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Conserved domains on  [gi|2787114911|ref|WP_370264200|]
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ATP-binding protein [Limnobacter sp.]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TMAO_torS super family cl37193
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
595-1112 8.76e-100

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


The actual alignment was detected with superfamily member TIGR02956:

Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 338.68  E-value: 8.76e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  595 EKLLQE------ARMAAEAANHAKSNFLSIMSHEIRTPLNAIIGTSYLLGLDGLTDTQRSDVATINASSKNLLALINDVL 668
Cdd:TIGR02956  441 ERLNAEvknhakARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDIL 520
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  669 DFSKIEAGELELEQRPFQLQETLLDLRAMFTTLALQKGLTLRIaDAPEQTPPVLNGDSNRLKQILINLLNNAIKFTDEGE 748
Cdd:TIGR02956  521 DYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRL-NIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGS 599
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  749 VNLRISeYAPASPstvyLRFEVSDTGIGIPQTAQAKLFTPFMQAEAstSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPG 828
Cdd:TIGR02956  600 VVLRVS-LNDDSS----LLFEVEDTGCGIAEEEQATLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESELG 672
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  829 QGTQFTVDLPFAthhgaiQHAPSAlriepSALGNTTQTLKQVHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKK 908
Cdd:TIGR02956  673 VGSCFWFTLPLT------RGKPAE-----DSATLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALEC 741
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  909 LAQHpDVDAILMDLQMPEMDGCeTTLQIRKRLSA---DVPILALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALRG 985
Cdd:TIGR02956  742 FHQH-AFDLALLDINLPDGDGV-TLLQQLRAIYGaknEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAV 819
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  986 QVdlhpqnppeHNSAMNTTEPANDPWPKLP---GIDLDHAKNITLGDANFFVeLLNE---------------------FF 1041
Cdd:TIGR02956  820 IL---------AGGKSNTEAPVLSASPSFDsasVIENAQADDIPESNQASEF-LLDEeqlqqdievlgvekvrqlvalFK 889
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2787114911 1042 EENASCLSQLEAMLGKQAWDEAARVAHHIAGQAGNLGATALYQAAKAMELGCKQKAVGLePLLLELQRAYT 1112
Cdd:TIGR02956  890 TSSAEQLEELSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQLCQQLEKQGKTGALEL-SDIDEIKQAWQ 959
KinE super family cl47428
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
327-847 2.11e-55

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5809:

Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 200.97  E-value: 2.11e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  327 EERTKRLSESEARHRELAQlaersgqrlfkatrAASLGVWIWDLRDNTLIWDERMFELYGIphlaTSQAVDYGMWASRVH 406
Cdd:COG5809      4 SKMELQLRKSEQRFRSLFE--------------NAPDAILILDLEGKILKVNPAAERIFGY----TEDELLGTNILDFLH 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  407 PNDLEMaESRVKNLLENKGLYDP-EFRIILPDGSIRYIQANAFLERDELGAATHVVGLNQDVTLLRQSQVDLKEAQR--- 482
Cdd:COG5809     66 PDDEKE-LREILKLLKEGESRDElEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEkfr 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  483 -IAKV---GSWRFDINKQHVEWSEELYRMFGADPKGPaLNLEQQAAIFtPESWQRLEPAIASAVEDGTPYEIELQFTRSD 558
Cdd:COG5809    145 lIFNHspdGIIVTDLDGRIIYANPAACKLLGISIEEL-IGKSILELIH-SDDQENVAAFISQLLKDGGIAQGEVRFWTKD 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  559 GSMGWMLARGERvLDANGQPVYLRGTASDITTLKHQEKLLQearmAAEAANHAkSNFLSIMSHEIRTPLNAIIGTSYLLg 638
Cdd:COG5809    223 GRWRLLEASGAP-IKKNGEVDGIVIIFRDITERKKLEELLR----KSEKLSVV-GELAAGIAHEIRNPLTSLKGFIQLL- 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  639 LDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAGELEleqrPFQLQETLLDLRAMFTTLALQKGLTLRiADAPEQT 718
Cdd:COG5809    296 KDTIDEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYE----PKDLNTLIEEVIPLLQPQALLKNVQIE-LELEDDI 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  719 PPVLnGDSNRLKQILINLLNNAIKFTDEGeVNLRISEYAPASPstvYLRFEVSDTGIGIPQTAQAKLFTPFMqaeastSR 798
Cdd:COG5809    371 PDIL-GDENQLKQVFINLLKNAIEAMPEG-GNITIETKAEDDD---KVVISVTDEGCGIPEERLKKLGEPFY------TT 439
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2787114911  799 KYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFATHHGAIQ 847
Cdd:COG5809    440 KEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQVSM 488
PDC1_DGC_like cd12914
first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
61-186 5.03e-12

first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


:

Pssm-ID: 350339  Cd Length: 123  Bit Score: 63.94  E-value: 5.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911   61 LNDINTLLSILAQRYRDYPSKSQDTLyNLESQIRRELPFYQVALRIVVANAKGEQLLNTGKARDEQQNLPnliDRKFYQR 140
Cdd:cd12914      1 LDEADLLLRSLADDLEARGAASADPA-ALQALLRRLLARLPEVRSIFVVDADGRVVASSGPGPAPGLDVS---DRDYFQA 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2787114911  141 AIAGERGLMYEGPVPAKLDATWSIIMARPMVGSQGDFQGMVIAILP 186
Cdd:cd12914     77 ARAGGGGLFISEPVISRVTGKPVIPLSRPIRDADGRFAGVVVASID 122
PDC2_DGC_like cd12915
second PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
194-290 5.65e-12

second PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


:

Pssm-ID: 350340 [Multi-domain]  Cd Length: 96  Bit Score: 63.15  E-value: 5.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  194 FEMAELGENGVINLRTDDLSQVVRYPPAQGdalGVGNKKVPTKVTELLGNSPDQhqlVFEAASQLDGIERLYVYQKLSTS 273
Cdd:cd12915      6 YRSLDLGPGGAVALLRRDGTVLARYPDDEG---AVGRSLADPLFRALLAAAPSG---TFRAVSPLDGVERLYAYRRLPGY 79
                           90
                   ....*....|....*..
gi 2787114911  274 PFWLSVGLSMQPFEAGW 290
Cdd:cd12915     80 PLVVVVGLSEDDVLAPW 96
 
Name Accession Description Interval E-value
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
595-1112 8.76e-100

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 338.68  E-value: 8.76e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  595 EKLLQE------ARMAAEAANHAKSNFLSIMSHEIRTPLNAIIGTSYLLGLDGLTDTQRSDVATINASSKNLLALINDVL 668
Cdd:TIGR02956  441 ERLNAEvknhakARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDIL 520
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  669 DFSKIEAGELELEQRPFQLQETLLDLRAMFTTLALQKGLTLRIaDAPEQTPPVLNGDSNRLKQILINLLNNAIKFTDEGE 748
Cdd:TIGR02956  521 DYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRL-NIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGS 599
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  749 VNLRISeYAPASPstvyLRFEVSDTGIGIPQTAQAKLFTPFMQAEAstSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPG 828
Cdd:TIGR02956  600 VVLRVS-LNDDSS----LLFEVEDTGCGIAEEEQATLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESELG 672
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  829 QGTQFTVDLPFAthhgaiQHAPSAlriepSALGNTTQTLKQVHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKK 908
Cdd:TIGR02956  673 VGSCFWFTLPLT------RGKPAE-----DSATLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALEC 741
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  909 LAQHpDVDAILMDLQMPEMDGCeTTLQIRKRLSA---DVPILALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALRG 985
Cdd:TIGR02956  742 FHQH-AFDLALLDINLPDGDGV-TLLQQLRAIYGaknEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAV 819
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  986 QVdlhpqnppeHNSAMNTTEPANDPWPKLP---GIDLDHAKNITLGDANFFVeLLNE---------------------FF 1041
Cdd:TIGR02956  820 IL---------AGGKSNTEAPVLSASPSFDsasVIENAQADDIPESNQASEF-LLDEeqlqqdievlgvekvrqlvalFK 889
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2787114911 1042 EENASCLSQLEAMLGKQAWDEAARVAHHIAGQAGNLGATALYQAAKAMELGCKQKAVGLePLLLELQRAYT 1112
Cdd:TIGR02956  890 TSSAEQLEELSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQLCQQLEKQGKTGALEL-SDIDEIKQAWQ 959
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
605-1108 2.26e-90

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 311.40  E-value: 2.26e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  605 AEAANHAKSNFLSIMSHEIRTPLNAIIG-TSYLLGLDgLTDTQRSDVATINASSKNLLALINDVLDFSKIEAGELELEQR 683
Cdd:PRK11107   286 AQEAARIKSEFLANMSHELRTPLNGVIGfTRQTLKTP-LTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENI 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  684 PFQLQETLLDLRAMFTTLALQKGLTLRIaDAPEQTPPVLNGDSNRLKQILINLLNNAIKFTDEGEVNLRISEYApASPST 763
Cdd:PRK11107   365 PFSLRETLDEVVTLLAHSAHEKGLELTL-NIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRA-LSNTK 442
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  764 VYLRFEVSDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFATHH 843
Cdd:PRK11107   443 VQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNP 522
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  844 GAIQHAP--------SALRIEP---------------------------------------------SALGNTTQTLKQV 870
Cdd:PRK11107   523 NPIIDGLptdclagkRLLYVEPnsaaaqatldilsetplevtysptlsqlpeahydilllglpvtfrEPLTMLHERLAKA 602
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 ------------------------------------------------------------------HVMVVDDSEINLAI 884
Cdd:PRK11107   603 ksmtdflilalpcheqvlaeqlkqdgadaclskplshtrllpallepchhkqppllpptdesrlplTVMAVDDNPANLKL 682
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  885 TKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRK-RLSADVPILALTAGATTTEKDRALA 963
Cdd:PRK11107   683 IGALLEEQVEHVVLCDSGHQAVEQAKQRP-FDLILMDIQMPGMDGIRACELIRQlPHNQNTPIIAVTAHAMAGERERLLS 761
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  964 SGMNGFLTKPVDPPALIQALrgqvdLHPQNPPEHNSAMNTTEPANDPWPKLPGID----LDHAKNitlgDANFFVELLN- 1038
Cdd:PRK11107   762 AGMDDYLAKPIDEAMLKQVL-----LRYKPGPKFTSRVVAPEPPEPVHFPNATLDwqlaLRQAAG----KPDLARDMLQm 832
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2787114911 1039 --EFFEEnasCLSQLEAMLGKQAWDEAARVAHHIAGQAGNLGATALYQAAKAMELGCKQKAV--GLEPLLLELQ 1108
Cdd:PRK11107   833 llDFLPE---VRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQQLRSGTSveDLEPELLELL 903
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
597-840 2.45e-77

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 257.91  E-value: 2.45e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  597 LLQEARMAAEAANHAKSNFLSIMSHEIRTPLNAIIGTSYLLgLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAG 676
Cdd:COG0642     95 LLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELL-LEELDEEQREYLETILRSADRLLRLINDLLDLSRLEAG 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  677 ELELEQRPFQLQETLLDLRAMFTTLALQKGLTLRIaDAPEQTPPVlNGDSNRLKQILINLLNNAIKFTDEGEvNLRISey 756
Cdd:COG0642    174 KLELEPEPVDLAELLEEVVELFRPLAEEKGIELEL-DLPDDLPTV-RGDPDRLRQVLLNLLSNAIKYTPEGG-TVTVS-- 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  757 apASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFMQAEAStsRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVD 836
Cdd:COG0642    249 --VRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVT 324

                   ....
gi 2787114911  837 LPFA 840
Cdd:COG0642    325 LPLA 328
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
327-847 2.11e-55

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 200.97  E-value: 2.11e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  327 EERTKRLSESEARHRELAQlaersgqrlfkatrAASLGVWIWDLRDNTLIWDERMFELYGIphlaTSQAVDYGMWASRVH 406
Cdd:COG5809      4 SKMELQLRKSEQRFRSLFE--------------NAPDAILILDLEGKILKVNPAAERIFGY----TEDELLGTNILDFLH 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  407 PNDLEMaESRVKNLLENKGLYDP-EFRIILPDGSIRYIQANAFLERDELGAATHVVGLNQDVTLLRQSQVDLKEAQR--- 482
Cdd:COG5809     66 PDDEKE-LREILKLLKEGESRDElEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEkfr 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  483 -IAKV---GSWRFDINKQHVEWSEELYRMFGADPKGPaLNLEQQAAIFtPESWQRLEPAIASAVEDGTPYEIELQFTRSD 558
Cdd:COG5809    145 lIFNHspdGIIVTDLDGRIIYANPAACKLLGISIEEL-IGKSILELIH-SDDQENVAAFISQLLKDGGIAQGEVRFWTKD 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  559 GSMGWMLARGERvLDANGQPVYLRGTASDITTLKHQEKLLQearmAAEAANHAkSNFLSIMSHEIRTPLNAIIGTSYLLg 638
Cdd:COG5809    223 GRWRLLEASGAP-IKKNGEVDGIVIIFRDITERKKLEELLR----KSEKLSVV-GELAAGIAHEIRNPLTSLKGFIQLL- 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  639 LDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAGELEleqrPFQLQETLLDLRAMFTTLALQKGLTLRiADAPEQT 718
Cdd:COG5809    296 KDTIDEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYE----PKDLNTLIEEVIPLLQPQALLKNVQIE-LELEDDI 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  719 PPVLnGDSNRLKQILINLLNNAIKFTDEGeVNLRISEYAPASPstvYLRFEVSDTGIGIPQTAQAKLFTPFMqaeastSR 798
Cdd:COG5809    371 PDIL-GDENQLKQVFINLLKNAIEAMPEG-GNITIETKAEDDD---KVVISVTDEGCGIPEERLKKLGEPFY------TT 439
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2787114911  799 KYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFATHHGAIQ 847
Cdd:COG5809    440 KEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQVSM 488
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
729-839 1.30e-54

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 185.00  E-value: 1.30e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFTDEGEVNLRIsEYAPASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLS 808
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEGEVTLRV-SLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLA 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2787114911  809 IVKRLAELIGGAVFVQSTPGQGTQFTVDLPF 839
Cdd:cd16922     80 ISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
724-840 3.02e-36

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 132.77  E-value: 3.02e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911   724 GDSNRLKQILINLLNNAIKFTDEGeVNLRISeyapASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFMQAeASTSRKYGGT 803
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEG-GRITVT----LERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRT-DKRSRKIGGT 74
                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 2787114911   804 GLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFA 840
Cdd:smart00387   75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
724-841 7.13e-33

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 122.86  E-value: 7.13e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  724 GDSNRLKQILINLLNNAIKFT-DEGEVNLRISEYApaspstvYLRFEVSDTGIGIPQTAQAKLFTPFMQAEastSRKYGG 802
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAaKAGEITVTLSEGG-------ELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGG 70
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2787114911  803 TGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFAT 841
Cdd:pfam02518   71 TGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
615-857 1.13e-26

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 115.51  E-value: 1.13e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  615 FLSIMSHEIRTPLNAIIGTSYLL--GLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAGELELEQRPFQLQETLL 692
Cdd:NF040691   274 FVSDVSHELRTPLTTIRMAADVIhdSRDDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAELDVEPVDLRPLVR 353
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  693 DLRAMFTTLALQKGLTLRIaDAPEqTPPVLNGDSNRLKQILINLLNNAIKFTDEGEVNLRISeyapASPSTVYLRfeVSD 772
Cdd:NF040691   354 RVVDALRQLAERAGVELRV-DAPG-TPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVA----QDDTAVAVT--VRD 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  773 TGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFATHHGAIQhapSA 852
Cdd:NF040691   426 HGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLPRVAGDRLTT---SP 502

