllalaV 84

                  ....*....
gi 1308984715 566 PDVILLGEI 574
Cdd:pfam13401  85 AVVLIIDEA 93
 
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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