                   ....*
gi 2787114911  853 LRIEP 857
Cdd:NF040691   503 LPLVP 507
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
602-838 7.45e-24

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 106.45  E-value: 7.45e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  602 RMAAEAANHAKS--NFLSIMSHEIRTPLnAIIGTSYLLGLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAGELE 679
Cdd:NF012163   228 QLASTLEKNEQMrrDFMADISHELRTPL-AVLRAELEAIQDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALA 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  680 LEQRPFQLQETLLDLRAMFTTLALQKGLTLRIaDAPEQtpPVLNGDSNRLKQILINLLNNAIKFTDEGEvNLRISeyAPA 759
Cdd:NF012163   307 YQKASVDLVPLLEVEGGAFRERFASAGLELEV-SLPDS--SLVFGDRDRLMQLFNNLLENSLRYTDSGG-SLHIS--ASQ 380
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2787114911  760 SPSTVYLRFEvsDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:NF012163   381 RPKEVTLTVA--DSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
314-480 2.30e-22

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 104.37  E-value: 2.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  314 KLDHYSMG---LEQQVEERTKRLSESEARHRE------LAQ--------LAERSGQRLFK----ATRAASLGVWIWDLRD 372
Cdd:PRK09776   351 EINSYSMEkryYRRDGEVVWALLAVSLVRDTDgtplyfIAQiedinelkRTEQVNERLMEritlANEAGGIGIWEWDLKP 430
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  373 NTLIWDERMFELYGI-PHLATSqavdYGMWASRVHPNDLEMAESRVKNLLENKGLYDPEFRIILPDGsIRYIQANAFLER 451
Cdd:PRK09776   431 NIISWDKRMFELYEIpPHIKPT----WQVWYACLHPEDRQRVEKEIRDALQGRSPFKLEFRIVVKDG-VRHIRALANRVL 505
                          170       180
                   ....*....|....*....|....*....
gi 2787114911  452 DELGAATHVVGLNQDVTLLRQsqvdLKEA 480
Cdd:PRK09776   506 NKDGEVERLLGINMDMTEVRQ----LNEA 530
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
377-464 1.52e-15

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 72.76  E-value: 1.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  377 WDERMFELYGI-PHLATSQAVDygmWASRVHPNDLEMAESRVKNLLENKGLYDPEFRIILPDGSIRYIQANAFLERDELG 455
Cdd:pfam08447    4 WSPRFEEILGYtPEELLGKGES---WLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80

                   ....*....
gi 2787114911  456 AATHVVGLN 464
Cdd:pfam08447   81 KPVRVIGVA 89
PDC1_DGC_like cd12914
first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
61-186 5.03e-12

first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350339  Cd Length: 123  Bit Score: 63.94  E-value: 5.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911   61 LNDINTLLSILAQRYRDYPSKSQDTLyNLESQIRRELPFYQVALRIVVANAKGEQLLNTGKARDEQQNLPnliDRKFYQR 140
Cdd:cd12914      1 LDEADLLLRSLADDLEARGAASADPA-ALQALLRRLLARLPEVRSIFVVDADGRVVASSGPGPAPGLDVS---DRDYFQA 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2787114911  141 AIAGERGLMYEGPVPAKLDATWSIIMARPMVGSQGDFQGMVIAILP 186
Cdd:cd12914     77 ARAGGGGLFISEPVISRVTGKPVIPLSRPIRDADGRFAGVVVASID 122
PDC2_DGC_like cd12915
second PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
194-290 5.65e-12

second PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350340 [Multi-domain]  Cd Length: 96  Bit Score: 63.15  E-value: 5.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  194 FEMAELGENGVINLRTDDLSQVVRYPPAQGdalGVGNKKVPTKVTELLGNSPDQhqlVFEAASQLDGIERLYVYQKLSTS 273
Cdd:cd12915      6 YRSLDLGPGGAVALLRRDGTVLARYPDDEG---AVGRSLADPLFRALLAAAPSG---TFRAVSPLDGVERLYAYRRLPGY 79
                           90
                   ....*....|....*..
gi 2787114911  274 PFWLSVGLSMQPFEAGW 290
Cdd:cd12915     80 PLVVVVGLSEDDVLAPW 96
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
42-275 4.27e-11

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 64.28  E-value: 4.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911   42 LKNNAANTAEITAARIESSLNDINTLLSILAQRYrDYPSKSQDTLYNLESQIRRELPFYQVALRIVVANAKGEQLLNTGk 121
Cdd:pfam02743    7 AEEQLLSLAKQLAENIESYLDSLEEILELLASNP-DLQDLLSAPAEEELAKLESLLRSNPGISSIYLVDADGRVLASSD- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  122 aRDEQQNLPNLIDRKFYQRAIAGERGLM--YEGPVPAKLDATWSIIMARPMVGSQGDFQGMVIAILPTERLGMGFEMAEL 199
Cdd:pfam02743   85 -ESPSYPGLDVSERPWYKEALKGGGGIIwvFSSPYPSSESGEPVLTIARPIYDDDGEVIGVLVADLDLDTLQELLSQIKL 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2787114911  200 GENGVINLrTDDLSQVVrYPPAQGDALGVGNKKVPTKVTELLGNSPdqhqlVFEAASQLDGIERLYVYQKLSTSPF 275
Cdd:pfam02743  164 GEGGYVFI-VDSDGRIL-AHPLGKNLRSLLAPFLGKSLADALPGSG-----ITEIAVDLDGEDYLVAYAPIPGTGW 232
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
364-467 3.83e-09

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 55.33  E-value: 3.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  364 GVWIWDLRDNTLIWDERMFELYGIphlatSQAVDYGM-WASRVHPNDLEMAESRVKNLLENKGLYDPEFRIILPDGSIRY 442
Cdd:cd00130      4 GVIVLDLDGRILYANPAAEQLLGY-----SPEELIGKsLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIW 78
                           90       100
                   ....*....|....*....|....*
gi 2787114911  443 IQANAFLERDELGAATHVVGLNQDV 467
Cdd:cd00130     79 VLVSLTPIRDEGGEVIGLLGVVRDI 103
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
549-589 1.43e-06

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 46.02  E-value: 1.43e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 2787114911   549 EIELQFTRSDGSMGWMLARGERVLDANGQPVYLRGTASDIT 589
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDIT 41
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
484-598 4.99e-03

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 38.04  E-value: 4.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  484 AKVGSWRFDINKQHVEWSEELYRMFG---ADPKGpaLNLEQqaaIFTPESWQRLEpAIASAVEDGT--PYEIELQFTRSD 558
Cdd:TIGR00229   12 SPDAIIVIDLEGNILYVNPAFEEIFGysaEELIG--RNVLE---LIPEEDREEVR-ERIERRLEGEpePVSEERRVRRKD 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2787114911  559 GSMGWMLARGERVLDANGQPVYLrGTASDITTLKHQEKLL 598
Cdd:TIGR00229   86 GSEIWVEVSVSPIRTNGGELGVV-GIVRDITERKEAEEAL 124
 
Name Accession Description Interval E-value
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
595-1112 8.76e-100

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 338.68  E-value: 8.76e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  595 EKLLQE------ARMAAEAANHAKSNFLSIMSHEIRTPLNAIIGTSYLLGLDGLTDTQRSDVATINASSKNLLALINDVL 668
Cdd:TIGR02956  441 ERLNAEvknhakARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDIL 520
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  669 DFSKIEAGELELEQRPFQLQETLLDLRAMFTTLALQKGLTLRIaDAPEQTPPVLNGDSNRLKQILINLLNNAIKFTDEGE 748
Cdd:TIGR02956  521 DYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRL-NIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGS 599
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  749 VNLRISeYAPASPstvyLRFEVSDTGIGIPQTAQAKLFTPFMQAEAstSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPG 828
Cdd:TIGR02956  600 VVLRVS-LNDDSS----LLFEVEDTGCGIAEEEQATLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESELG 672
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  829 QGTQFTVDLPFAthhgaiQHAPSAlriepSALGNTTQTLKQVHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKK 908
Cdd:TIGR02956  673 VGSCFWFTLPLT------RGKPAE-----DSATLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALEC 741
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  909 LAQHpDVDAILMDLQMPEMDGCeTTLQIRKRLSA---DVPILALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALRG 985
Cdd:TIGR02956  742 FHQH-AFDLALLDINLPDGDGV-TLLQQLRAIYGaknEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAV 819
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  986 QVdlhpqnppeHNSAMNTTEPANDPWPKLP---GIDLDHAKNITLGDANFFVeLLNE---------------------FF 1041
Cdd:TIGR02956  820 IL---------AGGKSNTEAPVLSASPSFDsasVIENAQADDIPESNQASEF-LLDEeqlqqdievlgvekvrqlvalFK 889
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2787114911 1042 EENASCLSQLEAMLGKQAWDEAARVAHHIAGQAGNLGATALYQAAKAMELGCKQKAVGLePLLLELQRAYT 1112
Cdd:TIGR02956  890 TSSAEQLEELSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQLCQQLEKQGKTGALEL-SDIDEIKQAWQ 959
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
605-1108 2.26e-90

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 311.40  E-value: 2.26e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  605 AEAANHAKSNFLSIMSHEIRTPLNAIIG-TSYLLGLDgLTDTQRSDVATINASSKNLLALINDVLDFSKIEAGELELEQR 683
Cdd:PRK11107   286 AQEAARIKSEFLANMSHELRTPLNGVIGfTRQTLKTP-LTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENI 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  684 PFQLQETLLDLRAMFTTLALQKGLTLRIaDAPEQTPPVLNGDSNRLKQILINLLNNAIKFTDEGEVNLRISEYApASPST 763
Cdd:PRK11107   365 PFSLRETLDEVVTLLAHSAHEKGLELTL-NIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRA-LSNTK 442
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  764 VYLRFEVSDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFATHH 843
Cdd:PRK11107   443 VQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNP 522
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  844 GAIQHAP--------SALRIEP---------------------------------------------SALGNTTQTLKQV 870
Cdd:PRK11107   523 NPIIDGLptdclagkRLLYVEPnsaaaqatldilsetplevtysptlsqlpeahydilllglpvtfrEPLTMLHERLAKA 602
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 ------------------------------------------------------------------HVMVVDDSEINLAI 884
Cdd:PRK11107   603 ksmtdflilalpcheqvlaeqlkqdgadaclskplshtrllpallepchhkqppllpptdesrlplTVMAVDDNPANLKL 682
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  885 TKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRK-RLSADVPILALTAGATTTEKDRALA 963
Cdd:PRK11107   683 IGALLEEQVEHVVLCDSGHQAVEQAKQRP-FDLILMDIQMPGMDGIRACELIRQlPHNQNTPIIAVTAHAMAGERERLLS 761
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  964 SGMNGFLTKPVDPPALIQALrgqvdLHPQNPPEHNSAMNTTEPANDPWPKLPGID----LDHAKNitlgDANFFVELLN- 1038
Cdd:PRK11107   762 AGMDDYLAKPIDEAMLKQVL-----LRYKPGPKFTSRVVAPEPPEPVHFPNATLDwqlaLRQAAG----KPDLARDMLQm 832
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2787114911 1039 --EFFEEnasCLSQLEAMLGKQAWDEAARVAHHIAGQAGNLGATALYQAAKAMELGCKQKAV--GLEPLLLELQ 1108
Cdd:PRK11107   833 llDFLPE---VRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQQLRSGTSveDLEPELLELL 903
PRK15347 PRK15347
two component system sensor kinase;
598-1090 9.85e-85

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 295.40  E-value: 9.85e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  598 LQEARMAAEAANHAKSNFLSIMSHEIRTPLNAIIGTSYLLGLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAGE 677
Cdd:PRK15347   384 LAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQ 463
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  678 LELeqrpfQLQET----LLDlRAMFT--TLALQKGLTLRIADAPEqTPPVLNGDSNRLKQILINLLNNAIKFTDEGEVNL 751
Cdd:PRK15347   464 MTL-----SLEETallpLLD-QAMLTiqGPAQSKSLTLRTFVGAH-VPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRL 536
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  752 RISEYAPaspstvYLRFEVSDTGIGIPQTAQAKLFTPFMQAEASTsrkyGGTGLGLSIVKRLAELIGGAVFVQSTPGQGT 831
Cdd:PRK15347   537 RVKRHEQ------QLCFTVEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKMMGGELTLFSTPGVGS 606
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  832 QFTVDLPFATH------HGAIQhAPSALRIEPSALGNTTQT----------------------LK--------------- 868
Cdd:PRK15347   607 CFSLVLPLNEYappeplKGELS-APLALHRQLSAWGITCQPghqnpalldpelaylpgrlydlLQqiiqgapnepvinlp 685
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  869 ----QVHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALkKLAQHPDVDAILMDLQMPEMDGCETTLQIR---KRLS 941
Cdd:PRK15347   686 lqpwQLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEAL-ELGRQHRFDLVLMDIRMPGLDGLETTQLWRddpNNLD 764
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  942 ADVPILALTAGATTTEKDRALASGMNGFLTKPVDPPAL---------IQALRGqVDLHPQNPPEHnsamnttepandpwp 1012
Cdd:PRK15347   765 PDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLaralelaaeYQLLRG-IELSPQDSSCS--------------- 828
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2787114911 1013 klPGIDLDHAKnitlgdanffveLLNEFFEENASCLSQLEAMLGKQawDEAARVAHHIAGQAGNLGATALYQAAKAME 1090
Cdd:PRK15347   829 --PLLDTDDMA------------LNSKLYQSLLLLLAQIEQAVENQ--EVLSQLLHTLKGCAGQAGLTELQCAVIDLE 890
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
597-840 2.45e-77

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 257.91  E-value: 2.45e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  597 LLQEARMAAEAANHAKSNFLSIMSHEIRTPLNAIIGTSYLLgLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAG 676
Cdd:COG0642     95 LLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELL-LEELDEEQREYLETILRSADRLLRLINDLLDLSRLEAG 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  677 ELELEQRPFQLQETLLDLRAMFTTLALQKGLTLRIaDAPEQTPPVlNGDSNRLKQILINLLNNAIKFTDEGEvNLRISey 756
Cdd:COG0642    174 KLELEPEPVDLAELLEEVVELFRPLAEEKGIELEL-DLPDDLPTV-RGDPDRLRQVLLNLLSNAIKYTPEGG-TVTVS-- 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  757 apASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFMQAEAStsRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVD 836
Cdd:COG0642    249 --VRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVT 324

                   ....
gi 2787114911  837 LPFA 840
Cdd:COG0642    325 LPLA 328
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
548-1090 1.29e-74

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 263.72  E-value: 1.29e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  548 YEIELQFtrSDGSMGWMLARGERVLDANGQPVYLRGTASDITTLK-HQEKLlqearmaaEAANHAKSNFLSIMSHEIRTP 626
Cdd:PRK11091   228 YEQWLDY--PDGRKACFELRKVPFYDRVGKRHGLMGFGRDITERKrYQDAL--------EKASRDKTTFISTISHELRTP 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  627 LNAIIGTSYLLgLDG-LTDTQRSDVATINASSKNLLALINDVLDFSKIEAGELELEQRPFQLQETLLDLRAMFTTLALQK 705
Cdd:PRK11091   298 LNGIVGLSRIL-LDTeLTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQK 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  706 GLTLRIaDAPEQTPPVLNGDSNRLKQILINLLNNAIKFTDEGEVNLRISEYAPASpstvyLRFEVSDTGIGIPQTAQAKL 785
Cdd:PRK11091   377 GLRFDL-EPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYEEGDM-----LTFEVEDSGIGIPEDELDKI 450
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  786 FTPFMQAEASTSRKYG-GTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPfathhgaiqhAPSALRIEPSALGNTT 864
Cdd:PRK11091   451 FAMYYQVKDSHGGKPAtGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIH----------APAVAEEVEDAFDEDD 520
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  865 QTLKQVHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAqhPD-VDAILMDLQMPEMDGCETTLQIRKRLSAD 943
Cdd:PRK11091   521 MPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFD--PDeYDLVLLDIQLPDMTGLDIARELRERYPRE 598
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  944 --VPILALTAGAtTTEKDRALASGMNGFLTKPVDPPALIQALRGQVDLHPqnppehnsamnttEPANDPWPKLPGIDLDH 1021
Cdd:PRK11091   599 dlPPLVALTANV-LKDKKEYLDAGMDDVLSKPLSVPALTAMIKKFWDTQD-------------DEESTVTTEESSKANEA 664
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2787114911 1022 AKNITLgdANFFVELLN--------EFFEE-NASCLSQLEAMLGKQAWDEAARVAHHIAGQAGNLGATALYQAAKAME 1090
Cdd:PRK11091   665 LLDIPM--LEQYVELVGpklitdslAVFEKmMPGYLSVLDSNLTARDQKGIVEEAHKIKGAAGSVGLRHLQQLAQQIQ 740
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
598-841 8.83e-72

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 238.65  E-value: 8.83e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  598 LQEARMAAEAANHAKSNFLSIMSHEIRTPLNAIIGTSYLL--GLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEA 675
Cdd:COG2205      2 LEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLldEEDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLES 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  676 GELELEQRPFQLQETLLDLRAMFTTLALQKGLTLRIADAPEqtPPVLNGDSNRLKQILINLLNNAIKFTDEG-EVNLRIS 754
Cdd:COG2205     82 GKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPE--LPLVYADPELLEQVLANLLDNAIKYSPPGgTITISAR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  755 EYAPaspstvYLRFEVSDTGIGIPQTAQAKLFTPFMQAEasTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFT 834
Cdd:COG2205    160 REGD------GVRISVSDNGPGIPEEELERIFERFYRGD--NSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFT 231

                   ....*..
gi 2787114911  835 VDLPFAT 841
Cdd:COG2205    232 VTLPLAE 238
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
516-838 6.64e-70

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 239.45  E-value: 6.64e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  516 ALNLEQQAAIFTPESWQRLEPAIASAVEDGTPYEIELQFTRSDGSMGWMLARGERVLDANGQPVYLRGTASDITTLKHQE 595
Cdd:COG5002     69 LLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLL 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  596 KLLQEARMAAEAANHAKSNFLSIMSHEIRTPLNAIIGTSYLL--GLDGLTDTQRSDVATINASSKNLLALINDVLDFSKI 673
Cdd:COG5002    149 AAVERDITELERLEQMRREFVANVSHELRTPLTSIRGYLELLldGAADDPEERREYLEIILEEAERLSRLVNDLLDLSRL 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  674 EAGELELEQRPFQLQETLLDLRAMFTTLALQKGLTLRIADAPEqtPPVLNGDSNRLKQILINLLNNAIKFTDEG-EVNLR 752
Cdd:COG5002    229 ESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPED--PLLVLGDPDRLEQVLTNLLDNAIKYTPEGgTITVS 306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  753 ISEYAPaspstvYLRFEVSDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQ 832
Cdd:COG5002    307 LREEDD------QVRISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTT 380

                   ....*.
gi 2787114911  833 FTVDLP 838
Cdd:COG5002    381 FTITLP 386
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
587-983 1.18e-62

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 231.02  E-value: 1.18e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  587 DITTLKHQEKLLQEARMAAEAANHAKSNFLSIMSHEIRTPLNAIIGTSYLLGLDGLTDTQRSDVATINASSKNLLALIND 666
Cdd:PRK10841   422 DVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISD 501
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  667 VLDFSKIEAGELELEQRPFQLQETLLDLRAMFTTLALQKGLTLRIADAPEqTPPVLNGDSNRLKQILINLLNNAIKFTDE 746
Cdd:PRK10841   502 ILDFSKIESEQLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPD-VPVALNGDPMRLQQVISNLLSNAIKFTDT 580
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  747 GEVNL--RISEYapaspstvYLRFEVSDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQ 824
Cdd:PRK10841   581 GCIVLhvRVDGD--------YLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVD 652
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  825 STPGQGTQFTVDLP-----------------------------------FATHHGA------------------------ 845
Cdd:PRK10841   653 SEPGMGSQFTIRIPlygaqypqkkgveglqgkrcwlavrnasleqfletLLQRSGIqvqryegqeptpedvlitddpvqk 732
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  846 -------IQ------------------HAPSALRIEPSALGN--------------------TTQTLKQVHVMVVDDSEI 880
Cdd:PRK10841   733 kwqgravITfcrrhigipleiapgewvHSTATPHELPALLARiyrielesddsanalpstdkAVSDNDDMMILVVDDHPI 812
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  881 NLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKrLSADVPILALTAGATTTEKDR 960
Cdd:PRK10841   813 NRRLLADQLGSLGYQCKTANDGVDALNVLSKNH-IDIVLTDVNMPNMDGYRLTQRLRQ-LGLTLPVIGVTANALAEEKQR 890
                          490       500
                   ....*....|....*....|...
gi 2787114911  961 ALASGMNGFLTKPVDPPALIQAL 983
Cdd:PRK10841   891 CLEAGMDSCLSKPVTLDVLKQTL 913
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
599-1091 2.41e-57

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 214.77  E-value: 2.41e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  599 QEARMAAEAANHAKSNFLSIMSHEIRTPLNAIIGTSYLLGLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAG-- 676
Cdd:PRK11466   431 RQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGgk 510
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  677 ELELEQRPFQLQEtLLDLRAMFTTLALQKGLTLRIADAPEQTPPVLNGDSNRLKQILINLLNNAIKFTDEGEVNLRIsey 756
Cdd:PRK11466   511 NVSVSDEPFEPRP-LLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRS--- 586
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  757 apASPSTVYLrFEVSDTGIGIPQTAQAKLFTPFMQAEAstsrKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVD 836
Cdd:PRK11466   587 --RTDGEQWL-VEVEDSGCGIDPAKLAEIFQPFVQVSG----KRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLR 659
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  837 LPFATHHGAIQHAPsalriepsalgNTTQTLKQVHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPDVD 916
Cdd:PRK11466   660 LPLRVATAPVPKTV-----------NQAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEPFA 728
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  917 AILMDLQMPEMDGCETTLQIRKRLSADVPIlALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALRGQVDLHPQNppe 996
Cdd:PRK11466   729 AALVDFDLPDYDGITLARQLAQQYPSLVLI-GFSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLLAHYLQLQVNN--- 804
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  997 hNSAMNTTEPANDpwpklpgidldhaknITLGDANFFVELLNEFFEENASCLSQLEAMLGKQAWDEAARVAHHIAGQAGN 1076
Cdd:PRK11466   805 -DQPLDVSQLNED---------------AALMGTEKIHEWLALFKQHALPLLDEIDIARASQDSEKIKRAAHQLKSSCSS 868
                          490
                   ....*....|....*
gi 2787114911 1077 LGATALYQAAKAMEL 1091
Cdd:PRK11466   869 LGMRQASQACAQLEQ 883
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
327-847 2.11e-55

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 200.97  E-value: 2.11e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  327 EERTKRLSESEARHRELAQlaersgqrlfkatrAASLGVWIWDLRDNTLIWDERMFELYGIphlaTSQAVDYGMWASRVH 406
Cdd:COG5809      4 SKMELQLRKSEQRFRSLFE--------------NAPDAILILDLEGKILKVNPAAERIFGY----TEDELLGTNILDFLH 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  407 PNDLEMaESRVKNLLENKGLYDP-EFRIILPDGSIRYIQANAFLERDELGAATHVVGLNQDVTLLRQSQVDLKEAQR--- 482
Cdd:COG5809     66 PDDEKE-LREILKLLKEGESRDElEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEkfr 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  483 -IAKV---GSWRFDINKQHVEWSEELYRMFGADPKGPaLNLEQQAAIFtPESWQRLEPAIASAVEDGTPYEIELQFTRSD 558
Cdd:COG5809    145 lIFNHspdGIIVTDLDGRIIYANPAACKLLGISIEEL-IGKSILELIH-SDDQENVAAFISQLLKDGGIAQGEVRFWTKD 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  559 GSMGWMLARGERvLDANGQPVYLRGTASDITTLKHQEKLLQearmAAEAANHAkSNFLSIMSHEIRTPLNAIIGTSYLLg 638
Cdd:COG5809    223 GRWRLLEASGAP-IKKNGEVDGIVIIFRDITERKKLEELLR----KSEKLSVV-GELAAGIAHEIRNPLTSLKGFIQLL- 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  639 LDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAGELEleqrPFQLQETLLDLRAMFTTLALQKGLTLRiADAPEQT 718
Cdd:COG5809    296 KDTIDEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYE----PKDLNTLIEEVIPLLQPQALLKNVQIE-LELEDDI 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  719 PPVLnGDSNRLKQILINLLNNAIKFTDEGeVNLRISEYAPASPstvYLRFEVSDTGIGIPQTAQAKLFTPFMqaeastSR 798
Cdd:COG5809    371 PDIL-GDENQLKQVFINLLKNAIEAMPEG-GNITIETKAEDDD---KVVISVTDEGCGIPEERLKKLGEPFY------TT 439
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2787114911  799 KYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFATHHGAIQ 847
Cdd:COG5809    440 KEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQVSM 488
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
729-839 1.30e-54

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 185.00  E-value: 1.30e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFTDEGEVNLRIsEYAPASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLS 808
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEGEVTLRV-SLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLA 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2787114911  809 IVKRLAELIGGAVFVQSTPGQGTQFTVDLPF 839
Cdd:cd16922     80 ISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
336-838 3.98e-54

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 197.70  E-value: 3.98e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  336 SEARHRELAQLAERSGQRLFKATRAASLGVWIWDLRDNTLIWDERMFELYGIPHLATSQAVDYGMWASRVHPNDLEMAES 415
Cdd:COG4251      1 LLLLALLLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  416 RVKNLLENKGLYDPEFRIILPDGSIRYIQANAFLERDELGAATHVVGLNQDVTLLRQSQVDLKEAQRIAKVGSWRFDINK 495
Cdd:COG4251     81 LLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  496 QHVEWSEELYRMFGADPKGPALNLEQQAAIFTPESWQRLEPAIASAVEDGTPYEIELQFTRSDGSMGWMLARGERVLDAN 575
Cdd:COG4251    161 LLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  576 GQPVYLRGTASDITT-----LKHQEKLLQEARMAAEAANHAKSNFLSIMSHEIRTPLNAIIGTSYLLG---LDGLTDTQR 647
Cdd:COG4251    241 LILLLLLLILVLELLelrleLEELEEELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEedyGDKLDEEGR 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  648 SDVATINASSKNLLALINDVLDFSKIEAGELELEqrPFQLQETLLDLRAMFTTLALQKGLTLRIADAPeqtppVLNGDSN 727
Cdd:COG4251    321 EYLERIRDAAERMQALIDDLLAYSRVGRQELEFE--PVDLNELLEEVLEDLEPRIEERGAEIEVGPLP-----TVRGDPT 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  728 RLKQILINLLNNAIKFTDEGEVN-LRISeyapASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFMQAeaSTSRKYGGTGLG 806
Cdd:COG4251    394 LLRQVFQNLISNAIKYSRPGEPPrIEIG----AEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRL--HSRDEYEGTGIG 467
                          490       500       510
                   ....*....|....*....|....*....|..
gi 2787114911  807 LSIVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:COG4251    468 LAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
572-1091 1.09e-47

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 186.09  E-value: 1.09e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  572 LDANGQPVYLRGTaSDITTLKHQEKLLQEARMAAEAANHAKSNFLSIMSHEIRTPLNAIIGTSYLLGLDGLTDTQRSDVA 651
Cdd:PRK09959   673 LPASDHAVYICGW-QDITETRDLIHALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAI 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  652 TIN-ASSKNLLALINDVLDFSKIEAGELELEQRPFQLQETLLDLRAMFTTLALQKGLTLRIADA-PEQTppVLNGDSNRL 729
Cdd:PRK09959   752 SLAyATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTfPDHY--LVKIDPQAF 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  730 KQILINLLNNAIKFTDEGEVNLRISeYAPASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFMQaeASTSRKYGGTGLGLSI 809
Cdd:PRK09959   830 KQVLSNLLSNALKFTTEGAVKITTS-LGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMI 906
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  810 VKRLAELIGGAVFVQSTPGQGTQFTVDLPFAThhgaIQHAPSalrIEPSALGNTTQTlKQVHVMVVDDSEINLAITKRIL 889
Cdd:PRK09959   907 CKELIKNMQGDLSLESHPGIGTTFTITIPVEI----SQQVAT---VEAKAEQPITLP-EKLSILIADDHPTNRLLLKRQL 978
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  890 ECEGATVTLCNGGHQALKKLA-QHPDVdaILMDLQMPEMDGCETTLQIRKRLSAdVPILALTAGATTTEKDRALASGMNG 968
Cdd:PRK09959   979 NLLGYDVDEATDGVQALHKVSmQHYDL--LITDVNMPNMDGFELTRKLREQNSS-LPIWGLTANAQANEREKGLSCGMNL 1055
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  969 FLTKPVDPPALiqalrgqvdlhpqnppehNSAMNTTEPANDPWPKLPGIDLDHAKNITLGDANFFVELLNEFFEENASCL 1048
Cdd:PRK09959  1056 CLFKPLTLDVL------------------KTHLSQLHQVAHIAPQYRHLDIEALKNNTANDLQLMQEILMTFQHETHKDL 1117
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 2787114911 1049 SQleAMLGKQAWDEAA--RVAHHIAGQAGNLGATALYQAAKAMEL 1091
Cdd:PRK09959  1118 PA--AFHALEAGDNRTfhQCIHRIHGAANILNLQKLINISHQLEI 1160
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
533-845 2.44e-44

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 165.02  E-value: 2.44e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  533 RLEPAIASAVEDGTPY-EIELQFTRSDGSMGWMLARGERVLDANGQPVYLrGTASDITTLKHQEK-LLQEARMAA--EAA 608
Cdd:COG3852     61 PLRELLERALAEGQPVtEREVTLRRKDGEERPVDVSVSPLRDAEGEGGVL-LVLRDITERKRLEReLRRAEKLAAvgELA 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  609 nhaksnflSIMSHEIRTPLNAIIGTSYLLGLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAGELEleqrPFQLQ 688
Cdd:COG3852    140 --------AGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPERE----PVNLH 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  689 ETLLDLRAMFTTlALQKGLTLRIaDAPEQTPPVLnGDSNRLKQILINLLNNAIKFTDEG---EVNLRISEYAPASPSTV- 764
Cdd:COG3852    208 EVLERVLELLRA-EAPKNIRIVR-DYDPSLPEVL-GDPDQLIQVLLNLVRNAAEAMPEGgtiTIRTRVERQVTLGGLRPr 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  765 -YLRFEVSDTGIGIPQTAQAKLFTPFMqaeaSTsrKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFATHH 843
Cdd:COG3852    285 lYVRIEVIDNGPGIPEEILDRIFEPFF----TT--KEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAE 358

                   ..
gi 2787114911  844 GA 845
Cdd:COG3852    359 EE 360
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
451-840 5.04e-43

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 162.82  E-value: 5.04e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  451 RDELGAATHVvgLNQDVTLLRQSQVDLKEAQRI-------AKVGSWRFDINKQHVEWSEELYRMFGADPKGpalNLEQQA 523
Cdd:COG5000     61 DDEIGELARA--FNRMTDQLKEQREELEERRRYletilenLPAGVIVLDADGRITLANPAAERLLGIPLEE---LIGKPL 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  524 AIFTPESwqRLEPAIASAVEDGTPYEIELQFtrsdgsmgwmlaRGERVLDANGQPVYLRG---TASDITTLKHQEKLLQE 600
Cdd:COG5000    136 EELLPEL--DLAELLREALERGWQEEIELTR------------DGRRTLLVRASPLRDDGyviVFDDITELLRAERLAAW 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  601 ARMAAeaanhaksnflsIMSHEIRTPLNAIIGTSYLL------GLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIE 674
Cdd:COG5000    202 GELAR------------RIAHEIKNPLTPIQLSAERLrrkladKLEEDREDLERALDTIIRQVDRLKRIVDEFLDFARLP 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  675 AGELEleqrPFQLQETLLDLRAMFTTLALQKGLTLRIADAPEqtPPVLNGDSNRLKQILINLLNNAIKFTDE-GEVNLRi 753
Cdd:COG5000    270 EPQLE----PVDLNELLREVLALYEPALKEKDIRLELDLDPD--LPEVLADRDQLEQVLINLLKNAIEAIEEgGEIEVS- 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  754 seyapASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFMqaeasTSRKyGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQF 833
Cdd:COG5000    343 -----TRREDGRVRIEVSDNGPGIPEEVLERIFEPFF-----TTKP-KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTF 411

                   ....*..
gi 2787114911  834 TVDLPFA 840
Cdd:COG5000    412 TIRLPLA 418
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
496-840 4.49e-39

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 149.56  E-value: 4.49e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  496 QHVEWSEELYRMFGADPKGPALNLEQQAAIFTPESWQRLEPAIASAVEDGTPYEIELQFTRSDGSMGWMLARGERVLDAN 575
Cdd:COG4191     24 LLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLLLLAALDA 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  576 GQPVYLRGTASDITTLKH--------QEKLLQEARMAA--EAAnhaksnflSIMSHEIRTPLNAIIGTSYLL----GLDG 641
Cdd:COG4191    104 EENAELEELERDITELERaeeelrelQEQLVQSEKLAAlgELA--------AGIAHEINNPLAAILGNAELLrrrlEDEP 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  642 LTDTQRSDVATINASSKNLLALINDVLDFSKIEagelELEQRPFQLQETLLDLRAMFTTLALQKGLTLRIaDAPEQTPPV 721
Cdd:COG4191    176 DPEELREALERILEGAERAAEIVRSLRAFSRRD----EEEREPVDLNELIDEALELLRPRLKARGIEVEL-DLPPDLPPV 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  722 LnGDSNRLKQILINLLNNAIKFTDEGEVN-LRISEYAPASpstvYLRFEVSDTGIGIPQTAQAKLFTPFmqaeASTSRKY 800
Cdd:COG4191    251 L-GDPGQLEQVLLNLLINAIDAMEEGEGGrITISTRREGD----YVVISVRDNGPGIPPEVLERIFEPF----FTTKPVG 321
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 2787114911  801 GGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFA 840
Cdd:COG4191    322 KGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPLA 361
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
872-983 8.15e-39

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: 140.30  E-value: 8.15e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRK--RLSADVPILAL 949
Cdd:cd17546      1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEP-FDLVLMDLQMPVMDGLEATRRIREleGGGRRTPIIAL 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2787114911  950 TAGATTTEKDRALASGMNGFLTKPVDPPALIQAL 983
Cdd:cd17546     80 TANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
867-984 4.92e-37

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: 135.75  E-value: 4.92e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  867 LKQVHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRLS-ADVP 945
Cdd:COG0784      3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGP-PDLILLDINMPGMDGLELLRRIRALPRlPDIP 81
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2787114911  946 ILALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:COG0784     82 IIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALR 120
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
724-840 3.02e-36

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 132.77  E-value: 3.02e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911   724 GDSNRLKQILINLLNNAIKFTDEGeVNLRISeyapASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFMQAeASTSRKYGGT 803
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEG-GRITVT----LERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRT-DKRSRKIGGT 74
                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 2787114911   804 GLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFA 840
Cdd:smart00387   75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
585-837 1.20e-33

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems]


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 132.72  E-value: 1.20e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  585 ASDITTLKHQEkllqeaRMaaeaanhaKSNFLSIMSHEIRTPLNAIIGtsYLLGLDGLTD----TQRSDVATINASSKNL 660
Cdd:TIGR02966  101 ARDVTRLRRLE------QM--------RRDFVANVSHELRTPLTVLRG--YLETLADGPDedpeEWNRALEIMLEQSQRM 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  661 LALINDVLDFSKIEAGELELEQRPFQLQETLLDLRAMFTTLALQKGLTLRIADAPeqtPPVLNGDSNRLKQILINLLNNA 740
Cdd:TIGR02966  165 QSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEALSQGKNHQITFEIDG---GVDVLGDEDELRSAFSNLVSNA 241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  741 IKFT-DEGEVNLRISEYAPAspstvyLRFEVSDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLSIVKRLAELIGG 819
Cdd:TIGR02966  242 IKYTpEGGTITVRWRRDGGG------AEFSVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHA 315
                          250
                   ....*....|....*...
gi 2787114911  820 AVFVQSTPGQGTQFTVDL 837
Cdd:TIGR02966  316 RLEIESELGKGSTFSFIF 333
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
724-841 7.13e-33

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 122.86  E-value: 7.13e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  724 GDSNRLKQILINLLNNAIKFT-DEGEVNLRISEYApaspstvYLRFEVSDTGIGIPQTAQAKLFTPFMQAEastSRKYGG 802
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAaKAGEITVTLSEGG-------ELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGG 70
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2787114911  803 TGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFAT 841
Cdd:pfam02518   71 TGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
871-983 1.84e-32

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: 124.64  E-value: 1.84e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKR-LSADVPILAL 949
Cdd:COG3706      3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHR-PDLILLDLEMPDMDGLELCRRLRADpRTADIPIIFL 81
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2787114911  950 TAGATTTEKDRALASGMNGFLTKPVDPPALIQAL 983
Cdd:COG3706     82 TALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
866-990 8.38e-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: 118.34  E-value: 8.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  866 TLKQVHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKR-LSADV 944
Cdd:COG3437      3 TGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAP-PDLILLDVRMPGMDGFELLRLLRADpSTRDI 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2787114911  945 PILALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALRGQVDLH 990
Cdd:COG3437     82 PVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELR 127
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
365-838 1.80e-29

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 124.07  E-value: 1.80e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  365 VWIWDLRDNTLIWDERMFELYGIphlaTSQAVDYGMWASRVHPNDLEMAESRVKNLLENKGLYDPEFRIILpDGSIRYIQ 444
Cdd:COG5805     47 IIAVNREGKVIYINPAMEKLLGY----TSEEIIGKTIFDFLEKEYHYRVKTRIERLQKGYDVVMIEQIYCK-DGELIYVE 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  445 ANAFLERDELGAAThvVGLNQDVTLLRQSQVDLKEA----QRIAKVGS---WRFDINKQHVEWSEELYRMFGADPKgpAL 517
Cdd:COG5805    122 VKLFPIYNQNGQAA--ILALRDITKKKKIEEILQEQeerlQTLIENSPdliCVIDTDGRILFINESIERLFGAPRE--EL 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  518 NLEQQAAIFTPESWQRLEPAIASAVEDGTPYEIELQFTRSDGSMGWMLARGERVLDANGQPVYLRGTASDITTLKHQEKL 597
Cdd:COG5805    198 IGKNLLELLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEEL 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  598 LqearmaaeaanhAKSNFLSI-------MSHEIRTPLNAIIGTSYLLGLdGLTDTQ------RSDVATINASSKNLLALi 664
Cdd:COG5805    278 M------------ARSEKLSIagqlaagIAHEIRNPLTSIKGFLQLLQP-GIEDKEeyfdimLSELDRIESIISEFLAL- 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  665 ndvldfskieAGELELEQRPFQLQETLLDLRAMFTTLALQKGLTLRiADAPEQTPPVLnGDSNRLKQILINLLNNAIK-F 743
Cdd:COG5805    344 ----------AKPQAVNKEKENINELIQDVVTLLETEAILHNIQIR-LELLDEDPFIY-CDENQIKQVFINLIKNAIEaM 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  744 TDEGEVNLRISEYApaspSTVYLRfeVSDTGIGIPQTAQAKLFTPFMqaeaSTSRKygGTGLGLSIVKRLAELIGGAVFV 823
Cdd:COG5805    412 PNGGTITIHTEEED----NSVIIR--VIDEGIGIPEERLKKLGEPFF----TTKEK--GTGLGLMVSYKIIENHNGTIDI 479
                          490
                   ....*....|....*
gi 2787114911  824 QSTPGQGTQFTVDLP 838
Cdd:COG5805    480 DSKVGKGTTFTITLP 494
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
869-984 3.02e-29

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: 116.21  E-value: 3.02e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  869 QVHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRlSADVPILA 948
Cdd:COG0745      1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEER-PDLILLDLMLPGMDGLEVCRRLRAR-PSDIPIIM 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2787114911  949 LTAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:COG0745     79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIR 114
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
619-840 2.54e-27

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 117.25  E-value: 2.54e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  619 MSHEIRTPLNAIIGTSYLLGLDGLTDTQRSDVATINASSKNLLALINDVLDFSKieageleLEQRPFQLQETLLDLRAMF 698
Cdd:PRK11100   263 LTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELAR-------LEQRQELEVLEPVALAALL 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  699 TTL-------ALQKGLTLRIADAPeqtpPVLNGDSNRLKQILINLLNNAIKFTDEG-EVNLRiseyapASPSTVYLRFEV 770
Cdd:PRK11100   336 EELveareaqAAAKGITLRLRPDD----ARVLGDPFLLRQALGNLLDNAIDFSPEGgTITLS------AEVDGEQVALSV 405
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2787114911  771 SDTGIGIPQTAQAKLFTPFMqaeaSTSRKYGG---TGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFA 840
Cdd:PRK11100   406 EDQGPGIPDYALPRIFERFY----SLPRPANGrksTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPRH 474
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
872-984 2.56e-27

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 107.24  E-value: 2.56e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHpDVDAILMDLQMPEMDGCETTLQIRKRlSADVPILALTA 951
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEE-RPDLILLDINMPGMDGLELLKRIRRR-DPTTPVIILTA 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2787114911  952 GATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:pfam00072   79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
872-983 3.04e-27

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: 107.16  E-value: 3.04e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQIRKR-LSADVPILAL 949
Cdd:cd17580      1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFrPDV--ILSDIGMPGMDGYELARRLRELpWLANTPAIAL 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2787114911  950 TAGATTTEKDRALASGMNGFLTKPVDPPALIQAL 983
Cdd:cd17580     79 TGYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
615-857 1.13e-26

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 115.51  E-value: 1.13e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  615 FLSIMSHEIRTPLNAIIGTSYLL--GLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAGELELEQRPFQLQETLL 692
Cdd:NF040691   274 FVSDVSHELRTPLTTIRMAADVIhdSRDDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAELDVEPVDLRPLVR 353
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  693 DLRAMFTTLALQKGLTLRIaDAPEqTPPVLNGDSNRLKQILINLLNNAIKFTDEGEVNLRISeyapASPSTVYLRfeVSD 772
Cdd:NF040691   354 RVVDALRQLAERAGVELRV-DAPG-TPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVA----QDDTAVAVT--VRD 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  773 TGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFATHHGAIQhapSA 852
Cdd:NF040691   426 HGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLPRVAGDRLTT---SP 502

                   ....*
gi 2787114911  853 LRIEP 857
Cdd:NF040691   503 LPLVP 507
PRK13557 PRK13557
histidine kinase; Provisional
528-988 1.53e-26

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 115.54  E-value: 1.53e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  528 PESWQRLEPAIASAVEDGTpyeiELQFTRSDGSMGWMLARGERVLDANGQPVYLRGTASDITTLKHQEKLLQEAR-MAA- 605
Cdd:PRK13557    88 RATVAEVRDAIAERREIAT----EILNYRKDGSSFWNALFVSPVYNDAGDLVYFFGSQLDVSRRRDAEDALRQAQkMEAl 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  606 ----EAANHAKSNFLSIMSheirtplnaiigtSYLLGLDGLTDTQRSDVATINASSKNLLA-------LINDVLDFSKie 674
Cdd:PRK13557   164 gqltGGIAHDFNNLLQVMS-------------GYLDVIQAALSHPDADRGRMARSVENIRAaaeraatLTQQLLAFAR-- 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  675 agelelEQRpfqLQETLLDLRAMFTTL------ALQKGLTLRIADAPEQTPPVLngDSNRLKQILINLLNNAIKFTDEGE 748
Cdd:PRK13557   229 ------KQR---LEGRVLNLNGLVSGMgelaerTLGDAVTIETDLAPDLWNCRI--DPTQAEVALLNVLINARDAMPEGG 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  749 V------NLRISEYAPASPSTV----YLRFEVSDTGIGIPQTAQAKLFTPFMqaeasTSRKYG-GTGLGLSIVKRLAELI 817
Cdd:PRK13557   298 RvtirtrNVEIEDEDLAMYHGLppgrYVSIAVTDTGSGMPPEILARVMDPFF-----TTKEEGkGTGLGLSMVYGFAKQS 372
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  818 GGAVFVQSTPGQGTqfTVDLPFATHHGAIQHAPSALRIEPSALGNTTqtlkqvhVMVVDDSEINLAITKRILECEGATVT 897
Cdd:PRK13557   373 GGAVRIYSEVGEGT--TVRLYFPASDQAENPEQEPKARAIDRGGTET-------ILIVDDRPDVAELARMILEDFGYRTL 443
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  898 LCNGGHQALKKLAQHPDVDAILMDLQMP-EMDGCETTLQIRKRLsADVPILaLTAGATTTEKDRALASGmNGF--LTKPV 974
Cdd:PRK13557   444 VASNGREALEILDSHPEVDLLFTDLIMPgGMNGVMLAREARRRQ-PKIKVL-LTTGYAEASIERTDAGG-SEFdiLNKPY 520
                          490
                   ....*....|....
gi 2787114911  975 DPPALIQALRGQVD 988
Cdd:PRK13557   521 RRAELARRVRMVLD 534
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
725-838 1.31e-24

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain.


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 99.49  E-value: 1.31e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  725 DSNRLKQILINLLNNAIKFT-DEGEVNLRISEYAPAspstvYLRFEVSDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGT 803
Cdd:cd16925      1 DAEKYERVVLNLLSNAFKFTpDGGRIRCILEKFRLN-----RFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGT 75
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  804 GLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16925     76 GLGLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
551-838 1.93e-24

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 109.67  E-value: 1.93e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  551 ELQFTRSDGSMGwMLARGERVLDANGQPVYLRGTASDITTLKH-QEKLLQEARMAAEAanhaksNFLSIMSHEIRTPLNA 629
Cdd:PRK11360   335 EISFPGRDRTIE-LSVSTSLLHNTHGEMIGALVIFSDLTERKRlQRRVARQERLAALG------ELVAGVAHEIRNPLTA 407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  630 IIG-TSYLLGLDGLTDTQRSdVATINASSKNLLALINDVLDFSKIEagelELEQRPFQLQETLLDLRAMFTTLALQKGLT 708
Cdd:PRK11360   408 IRGyVQIWRQQTSDPPSQEY-LSVVLREVDRLNKVIDQLLEFSRPR----ESQWQPVSLNALVEEVLQLFQTAGVQARVD 482
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  709 LRIADAPEQTPPVLNGDSnrLKQILINLLNNAIK-FTDEGEVNLRISEYAPAspsTVYLrfEVSDTGIGIPQTAQAKLFT 787
Cdd:PRK11360   483 FETELDNELPPIWADPEL--LKQVLLNILINAVQaISARGKIRIRTWQYSDG---QVAV--SIEDNGCGIDPELLKKIFD 555
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2787114911  788 PFMQAEAStsrkygGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:PRK11360   556 PFFTTKAK------GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLP 600
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
602-838 7.45e-24

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 106.45  E-value: 7.45e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  602 RMAAEAANHAKS--NFLSIMSHEIRTPLnAIIGTSYLLGLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAGELE 679
Cdd:NF012163   228 QLASTLEKNEQMrrDFMADISHELRTPL-AVLRAELEAIQDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALA 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  680 LEQRPFQLQETLLDLRAMFTTLALQKGLTLRIaDAPEQtpPVLNGDSNRLKQILINLLNNAIKFTDEGEvNLRISeyAPA 759
Cdd:NF012163   307 YQKASVDLVPLLEVEGGAFRERFASAGLELEV-SLPDS--SLVFGDRDRLMQLFNNLLENSLRYTDSGG-SLHIS--ASQ 380
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2787114911  760 SPSTVYLRFEvsDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:NF012163   381 RPKEVTLTVA--DSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
PRK09303 PRK09303
histidine kinase;
610-838 1.08e-23

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 104.65  E-value: 1.08e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  610 HAKSNFLSIMSHEIRTPLNA--------------IIGTSYLLGLDGLTDTQRSDVATINAssknllaLINDVLDFSKIEA 675
Cdd:PRK09303   149 KFKDRVLAMLAHDLRTPLTAaslaletlelgqidEDTELKPALIEQLQDQARRQLEEIER-------LITDLLEVGRTRW 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  676 GELELEQRPFQL----QETLLDLRAMFTTlalqKGLTLrIADAPEQTPPVLnGDSNRLKQILINLLNNAIKFT-DEGEVN 750
Cdd:PRK09303   222 EALRFNPQKLDLgslcQEVILELEKRWLA----KSLEI-QTDIPSDLPSVY-ADQERIRQVLLNLLDNAIKYTpEGGTIT 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  751 LRISEYapaspSTVYLRFEVSDTGIGIPQTAQAKLF--TPFMQAEASTSrkygGTGLGLSIVKRLAELIGGAVFVQSTPG 828
Cdd:PRK09303   296 LSMLHR-----TTQKVQVSICDTGPGIPEEEQERIFedRVRLPRDEGTE----GYGIGLSVCRRIVRVHYGQIWVDSEPG 366
                          250
                   ....*....|
gi 2787114911  829 QGTQFTVDLP 838
Cdd:PRK09303   367 QGSCFHFTLP 376
PAS COG2202
PAS domain [Signal transduction mechanisms];
342-598 1.70e-23

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 101.25  E-value: 1.70e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  342 ELAQLAERSGQRLFKATRAASLGVWIWDLRDNTLIWDERMFELYGIphlaTSQAVDYGMWASRVHPNDLEMAESRVKNLL 421
Cdd:COG2202      1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGY----SAEELLGKTLRDLLPPEDDDEFLELLRAAL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  422 ENKGLYDPEFRIILPDGSIRYIQANAFLERDELGAATHVVGLNQDVTLLRQSQVDLKEAQRI-------AKVGSWRFDIN 494
Cdd:COG2202     77 AGGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERlrllvenAPDGIFVLDLD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  495 KQHVEWSEELYRMFGADPKgpALNLEQQAAIFTPESWQRLEPAIASAVEDG-TPYEIELQFTRSDGSMGWMLARGERVLD 573
Cdd:COG2202    157 GRILYVNPAAEELLGYSPE--ELLGKSLLDLLHPEDRERLLELLRRLLEGGrESYELELRLKDGDGRWVWVEASAVPLRD 234
                          250       260
                   ....*....|....*....|....*
gi 2787114911  574 aNGQPVYLRGTASDITTLKHQEKLL 598
Cdd:COG2202    235 -GGEVIGVLGIVRDITERKRAEEAL 258
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
870-979 4.16e-23

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: 95.54  E-value: 4.16e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  870 VHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHP-DVDAILMDLQMPEMDGCETTLQIRKRLSADVP--I 946
Cdd:cd19933      1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEhSFQLVLLDLCMPEMDGFEVALRIRKLFGRRERplI 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2787114911  947 LALTAGATTTEKDRALASGMNGFLTKPVDPPAL 979
Cdd:cd19933     81 VALTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
873-973 1.08e-22

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: 93.45  E-value: 1.08e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  873 MVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRlSADVPILALTAG 952
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREER-PDLVLLDLMMPGMDGLELLRKLREL-PPDIPVIVLTAK 78
                           90       100
                   ....*....|....*....|.
gi 2787114911  953 ATTTEKDRALASGMNGFLTKP 973
Cdd:cd00156     79 ADEEDAVRALELGADDYLVKP 99
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
871-980 1.33e-22

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: 94.05  E-value: 1.33e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILECEGAT-VTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRLS-ADVPILA 948
Cdd:cd17551      2 RILIVDDNPTNLLLLEALLRSAGYLeVVSFTDPREALAWCRENP-PDLILLDYMMPGMDGLEFIRRLRALPGlEDVPIVM 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  949 LTAgatTTEKD---RALASGMNGFLTKPVDPPALI 980
Cdd:cd17551     81 ITA---DTDREvrlRALEAGATDFLTKPFDPVELL 112
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
592-987 1.47e-22

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 104.37  E-value: 1.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  592 KHQEKLLQEARMAAEAANHAKSNFLSIMSHEIRTPLNAIIGTSYLlGLDGLTDTQRS--DVATINASSKNLLALINDVLD 669
Cdd:PRK13837   430 LETERDALERRLEHARRLEAVGTLASGIAHNFNNILGAILGYAEM-ALNKLARHSRAarYIDEIISAGARARLIIDQILA 508
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  670 FSKieagELELEQRPFQLQETLLDLRAMFTtLALQKGLTLRIADAPEQTppVLNGDSNRLKQILINLLNNAIK-FTDEGE 748
Cdd:PRK13837   509 FGR----KGERNTKPFDLSELVTEIAPLLR-VSLPPGVELDFDQDQEPA--VVEGNPAELQQVLMNLCSNAAQaMDGAGR 581
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  749 VNLRISEYAPASPSTV---------YLRFEVSDTGIGIPQTAQAKLFTPFMqaeasTSRKyGGTGLGLSIVKRLAELIGG 819
Cdd:PRK13837   582 VDISLSRAKLRAPKVLshgvlppgrYVLLRVSDTGAGIDEAVLPHIFEPFF-----TTRA-GGTGLGLATVHGIVSAHAG 655
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  820 AVFVQSTPGQGTQFTVDLPFATHhgaIQHAPSALRIEPSALGNTTQTlkqvhVMVVDDSEINLAITKRIL---------- 889
Cdd:PRK13837   656 YIDVQSTVGRGTRFDVYLPPSSK---VPVAPQAFFGPGPLPRGRGET-----VLLVEPDDATLERYEEKLaalgyepvgf 727
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  890 -ECEGAtVTLCNGGHQALkklaqhpdvDAILMDLQMPEMDGCETTLQirkRLSADVPILALTAGATTTEKDRALASGMNg 968
Cdd:PRK13837   728 sTLAAA-IAWISKGPERF---------DLVLVDDRLLDEEQAAAALH---AAAPTLPIILGGNSKTMALSPDLLASVAE- 793
                          410
                   ....*....|....*....
gi 2787114911  969 FLTKPVDPPALIQALRGQV 987
Cdd:PRK13837   794 ILAKPISSRTLAYALRTAL 812
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
613-838 1.83e-22

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 102.08  E-value: 1.83e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  613 SNFLSIMSHEIRTPLNAIIG-TSYLLGLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAGELELEQRPFQLQETL 691
Cdd:TIGR01386  242 SQFSADLAHELRTPLTNLLGqTQVALSQPRTGEEYREVLESNLEELERLSRMVSDMLFLARADNGQLALERVRLDLAAEL 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  692 LDLRAMFTTLALQKGLTLRIadapeQTPPVLNGDSNRLKQILINLLNNAIKFT-DEGEVNLRISEYAPAspstvyLRFEV 770
Cdd:TIGR01386  322 AKVAEYFEPLAEERGVRIRV-----EGEGLVRGDPQMFRRAISNLLSNALRHTpDGGTITVRIERRSDE------VRVSV 390
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2787114911  771 SDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQStPGQGTQFTVDLP 838
Cdd:TIGR01386  391 SNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAES-PDGKTRFILRFP 457
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
314-480 2.30e-22

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 104.37  E-value: 2.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  314 KLDHYSMG---LEQQVEERTKRLSESEARHRE------LAQ--------LAERSGQRLFK----ATRAASLGVWIWDLRD 372
Cdd:PRK09776   351 EINSYSMEkryYRRDGEVVWALLAVSLVRDTDgtplyfIAQiedinelkRTEQVNERLMEritlANEAGGIGIWEWDLKP 430
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  373 NTLIWDERMFELYGI-PHLATSqavdYGMWASRVHPNDLEMAESRVKNLLENKGLYDPEFRIILPDGsIRYIQANAFLER 451
Cdd:PRK09776   431 NIISWDKRMFELYEIpPHIKPT----WQVWYACLHPEDRQRVEKEIRDALQGRSPFKLEFRIVVKDG-VRHIRALANRVL 505
                          170       180
                   ....*....|....*....|....*....
gi 2787114911  452 DELGAATHVVGLNQDVTLLRQsqvdLKEA 480
Cdd:PRK09776   506 NKDGEVERLLGINMDMTEVRQ----LNEA 530
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
545-838 3.52e-22

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 100.31  E-value: 3.52e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  545 GTPYEIELQFTRSDGSMGWMLARGERVLDANGQPVYLRG-------TASDITTLKHQEKLLQEARMAAEAanhaksnfLS 617
Cdd:COG3290    123 GRPIDEVLAEVLETGERDEEILLNGRVLVVNRVPIRDDGrvvgavaTFRDRTELERLEEELEGVKELAEA--------LR 194
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  618 IMSHEIRTPLNAIigtsyllglDGLTDTQRSD--VATINASSKNLLALINDVLDFSKIEAgeleleqrpfqLQETLLDlr 695
Cdd:COG3290    195 AQRHDFRNHLHTI---------SGLLQLGEYDeaLEYIDEISEELQELIDSLLSRIGNPV-----------LAALLLG-- 252
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  696 amFTTLALQKGLTLRIAdaPEQTPPVLNGDSNRLKQILINLLNNAI-----KFTDEGEVNLRISEYAPaspstvYLRFEV 770
Cdd:COG3290    253 --KAARARERGIDLTID--IDSDLPDLPLSDTDLVTILGNLLDNAIeavekLPEEERRVELSIRDDGD------ELVIEV 322
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2787114911  771 SDTGIGIPQTAQAKLFTP-FmqaeasTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:COG3290    323 EDSGPGIPEELLEKIFERgF------STKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLP 385
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
872-984 7.62e-22

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: 91.83  E-value: 7.62e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQIRKRLS-ADVPILAL 949
Cdd:cd17548      2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEkPDL--ILMDIQLPGMDGLEATRLLKEDPAtRDIPVIAL 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  950 TAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:cd17548     80 TAYAMKGDREKILEAGCDGYISKPIDTREFLETVA 114
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
615-842 1.03e-21

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 99.71  E-value: 1.03e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  615 FLSIMSHEIRTPLNAIIGTsyllgLDGLTDTQR----SDVATINASSKNLLALINDVLDFSKIEAGELELEQRPFQLQET 690
Cdd:PRK10549   243 FMADISHELRTPLAVLRGE-----LEAIQDGVRkftpESVASLQAEVGTLTKLVDDLHQLSLSDEGALAYRKTPVDLVPL 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  691 LLDLRAMFTTLALQKGLTLRIaDAPEQTPpvLNGDSNRLKQILINLLNNAIKFTDEGEvNLRISeyAPASPSTVYLRFEV 770
Cdd:PRK10549   318 LEVAGGAFRERFASRGLTLQL-SLPDSAT--VFGDPDRLMQLFNNLLENSLRYTDSGG-SLHIS--AEQRDKTLRLTFAD 391
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2787114911  771 SDTGIGIPQtaQAKLFTPFMQAEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFATH 842
Cdd:PRK10549   392 SAPGVSDEQ--LQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAHSPFGGVSITVELPLERD 461
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
612-838 6.16e-21

Cu(+)/Ag(+) sensor histidine kinase;


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 97.54  E-value: 6.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  612 KSNFLSIMSHEIRTPLNAIIGTSYLLGLDGLTDTQRSDVATINASSKNLLA-LINDVLDFSKIEAGELELEQRPFQLQET 690
Cdd:PRK09835   262 QSNFSADIAHEIRTPITNLITQTEIALSQSRSQKELEDVLYSNLEELTRMAkMVSDMLFLAQADNNQLIPEKKMLDLADE 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  691 LLDLRAMFTTLALQKGLTLRIadapEQTPPVLNGDSNRLKQILINLLNNAIKFTDEGE-VNLRISEYAPAspstvyLRFE 769
Cdd:PRK09835   342 VGKVFDFFEAWAEERGVELRF----VGDPCQVAGDPLMLRRAISNLLSNALRYTPAGEaITVRCQEVDHQ------VQLV 411
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2787114911  770 VSDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPgQGTQFTVDLP 838
Cdd:PRK09835   412 VENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVISLP 479
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
871-974 1.18e-20

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: 87.94  E-value: 1.18e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQIRKR-LSADVPILA 948
Cdd:cd17538      1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEElPDL--ILLDVMMPGMDGFEVCRRLKEDpETRHIPVIM 78
                           90       100
                   ....*....|....*....|....*.
gi 2787114911  949 LTAGATTTEKDRALASGMNGFLTKPV 974
Cdd:cd17538     79 ITALDDREDRIRGLEAGADDFLSKPI 104
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
868-984 1.94e-20

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: 95.42  E-value: 1.94e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  868 KQVHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRlSADVPIL 947
Cdd:COG2204      1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEP-PDLVLLDLRMPGMDGLELLRELRAL-DPDLPVI 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2787114911  948 ALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:COG2204     79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVE 115
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
724-837 4.05e-20

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 86.69  E-value: 4.05e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  724 GDSNRLKQILINLLNNAIKFTDEG-EVNLRISEYAPAspstvylRFEVSDTGIGIPQTAQAKLFTPFMQaeaSTSRKYGG 802
Cdd:cd16940      9 GDALLLFLLLRNLVDNAVRYSPQGsRVEIKLSADDGA-------VIRVEDNGPGIDEEELEALFERFYR---SDGQNYGG 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  803 TGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDL 837
Cdd:cd16940     79 SGLGLSIVKRIVELHGGQIFLGNAQGGGLEAWVRL 113
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
725-838 4.17e-20

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain.


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 86.75  E-value: 4.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  725 DSNRLKQILINLLNNAIKFTDEGEVnLRISeyAPASPSTVYLRFEvsDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTG 804
Cdd:cd16946      1 DRDRLQQLFVNLLENSLRYTDTGGK-LRIR--AAQTPQEVRLDVE--DSAPGVSDDQLARLFERFYRVESSRNRASGGSG 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2787114911  805 LGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16946     76 LGLAICHNIALAHGGTISAEHSPLGGLRLVLTLP 109
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
596-843 6.86e-20

phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 96.15  E-value: 6.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  596 KLLQEARMAAEAANHAKSNFLSIMSHEIRTPLNAIIGTSYLLGLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEA 675
Cdd:PRK10618   434 KKLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLET 513
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  676 GELELEQRPFQLQeTLLD--LRAMFTTLAlQKGLTLRIAD--APEQTppvLNGDSNRLKQILINLLNNAIKFTDEGEVNL 751
Cdd:PRK10618   514 QDWKPEQELFSLQ-DLIDevLPEVLPAIK-RKGLQLLIHNhlKAEQL---RIGDRDALRKILLLLLNYAITTTAYGKITL 588
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  752 RIsEYAPASPSTvyLRFEVSDTGIGIPQTAQAKLFTPFMqAEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGT 831
Cdd:PRK10618   589 EV-DQDESSPDR--LTIRILDTGAGVSIKELDNLHFPFL-NQTQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGT 664
                          250
                   ....*....|..
gi 2787114911  832 QFTVDLPFATHH 843
Cdd:PRK10618   665 RYSIHLKMLAAD 676
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
716-837 7.30e-20

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA).


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 86.41  E-value: 7.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  716 EQTPPVLNGDSNRLKQILINLLNNAIKFTDEGEVnLRISEYApaSPSTVYLrfEVSDTGIGIPQTAQAKLFTPFMQAEAS 795
Cdd:cd16947      8 PDRPIYANANTEALQRILKNLISNAIKYGSDGKF-LGMTLRE--DEKHVYI--DIWDKGKGISETEKDHVFERLYTLEDS 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2787114911  796 TSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDL 837
Cdd:cd16947     83 RNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
729-838 9.42e-20

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 85.46  E-value: 9.42e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFTDEGEvNLRISEYAPASPSTvyLRFEVSDTGIGIPQTAQAKLFTPFMQAEasTSRKYGGTGLGLS 808
Cdd:cd16921      1 LGQVLTNLLGNAIKFRRPRR-PPRIEVGAEDVGEE--WTFYVRDNGIGIDPEYAEKVFGIFQRLH--SREEYEGTGVGLA 75
                           90       100       110
                   ....*....|....*....|....*....|
gi 2787114911  809 IVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16921     76 IVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
591-838 9.74e-20

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 93.70  E-value: 9.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  591 LKHQEKLLQEARMAAEAAnhaksnflsimsHEIRTPLNAIIGTSYLLGLDGLTDTQRSDVATINASSKNLL-ALINDVLD 669
Cdd:PRK10364   228 MKRKEKLVALGHLAAGVA------------HEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADRLnRVVSELLE 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  670 FSKieagELELEQRPFQLQETLLDLRAMFTTLALQKGLTLRIADAPeqTPPVLNGDSNRLKQILINLLNNAIKFTDEGEV 749
Cdd:PRK10364   296 LVK----PTHLALQAVDLNDLINHSLQLVSQDANSREIQLRFTAND--TLPEIQADPDRLTQVLLNLYLNAIQAIGQHGV 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  750 nlrISEYAPASPSTVYLRfeVSDTGIGIPQTAQAKLFTPFMQAEAStsrkygGTGLGLSIVKRLAELIGGAVFVQSTPGQ 829
Cdd:PRK10364   370 ---ISVTASESGAGVKIS--VTDSGKGIAADQLEAIFTPYFTTKAE------GTGLGLAVVHNIVEQHGGTIQVASQEGK 438

                   ....*....
gi 2787114911  830 GTQFTVDLP 838
Cdd:PRK10364   439 GATFTLWLP 447
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
867-990 3.49e-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: 3.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  867 LKQVHVMVVDDSEINLAITKRILE-CEGAT-VTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRlSADV 944
Cdd:COG4565      1 MKMIRVLIVEDDPMVAELLRRYLErLPGFEvVGVASSGEEALALLAEHR-PDLILLDIYLPDGDGLELLRELRAR-GPDV 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2787114911  945 PILALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALRGQVDLH 990
Cdd:COG4565     79 DVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYR 124
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
872-974 7.21e-19

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: 82.94  E-value: 7.21e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPDvDAILMDLQMPEMDGCETTLQIRKR-LSADVPILALT 950
Cdd:cd19920      1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPP-DLILLDVMMPGMDGFEVCRRLKADpATRHIPVIFLT 79
                           90       100
                   ....*....|....*....|....
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKPV 974
Cdd:cd19920     80 ALTDTEDKVKGFELGAVDYITKPF 103
PRK10604 PRK10604
sensor protein RstB; Provisional
620-851 9.04e-19

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 90.43  E-value: 9.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  620 SHEIRTPLnaiIGTSYLLG-LDGLTDTQRsdvATINASSKNLLALINDVLDFSKIEAGELELEQRPFQLQETLLDLRAMF 698
Cdd:PRK10604   220 AHELRTPL---VRLRYRLEmSDNLSAAES---QALNRDIGQLEALIEELLTYARLDRPQNELHLSEPDLPAWLSTHLADI 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  699 TTLALQKGLTLRIAdapeQTPPVLNGDSNRLKQILINLLNNAIKFTDEgevNLRISEYAPASPSTVylrfEVSDTGIGIP 778
Cdd:PRK10604   294 QAVTPEKTVRLDTP----HQGDYGALDMRLMERVLDNLLNNALRYAHS---RVRVSLLLDGNQACL----IVEDDGPGIP 362
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2787114911  779 QTAQAKLFTPFMQAEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPfaTHHGAIQHAPS 851
Cdd:PRK10604   363 PEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSWP--VWHNLPQFTSA 433
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
870-973 1.08e-18

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: 82.95  E-value: 1.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  870 VHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPDVDAILMDLQMPEMDGCETTLQIRKRLSAD-VPILA 948
Cdd:cd17544      1 IKVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDIKLVITDYNMPEMDGFELVREIRKKYSRDqLAIIG 80
                           90       100
                   ....*....|....*....|....*
gi 2787114911  949 LTAGATTTEKDRALASGMNGFLTKP 973
Cdd:cd17544     81 ISASGDNALSARFIKAGANDFLTKP 105
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
247-1114 1.60e-18

HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 91.65  E-value: 1.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  247 QHQLVFEAASQLDGIERLYVYQKLSTSPFWLSVGLSMQPFEAGWRQTGALVLALSGTVMGLLLWGARKLDHYSMGLEQQV 326
Cdd:COG2198      5 LLALLLLLLLLLLLLLLLLALLALLLLLLLAALALLLLLLLLLALLALLLLLVALALLLALLLLLLGVLLLLLDLLELLL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  327 EERTKRLSESEARHRELAQLAERSGQRLFKATRAASLGVWIWDLRDNTLIWDERMFELYGIPHLATSQAVDYGMWASRVH 406
Cdd:COG2198     85 LLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLLLLA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  407 PNDLEMAESRVKNLLENKGLYDPEFRIILPDGSIRYIQANAFLERDELGAATHVVGLNQDVTLLRQSQVDLKEAQRIAKV 486
Cdd:COG2198    165 LLLALLLLVLLVLLLLLLLLLLLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAELAAL 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  487 GSWRFDINKQHVEWSEELYRMFGADPKGPALNLEQQAAIFTPESWQRLEPAIASAVEDGTPYEIELQFTRSDGSMGWMLA 566
Cdd:COG2198    245 LLLLLLLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLLL 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  567 RGERVLDANGQPVYLRGTASDITTLKHQEKLLQEARMAAEAANHAKSNFLSIMSHEIRTPLNAIIGTSYLLGLDGLTDTQ 646
Cdd:COG2198    325 LLLLLLLLLLLLLLLLLLLLLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLL 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  647 RSDVATINASSKNLLALINDVLDFSKIEAGELELEQRPFQLQETLLDLRAMFTTLALQKGLTLRIADAPEQTPPVLNGDS 726
Cdd:COG2198    405 SLLLSLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLL 484
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  727 NRLKQILINLLNNAIKFTDEGEVNLRISEYAPASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLG 806
Cdd:COG2198    485 LLLLLLLLLLLLLLLLLLLLLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALLLGL 564
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  807 LSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFATHHGAIQHAPSALRIEPSALGNTTQTLKQVHVMVVDDSEINLAITK 886
Cdd:COG2198    565 GLLLGLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLL 644
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  887 RILECEGATVTLCNGGHQALKKLAQHPDVDAILMDLQMPEMDGCETTLQIRKRLSADVPILALTAGATTTEKDRALASGM 966
Cdd:COG2198    645 LLLLLLLLAVLLAAAAAAAALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLA 724
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  967 NGFLTKPVDPPALIQALRGQVDLHPQNPPEHNSamnttepandpwPKLPGIDLDHAKNItLGDANFFVELLNEFFEENAS 1046
Cdd:COG2198    725 ALLLLLLLLLLLLLLLLLLLLAAAAAAAASPAA------------PALPVLDLEALRRL-GGDPELLRELLELFLEELPE 791
                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2787114911 1047 CLSQLEAMLGKQAWDEAARVAHHIAGQAGNLGATALYQAAKAMELGCKQKAV-GLEPLLLELQRAYTEL 1114
Cdd:COG2198    792 LLAELRQALAAGDLEALARLAHKLKGSAGNLGAPRLAELAAELEQAARAGDLeEAEELLAELEAELERV 860
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
873-973 2.47e-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: 81.30  E-value: 2.47e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  873 MVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRLSaDVPILALTAG 952
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQ-PDLIILDVMLPGMDGFEVCRRLREKGS-DIPIIMLTAK 78
                           90       100
                   ....*....|....*....|.
gi 2787114911  953 ATTTEKDRALASGMNGFLTKP 973
Cdd:cd17574     79 DEEEDKVLGLELGADDYITKP 99
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
729-838 5.43e-18

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 80.52  E-value: 5.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFTDEGEVNLRISEYAPASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFmqaeasTSRKYGGTGLGLS 808
Cdd:cd16920      1 IQQVLINLVRNGIEAMSEGGCERRELTIRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPF------YTTKSEGLGMGLS 74
                           90       100       110
                   ....*....|....*....|....*....|
gi 2787114911  809 IVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16920     75 ICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
872-973 7.03e-18

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: 79.82  E-value: 7.03e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILE--CEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRlSADVPILAL 949
Cdd:COG4753      2 VLIVDDEPLIREGLKRILEweAGFEVVGEAENGEEALELLEEHK-PDLVITDINMPGMDGLELLEAIREL-DPDTKIIIL 79
                           90       100
                   ....*....|....*....|....
gi 2787114911  950 TAGATTTEKDRALASGMNGFLTKP 973
Cdd:COG4753     80 SGYSDFEYAQEAIKLGADDYLLKP 103
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
872-984 8.76e-18

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: 80.25  E-value: 8.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILE--CEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRLSaDVPILAL 949
Cdd:cd17535      1 VLIVDDHPLVREGLRRLLEsePDIEVVGEAADGEEALALLRELR-PDVVLMDLSMPGMDGIEALRRLRRRYP-DLKVIVL 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  950 TAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:cd17535     79 TAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIR 113
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
729-838 1.11e-17

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 79.39  E-value: 1.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFTDE-GEVNLRISEYAPAspstvyLRFEVSDTGIGIPQTAQAKLFTPFMqaeasTSRKYG-GTGLG 806
Cdd:cd16943      4 LNQVLLNLLVNAAQAMEGrGRITIRTWAHVDQ------VLIEVEDTGSGIDPEILGRIFDPFF-----TTKPVGeGTGLG 72
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2787114911  807 LSIVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16943     73 LSLSYRIIQKHGGTIRVASVPGGGTRFTIILP 104
PRK10490 PRK10490
sensor protein KdpD; Provisional
599-841 1.24e-17

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 88.55  E-value: 1.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  599 QEARMAAEAaNHAKSNFLSIMSHEIRTPLNAIIGTSYLLGLDGLTDTQR--SDVATINASSKNLLALINDVLDFSKIEAG 676
Cdd:PRK10490   652 EQARLASER-EQLRNALLAALSHDLRTPLTVLFGQAEILTLDLASEGSPhaRQASEIRQQVLNTTRLVNNLLDMARIQSG 730
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  677 ELELEQRPFQLQETLLDLRAMFTTLALQKGLTLRIadaPEQTPpVLNGDSNRLKQILINLLNNAIKFTDEGeVNLRISey 756
Cdd:PRK10490   731 GFNLRKEWLTLEEVVGSALQMLEPGLSGHPINLSL---PEPLT-LIHVDGPLFERVLINLLENAVKYAGAQ-AEIGID-- 803
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  757 apASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFMQAEASTSrkYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVD 836
Cdd:PRK10490   804 --AHVEGERLQLDVWDNGPGIPPGQEQLIFDKFARGNKESA--IPGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVT 879

                   ....*
gi 2787114911  837 LPFAT 841
Cdd:PRK10490   880 LPLET 884
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
871-984 3.26e-17

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


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 78.50  E-value: 3.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKlAQHPDVDAILMDLQMPEMDGCETTLQIRKRLS-ADVPILAL 949
Cdd:cd17562      2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSK-AQSKKFDLIITDQNMPNMDGIELIKELRKLPAyKFTPILML 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  950 TAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:cd17562     81 TTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVK 115
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
872-973 4.02e-17

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: 78.19  E-value: 4.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPDvDAILMDLQMPEMDGCETTLQIRKRLSaDVPILALTA 951
Cdd:cd17627      1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRP-DAVVLDVMMPRLDGLEVCRRLRAAGN-DLPILVLTA 78
                           90       100
                   ....*....|....*....|..
gi 2787114911  952 GATTTEKDRALASGMNGFLTKP 973
Cdd:cd17627     79 RDSVSDRVAGLDAGADDYLVKP 100
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
611-676 4.02e-17

His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 76.48  E-value: 4.02e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2787114911  611 AKSNFLSIMSHEIRTPLNAIIGTSYLLGLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAG 676
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
611-676 1.07e-16

His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 75.30  E-value: 1.07e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2787114911   611 AKSNFLSIMSHEIRTPLNAIIGTSYLLGLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAG 676
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
585-838 1.87e-16

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 83.14  E-value: 1.87e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  585 ASDITtlkhQEKLLQEARmaaeaanhakSNFLSIMSHEIRTPLNAIIGTSYLLGLDGLTDTQRSDV-ATINASSKNLLAL 663
Cdd:PRK11006   191 ARDVT----QMHQLEGAR----------RNFFANVSHELRTPLTVLQGYLEMMQDQPLEGALREKAlHTMREQTQRMEGL 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  664 INDVLDFSKIEAG-ELELEQRpfqlqetlLDLRAMFTTL-----ALQKG---LTLRIADAPEqtppVLnGDSNRLKQILI 734
Cdd:PRK11006   257 VKQLLTLSKIEAApTIDLNEK--------VDVPMMLRVLereaqTLSQGkhtITFEVDNSLK----VF-GNEDQLRSAIS 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  735 NLLNNAIKFTDEGeVNLRISEYAPASPStvylRFEVSDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLSIVK--- 811
Cdd:PRK11006   324 NLVYNAVNHTPEG-THITVRWQRVPQGA----EFSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKhal 398
                          250       260       270
                   ....*....|....*....|....*....|..
gi 2787114911  812 -----RLAeliggavfVQSTPGQGTQFTVDLP 838
Cdd:PRK11006   399 shhdsRLE--------IESEVGKGTRFSFVLP 422
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
729-838 7.86e-16

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain.


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 74.39  E-value: 7.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFTDEgevNLRISEYAPASpstvYLRFEVSDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLS 808
Cdd:cd16939      1 MARALDNLLRNALRYAHR---TVRIALLVSGG----RLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLA 73
                           90       100       110
                   ....*....|....*....|....*....|
gi 2787114911  809 IVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16939     74 IVHRVALWHGGHVECDDSELGGACFRLTWP 103
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
377-464 1.52e-15

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 72.76  E-value: 1.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  377 WDERMFELYGI-PHLATSQAVDygmWASRVHPNDLEMAESRVKNLLENKGLYDPEFRIILPDGSIRYIQANAFLERDELG 455
Cdd:pfam08447    4 WSPRFEEILGYtPEELLGKGES---WLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80

                   ....*....
gi 2787114911  456 AATHVVGLN 464
Cdd:pfam08447   81 KPVRVIGVA 89
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
872-984 2.43e-15

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: 73.08  E-value: 2.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTL-CNGGHQALKKlAQHPDVDAILMDLQMPEMDGCETTLQIRKrLSADVPILALT 950
Cdd:cd17542      3 VLIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEK-YKELKPDLVTMDITMPEMDGIEALKEIKK-IDPNAKVIMCS 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:cd17542     81 AMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVE 114
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
872-979 3.68e-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: 72.66  E-value: 3.68e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPD-VDAILMDLQMPEMDGCETTLQIrkRLSADVPILALT 950
Cdd:cd17584      1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDeFDLVITDVHMPDMDGFEFLELI--RLEMDLPVIMMS 78
                           90       100
                   ....*....|....*....|....*....
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKPVDPPAL 979
Cdd:cd17584     79 ADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
406-596 4.72e-15

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 80.49  E-value: 4.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  406 HPNDLEMAESRVKNLLENK-GLYDPEFRIILPDGSIRYIQANAFLERDELGAATHVVGLNQDVTLLRQSQVDLKE-AQRI 483
Cdd:PRK09776   333 WPEDLNKDLQQVEKLLSGEiNSYSMEKRYYRRDGEVVWALLAVSLVRDTDGTPLYFIAQIEDINELKRTEQVNERlMERI 412
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  484 ------AKVGSWRFDINKQHVEWSEELYRMFGADPkGPALNLEQQAAIFTPESWQRLEPAIASAVEDGTPYEIELQFTRS 557
Cdd:PRK09776   413 tlaneaGGIGIWEWDLKPNIISWDKRMFELYEIPP-HIKPTWQVWYACLHPEDRQRVEKEIRDALQGRSPFKLEFRIVVK 491
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2787114911  558 DGsMGWMLARGERVLDANGQPVYLRGTASDITTLK------HQEK 596
Cdd:PRK09776   492 DG-VRHIRALANRVLNKDGEVERLLGINMDMTEVRqlnealFQEK 535
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
729-838 4.86e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoR; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli or Vibrio cholera PhoR, the histidine kinase (HK) of PhoB-PhoR a two-component signal transduction system (TCS) involved in phosphate regulation. PhoR monitors extracellular inorganic phosphate (Pi) availability and PhoB, the response regulator, regulates transcription of genes of the phosphate regulon. PhoR is a bifunctional histidine autokinase/phospho-PhoB phosphatase; in phosphate deficiency, it autophosphorylates and Pi is transferred to PhoB, and when environmental Pi is abundant, it removes the phosphoryl group from phosphorylated PhoB. Other roles of PhoB-PhoR TCS have been described, including motility, biofilm formation, intestinal colonization, and virulence in V. cholera. E.coli PhoR and Bacillus subtilis PhoR (whose HATPase domain belongs to a different family) sense very different signals in each bacterium. In E. coli the PhoR signal comes from phosphate transport mediated by the PstSCAB2 phosphate transporter and the PhoU chaperone-like protein while in B. subtilis, the PhoR activation signal comes from wall teichoic acid (WTA) metabolism.


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 72.23  E-value: 4.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFT-DEGEVNLRISeyapASPSTVylRFEVSDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGL 807
Cdd:cd16952      1 LRSAFSNLVSNAVKYTpPSDTITVRWS----QEESGA--RLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGL 74
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2787114911  808 SIVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16952     75 AIVKHVMSRHDARLLIASELGKGSRFTCLFP 105
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
871-984 9.17e-15

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: 72.06  E-value: 9.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILECEGATVTL--CNGGHQALKKL------AQHPDVDAILMDLQMPEMDGCETTLQIRK--RL 940
Cdd:cd17557      1 TILLVEDNPGDAELIQEAFKEAGVPNELhvVRDGEEALDFLrgegeyADAPRPDLILLDLNMPRMDGFEVLREIKAdpDL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2787114911  941 sADVPILALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:cd17557     81 -RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIR 123
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
871-985 1.16e-14

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: 71.43  E-value: 1.16e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILECEGA-TVTLCNGGHQALKKLAQHPDvDAILMDLQMPEMDGCeTTLQirkRLSAD-----V 944
Cdd:cd17552      3 RILVIDDEEDIREVVQACLEKLAGwEVLTASSGQEGLEKAATEQP-DAILLDVMMPDMDGL-ATLK---KLQANpetqsI 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2787114911  945 PILALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALRG 985
Cdd:cd17552     78 PVILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAK 118
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
729-838 1.97e-14

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain.


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 70.17  E-value: 1.97e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFTDeGEVNLRiSEYAPAspstvYLRFEVSDTGIGIPQTAQAKLFTPFMQAEAStsRKYGGTGLGLS 808
Cdd:cd16950      1 LKRVLSNLVDNALRYGG-GWVEVS-SDGEGN-----RTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLA 71
                           90       100       110
                   ....*....|....*....|....*....|
gi 2787114911  809 IVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16950     72 IVQRISDAHGGSLTLANRAGGGLCARIELP 101
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
872-973 3.36e-14

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: 70.11  E-value: 3.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILE-CEGATV--TLCNGgHQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQIRKRlsADVPIL 947
Cdd:cd17541      3 VLIVDDSAVMRKLLSRILEsDPDIEVvgTARDG-EEALEKIKELkPDV--ITLDIEMPVMDGLEALRRIMAE--RPTPVV 77
                           90       100       110
                   ....*....|....*....|....*....|
gi 2787114911  948 ---ALT-AGATTTEkdRALASGMNGFLTKP 973
Cdd:cd17541     78 mvsSLTeEGAEITL--EALELGAVDFIAKP 105
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
871-987 6.99e-14

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 69.05  E-value: 6.99e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSE-INLAItKRILECEGATVTLCNGGHQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQIRKrLSADVPILA 948
Cdd:COG5803      4 KILIVDDQAgIRMLL-KEVLKKEGYEVFQAANGKEALEKVKELkPDL--VLLDMKMPGMDGIEILKEIKE-IDPDIPVIM 79
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2787114911  949 LTAGATTTEKDRALASGMNGFLTKPVDPPALIQALRGQV 987
Cdd:COG5803     80 MTAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLL 118
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
609-838 9.20e-14

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 75.94  E-value: 9.20e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  609 NHAKSNFLSIMSHEIRTPLnAIIGTSY-LLGLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIEAGELELEQRPFQL 687
Cdd:TIGR03785  482 THYLENMSSRLSHELRTPV-AVVRSSLeNLELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDL 560
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  688 QETLLDLRAMFTTLALQKGLTLRIadapEQTPPVLNGDSNRLKQILINLLNNAIKFTDEG---EVNLRISEYApaspstv 764
Cdd:TIGR03785  561 SEVLSGCMQGYQMTYPPQRFELNI----PETPLVMRGSPELIAQMLDKLVDNAREFSPEDgliEVGLSQNKSH------- 629
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2787114911  765 YLrFEVSDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTP-GQGTQFTVDLP 838
Cdd:TIGR03785  630 AL-LTVSNEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRISLP 703
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
729-838 9.53e-14

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 68.56  E-value: 9.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIK-FTDEGEVNLRIS------EYAPASPSTV---YLRFEVSDTGIGIPQTAQAKLFTPFMqaeasTSR 798
Cdd:cd16919      1 LELAILNLAVNARDaMPEGGRLTIETSnqrvdaDYALNYRDLIpgnYVCLEVSDTGSGMPAEVLRRAFEPFF-----TTK 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2787114911  799 KYG-GTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16919     76 EVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
615-844 1.09e-13

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 73.85  E-value: 1.09e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  615 FLSIMSHEIRTPLNAIigtsyLLGLDGLTDTQRSDVATINASSKNLLALINDVLDFSKIE----AGeleLEQRPFQLQET 690
Cdd:PRK10755   140 FTADVAHELRTPLAGI-----RLHLELLEKQHHIDVAPLIARLDQMMHTVEQLLQLARAGqsfsSG---HYQTVKLLEDV 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  691 LLDLRAMFTTLALQKGLTLRIADAPeqTPPVLNGDSNRLKQILINLLNNAIKFTDEGEvNLRISEYAPASPStvylRFEV 770
Cdd:PRK10755   212 ILPSQDELSEMLEQRQQTLLLPESA--ADITVQGDATLLRLLLRNLVENAHRYSPEGS-TITIKLSQEDGGA----VLAV 284
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2787114911  771 SDTGIGIPQTAQAKLFTPFMQAEastsRKYGGTGLGLSIVKRLAELIGGAVFVQS-TPGQGTQFTVDLPFATHHG 844
Cdd:PRK10755   285 EDEGPGIDESKCGELSKAFVRMD----SRYGGIGLGLSIVSRITQLHHGQFFLQNrQERSGTRAWVWLPKAQNVA 355
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
872-984 1.11e-13

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: 70.76  E-value: 1.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATV-TLCNGGHQALKKLAQHpDVDAILMDLQMPEMDGCETTLQIRKRLSAdvPILALT 950
Cdd:COG3707      6 VLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVREL-KPDLVIVDIDMPDRDGLEAARQISEERPA--PVILLT 82
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:COG3707     83 AYSDPELIERALEAGVSAYLVKPLDPEDLLPALE 116
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
616-843 1.34e-13

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 74.58  E-value: 1.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  616 LSIMSHEIRTPL------NAII----GTSyllgldglTDTQRsdvatINASSKNLLALINDVLDFSKIEA-GELELEQRP 684
Cdd:PRK09470   247 LSDISHELRTPLtrlqlaTALLrrrqGES--------KELER-----IETEAQRLDSMINDLLVLSRNQQkNHLERETFK 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  685 F-QLQETLLDlRAMFTtlALQKGLTLRIADAPEQTPpvLNGDSNRLKQILINLLNNAIKFT-DEGEVNLRISEyapaspS 762
Cdd:PRK09470   314 AnSLWSEVLE-DAKFE--AEQMGKSLTVSAPPGPWP--INGNPNALASALENIVRNALRYShTKIEVAFSVDK------D 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  763 TVYLRfeVSDTGIGIPQTAQAKLFTPFMQAEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPFATH 842
Cdd:PRK09470   383 GLTIT--VDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWVKAEDSPLGGLRLTIWLPLYKR 460

                   .
gi 2787114911  843 H 843
Cdd:PRK09470   461 S 461
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
870-983 1.38e-13

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: 68.13  E-value: 1.38e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  870 VHVMVVDDSEINLAITKRILECEGAT-VTLCNGGHQALKKLaQHPDVDAILMDLQMPEMDGCETTLQIR--KRLSaDVPI 946
Cdd:cd19923      1 MKVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKL-KAGGFDFVITDWNMPNMDGLELLKTIRadGALS-HLPV 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2787114911  947 LALTAGATTTEKDRALASGMNGFLTKPVDPPALIQAL 983
Cdd:cd19923     79 LMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKL 115
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
872-973 2.11e-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: 67.14  E-value: 2.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPDVDAILMDLQMPEMDGCETTLQIRKrLSADVPILALTA 951
Cdd:cd18160      2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDIDIVVTDIVMPEMDGIELAREARK-IDPDVKILFISG 80
                           90       100
                   ....*....|....*....|..
gi 2787114911  952 GATTTEKDRALASGMNGFLTKP 973
Cdd:cd18160     81 GAAAAPELLSDAVGDNATLKKP 102
pleD PRK09581
response regulator PleD; Reviewed
872-984 2.27e-13

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 73.78  E-value: 2.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTlqirKRLSAD-----VPI 946
Cdd:PRK09581     5 ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQ-PDIILLDVMMPGMDGFEVC----RRLKSDpatthIPV 79
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2787114911  947 LALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:PRK09581    80 VMVTALDDPEDRVRGLEAGADDFLTKPINDVALFARVK 117
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
872-984 2.67e-13

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: 67.43  E-value: 2.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRLSADVPILaLTA 951
Cdd:cd17569      3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEP-VDVVISDQRMPGMDGAELLKRVRERYPDTVRIL-LTG 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2787114911  952 GATTTekdrALASGMN-----GFLTKPVDPPALIQALR 984
Cdd:cd17569     81 YADLD----AAIEAINegeiyRFLTKPWDDEELKETIR 114
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
874-983 2.73e-13

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: 67.25  E-value: 2.73e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  874 VVDDSEINLAITKrILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRlSADVPILALTAGA 953
Cdd:cd17625      3 VEDEKDLSEAITK-HLKKEGYTVDVCFDGEEGLEYALSGI-YDLIILDIMLPGMDGLEVLKSLREE-GIETPVLLLTALD 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2787114911  954 TTTEKDRALASGMNGFLTKPVDPPAL---IQAL 983
Cdd:cd17625     80 AVEDRVKGLDLGADDYLPKPFSLAELlarIRAL 112
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
871-983 2.88e-13

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 67.18  E-value: 2.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSeiNLA---ITKRILECEGATVTLCNGGHQALKKLAQHpDVDAILMDLQMPEMDGCETTLQIRKR-------- 939
Cdd:cd17593      2 KVLICDDS--SMArkqLARALPADWDVEITFAENGEEALEILREG-RIDVLFLDLTMPVMDGYEVLEALPVEqletkviv 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2787114911  940 LSADVPILAltagattteKDRALASGMNGFLTKPVDPPALIQAL 983
Cdd:cd17593     79 VSGDVQPEA---------KERVLELGALAFLKKPFDPEKLAQLL 113
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
872-984 2.98e-13

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: 67.35  E-value: 2.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQIRKRLS-ADVPILAL 949
Cdd:cd17598      1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHrPTL--VISDIVMPEMDGYELCRKIKSDPDlKDIPVILL 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  950 TAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:cd17598     79 TTLSDPRDVIRGLECGADNFITKPYDEKYLLSRIK 113
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
729-838 3.31e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII); This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s).


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 67.04  E-value: 3.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFTDE--GEVNLRIS-EYAPASPSTVY---LRFEVSDTGIGIPQTAQAKLFTPFMqaeasTSRKyGG 802
Cdd:cd16918      1 LIQVFLNLVRNAAQALAGsgGEIILRTRtQRQVTLGHPRHrlaLRVSVIDNGPGIPPDLQDTIFYPMV-----SGRE-NG 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2787114911  803 TGLGLSIVKRLAELIGGAVFVQSTPGQgTQFTVDLP 838
Cdd:cd16918     75 TGLGLAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
609-672 3.94e-13

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 65.31  E-value: 3.94e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2787114911  609 NHAKSNFLSIMSHEIRTPLNAIIG-TSYLLGLDGLTDTQRSDVATINASSKNLLALINDVLDFSK 672
Cdd:cd00082      1 LQAKGEFLANVSHELRTPLTAIRGaLELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
725-838 3.95e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 66.54  E-value: 3.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  725 DSNRLKQILINLLNNAIKFTDE-GEVNLRISEyapaspSTVYLRFEVSDTGIGIPQTAQAKLFTPFMQAEasTSRKYG-G 802
Cdd:cd16948      2 DAKWLSFIIGQIVSNALKYSKQgGKIEIYSET------NEQGVVLSIKDFGIGIPEEDLPRVFDKGFTGE--NGRNFQeS 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2787114911  803 TGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16948     74 TGMGLYLVKKLCDKLGHKIDVESEVGEGTTFTITFP 109
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
872-987 4.81e-13

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: 66.72  E-value: 4.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQ-HPDVdaILMDLQMPEMDGCETTLQIRkrLSADVPILALT 950
Cdd:cd17626      3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREvRPDL--VLLDLMLPGIDGIEVCRQIR--AESGVPIVMLT 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKPVDPPALIQALRGQV 987
Cdd:cd17626     79 AKSDTVDVVLGLESGADDYVAKPFKPKELVARIRARL 115
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
872-984 5.45e-13

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 66.56  E-value: 5.45e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHpDVDAILMDLQMPEMDGCETTLQIRKRlsADVPILALTA 951
Cdd:cd17623      1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEG-SPDLVVLDVMLPKMNGLDVLKELRKT--SQVPVLMLTA 77
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2787114911  952 GATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:cd17623     78 RGDDIDRILGLELGADDYLPKPFNPRELVARIR 110
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
872-983 1.24e-12

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: 65.51  E-value: 1.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVT-LCNGGHQALKKLAQH-PDVdaILMDLQMP-EMDGCETTLQIRKRLsaDVPILA 948
Cdd:cd17534      3 ILIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENkPDL--ILMDINLKgDMDGIEAAREIREKF--DIPVIF 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  949 LTAGATTTEKDRALASGMNGFLTKPVDPPALIQAL 983
Cdd:cd17534     79 LTAYSDEETLERAKETNPYGYLVKPFNERELKAAI 113
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
872-973 1.76e-12

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: 65.09  E-value: 1.76e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKL--------AQHPDVDAILMDLQMPEMDGCETTLQIRK-RLSA 942
Cdd:cd19924      1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLenlakegnDLSKELDLIITDIEMPKMDGYELTFELRDdPRLA 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2787114911  943 DVPILALTAGATTTEKDRALASGMNGFLTKP 973
Cdd:cd19924     81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
PRK15115 PRK15115
response regulator GlrR; Provisional
868-983 1.80e-12

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 71.02  E-value: 1.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  868 KQVHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRlSADVPIL 947
Cdd:PRK15115     4 KPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREK-VDLVISDLRMDEMDGMQLFAEIQKV-QPGMPVI 81
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2787114911  948 ALTAGATTTEKDRALASGMNGFLTKPVDPPALIQAL 983
Cdd:PRK15115    82 ILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAI 117
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
873-980 2.21e-12

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: 64.60  E-value: 2.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  873 MVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRK-RLSADVPILALTA 951
Cdd:cd19937      1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEK-PDLIILDLMLPGIDGLEVCRILRSdPKTSSIPIIMLTA 79
                           90       100
                   ....*....|....*....|....*....
gi 2787114911  952 GATTTEKDRALASGMNGFLTKPVDPPALI 980
Cdd:cd19937     80 KGEEFDKVLGLELGADDYITKPFSPRELL 108
PAS COG2202
PAS domain [Signal transduction mechanisms];
469-698 2.23e-12

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 68.51  E-value: 2.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  469 LLRQSQVDLKEAQRIAKVGSWRFDINKQHVEWSEELYRMFGADPKgpALNLEQQAAIFTPESWQRLEPAIASAVEDGTPY 548
Cdd:COG2202      5 ALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAE--ELLGKTLRDLLPPEDDDEFLELLRAALAGGGVW 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  549 EIELQFTRSDGSMGWMLARGERVLDANGQPVYLRGTASDITTLKHQEKLLQEARMAAEAANHAKSNFLSIMSHEIRTPLN 628
Cdd:COG2202     83 RGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYV 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  629 AIIGTSYLLGLDGLTDTQRSDVATINASSKNLLALINDVLDfSKIEAGELELEQRPFQLQETLLDLRAMF 698
Cdd:COG2202    163 NPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLE-GGRESYELELRLKDGDGRWVWVEASAVP 231
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
869-983 2.24e-12

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 70.44  E-value: 2.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  869 QVHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKlAQHPDVDAILMDLQMPEMDGCETTLQIrKRLSADVPILA 948
Cdd:PRK10365     5 NIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQ-VREQVFDLVLCDVRMAEMDGIATLKEI-KALNPAIPVLI 82
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  949 LTAGATTTEKDRALASGMNGFLTKPVDPPALIQAL 983
Cdd:PRK10365    83 MTAYSSVETAVEALKTGALDYLIKPLDFDNLQATL 117
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
732-838 2.98e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 63.85  E-value: 2.98e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  732 ILINLLNNAIK-FTDEGEVNLRIseyapaspsTVYLRF-------EVSDTGIGIPQTAQAKLFtpfmqAEASTSRKYGGT 803
Cdd:cd16915      4 IVGNLIDNALDaLAATGAPNKQV---------EVFLRDegddlviEVRDTGPGIAPELRDKVF-----ERGVSTKGQGER 69
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  804 GLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16915     70 GIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
702-839 3.96e-12

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 70.33  E-value: 3.96e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  702 ALQKGLTLRIADApEQTPPVLNGD-SNRLKQILINLLNN---AIKFTDEGEVnlriseyapaspsTVYLRF-------EV 770
Cdd:PRK11086   407 ARELGITLIISED-SQLPDSGDEDqVHELITILGNLIENaleAVGGEEGGEI-------------SVSLHYrngwlhcEV 472
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2787114911  771 SDTGIGIPQTAQAKLFtpfmqaEASTSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPF 839
Cdd:PRK11086   473 SDDGPGIAPDEIDAIF------DKGYSTKGSNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIPW 535
PDC1_DGC_like cd12914
first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
61-186 5.03e-12

first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350339  Cd Length: 123  Bit Score: 63.94  E-value: 5.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911   61 LNDINTLLSILAQRYRDYPSKSQDTLyNLESQIRRELPFYQVALRIVVANAKGEQLLNTGKARDEQQNLPnliDRKFYQR 140
Cdd:cd12914      1 LDEADLLLRSLADDLEARGAASADPA-ALQALLRRLLARLPEVRSIFVVDADGRVVASSGPGPAPGLDVS---DRDYFQA 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2787114911  141 AIAGERGLMYEGPVPAKLDATWSIIMARPMVGSQGDFQGMVIAILP 186
Cdd:cd12914     77 ARAGGGGLFISEPVISRVTGKPVIPLSRPIRDADGRFAGVVVASID 122
PDC2_DGC_like cd12915
second PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
194-290 5.65e-12

second PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350340 [Multi-domain]  Cd Length: 96  Bit Score: 63.15  E-value: 5.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  194 FEMAELGENGVINLRTDDLSQVVRYPPAQGdalGVGNKKVPTKVTELLGNSPDQhqlVFEAASQLDGIERLYVYQKLSTS 273
Cdd:cd12915      6 YRSLDLGPGGAVALLRRDGTVLARYPDDEG---AVGRSLADPLFRALLAAAPSG---TFRAVSPLDGVERLYAYRRLPGY 79
                           90
                   ....*....|....*..
gi 2787114911  274 PFWLSVGLSMQPFEAGW 290
Cdd:cd12915     80 PLVVVVGLSEDDVLAPW 96
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
729-833 6.51e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 63.25  E-value: 6.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFTDE-GEVNLRiseyapASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFMQ-AEASTSRKygGTGLG 806
Cdd:cd16945      5 LRQAINNLLDNAIDFSPEgGLIALQ------LEADTEGIELLVFDEGSGIPDYALNRVFERFYSlPRPHSGQK--STGLG 76
                           90       100
                   ....*....|....*....|....*..
gi 2787114911  807 LSIVKRLAELIGGAVFVQSTPGQGTQF 833
Cdd:cd16945     77 LAFVQEVAQLHGGRITLRNRPDGVLAF 103
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
594-826 6.66e-12

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 69.72  E-value: 6.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  594 QEKLLQEARMAAEAANhaksnfLSIMSHEIRTPLNAIIGTSYLLGL---DGLTDTQRSDVATINASSKNLLALINDVLDF 670
Cdd:COG4192    421 QDELIQAAKMAVVGQT------MTSLAHELNQPLNAMSMYLFSAKKaleQENYAQLPTSLDKIEGLIERMDKIIKSLRQF 494
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  671 SKIEAGELeleqRPFQLQETLLDLRAMFTTLALQKGLTLRIADapeqtPPVLNGDSNRLKQILINLLNNAIK-FTDEGEV 749
Cdd:COG4192    495 SRKSDTPL----QPVDLRQVIEQAWELVESRAKPQQITLHIPD-----DLMVQGDQVLLEQVLVNLLVNALDaVATQPQI 565
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2787114911  750 NLRISEYAPaspstvYLRFEVSDTGIGIPQTAqaKLFTPFmqaeasTSRKYGGTGLGLSIVKRLAELIGGAVFVQST 826
Cdd:COG4192    566 SVDLLSNAE------NLRVAISDNGNGWPLVD--KLFTPF------TTTKEVGLGLGLSICRSIMQQFGGDLYLAST 628
envZ PRK09467
osmolarity sensor protein; Provisional
729-838 7.47e-12

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 68.78  E-value: 7.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFTdEGEVnlRISEYApaspSTVYLRFEVSDTGIGIPQTAQAKLFTPFMQAEasTSRKYGGTGLGLS 808
Cdd:PRK09467   332 IKRALANLVVNAARYG-NGWI--KVSSGT----EGKRAWFQVEDDGPGIPPEQLKHLFQPFTRGD--SARGSSGTGLGLA 402
                           90       100       110
                   ....*....|....*....|....*....|
gi 2787114911  809 IVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:PRK09467   403 IVKRIVDQHNGKVELGNSEEGGLSARAWLP 432
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
871-951 7.92e-12

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: 63.01  E-value: 7.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLaQHPDVDAILMDLQMPEMDGCETTLQIRKRlSADVPILALT 950
Cdd:cd17554      2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKL-ESEDPDLVILDIKMPGMDGLETLRKIREK-KPDLPVIICT 79

                   .
gi 2787114911  951 A 951
Cdd:cd17554     80 A 80
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
872-973 1.08e-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: 62.07  E-value: 1.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDsEINLAIT-KRILECEGATVTLCNGGHQALKkLAQHPDVDAILMDLQMPEMDGcettLQIRKRLSA---DVPIL 947
Cdd:cd19935      1 ILVVED-EKKLAEYlKKGLTEEGYAVDVAYDGEDGLH-LALTNEYDLIILDVMLPGLDG----LEVLRRLRAagkQTPVL 74
                           90       100
                   ....*....|....*....|....*.
gi 2787114911  948 ALTAGATTTEKDRALASGMNGFLTKP 973
Cdd:cd19935     75 MLTARDSVEDRVKGLDLGADDYLVKP 100
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
497-585 1.32e-11

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 61.59  E-value: 1.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  497 HVEWSEELYRMFGADPKGPALNLEQQAAIFTPESWQRLEPAIASAVEDGTPYEIELQFTRSDGSMGWMLARGERVLDANG 576
Cdd:pfam08447    1 IIYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80

                   ....*....
gi 2787114911  577 QPVYLRGTA 585
Cdd:pfam08447   81 KPVRVIGVA 89
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
729-838 1.66e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 61.96  E-value: 1.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFtdegevnlriseyapaSPSTVYLRFE---------VSDTGIGIPQTAQAKLFTPFMQAEASTSRK 799
Cdd:cd16949      1 LARALENVLRNALRY----------------SPSKILLDISqdgdqwtitITDDGPGVPEDQLEQIFLPFYRVDSARDRE 64
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2787114911  800 YGGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16949     65 SGGTGLGLAIAERAIEQHGGKIKASNRKPGGLRVRIWLP 103
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
872-973 1.70e-11

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: 61.62  E-value: 1.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPDvDAILMDLQMPEMDGCETTLQIRKrLSA--DVPILAL 949
Cdd:cd17602      1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKP-DLILIDIDMPDLDGYELCSLLRK-SSAlkDTPIIML 78
                           90       100
                   ....*....|....*....|....
gi 2787114911  950 TAGATTTEKDRALASGMNGFLTKP 973
Cdd:cd17602     79 TGKDGLVDRIRAKMAGASGYLTKP 102
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
872-973 4.05e-11

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: 60.64  E-value: 4.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQIRKrlSADVPILALT 950
Cdd:cd17620      1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRkPDL--IILDLGLPDMDGLEVIRRLRE--WSAVPVIVLS 76
                           90       100
                   ....*....|....*....|...
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKP 973
Cdd:cd17620     77 ARDEESDKIAALDAGADDYLTKP 99
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
42-275 4.27e-11

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 64.28  E-value: 4.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911   42 LKNNAANTAEITAARIESSLNDINTLLSILAQRYrDYPSKSQDTLYNLESQIRRELPFYQVALRIVVANAKGEQLLNTGk 121
Cdd:pfam02743    7 AEEQLLSLAKQLAENIESYLDSLEEILELLASNP-DLQDLLSAPAEEELAKLESLLRSNPGISSIYLVDADGRVLASSD- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  122 aRDEQQNLPNLIDRKFYQRAIAGERGLM--YEGPVPAKLDATWSIIMARPMVGSQGDFQGMVIAILPTERLGMGFEMAEL 199
Cdd:pfam02743   85 -ESPSYPGLDVSERPWYKEALKGGGGIIwvFSSPYPSSESGEPVLTIARPIYDDDGEVIGVLVADLDLDTLQELLSQIKL 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2787114911  200 GENGVINLrTDDLSQVVrYPPAQGDALGVGNKKVPTKVTELLGNSPdqhqlVFEAASQLDGIERLYVYQKLSTSPF 275
Cdd:pfam02743  164 GEGGYVFI-VDSDGRIL-AHPLGKNLRSLLAPFLGKSLADALPGSG-----ITEIAVDLDGEDYLVAYAPIPGTGW 232
PRK09483 PRK09483
response regulator; Provisional
870-984 4.30e-11

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 63.97  E-value: 4.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  870 VHVMVVDDSEINLAITKRILECE-GATVT-LCNGGHQALKKLAQHpDVDAILMDLQMPEMDGCETTLQIrKRLSADVPIL 947
Cdd:PRK09483     2 INVLLVDDHELVRAGIRRILEDIkGIKVVgEACCGEDAVKWCRTN-AVDVVLMDMNMPGIGGLEATRKI-LRYTPDVKII 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2787114911  948 ALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:PRK09483    80 MLTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIR 116
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
872-984 4.42e-11

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: 61.35  E-value: 4.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQIRKrLSADVPILALT 950
Cdd:cd17549      1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDfPGV--VISDIRMPGMDGLELLAQIRE-LDPDLPVILIT 77
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:cd17549     78 GHGDVPMAVEAMRAGAYDFLEKPFDPERLLDVVR 111
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
729-837 4.57e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 60.55  E-value: 4.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFTDEGEvNLRISEYAPASPSTVYLRfeVSDTGIGIPQTAQAKLFTPFMqaeasTSRKYG-GTGLGL 807
Cdd:cd16976      1 IQQVLMNLLQNALDAMGKVE-NPRIRIAARRLGGRLVLV--VRDNGPGIAEEHLSRVFDPFF-----TTKPVGkGTGLGL 72
                           90       100       110
                   ....*....|....*....|....*....|
gi 2787114911  808 SIVKRLAELIGGAVFVQSTPGQGTQFTVDL 837
Cdd:cd16976     73 SISYGIVEEHGGRLSVANEEGAGARFTFDL 102
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
870-983 6.06e-11

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: 60.89  E-value: 6.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  870 VHVMVVDDSEINLAITKRILECEGATVT-LCNGGHQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQIRKRLSAdvPIL 947
Cdd:cd19932      1 VRVLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKHkPDL--VIMDVKMPRLDGIEAAKIITSENIA--PIV 76
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2787114911  948 ALTAGATTTEKDRALASGMNGFLTKPVDPPALIQAL 983
Cdd:cd19932     77 LLTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAI 112
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
872-984 6.29e-11

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: 60.81  E-value: 6.29e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRIL--ECEGATVTL-CNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRLSaDVPILA 948
Cdd:cd17536      1 VLIVDDEPLIREGLKKLIdwEELGFEVVGeAENGEEALELIEEHK-PDIVITDIRMPGMDGLELIEKIRELYP-DIKIII 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2787114911  949 LTAGAtttEKD---RALASGMNGFLTKPVDPPALIQALR 984
Cdd:cd17536     79 LSGYD---DFEyaqKAIRLGVVDYLLKPVDEEELEEALE 114
glnL PRK11073
nitrogen regulation protein NR(II);
575-838 8.76e-11

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 64.72  E-value: 8.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  575 NGQPVYLRGTASDITT---LKHQEKLLQEARMAAEAANHAKS----NFLSIMSHEIRTPLNAIIGTSYLLGlDGLTD--- 644
Cdd:PRK11073    86 DGRSHILSLTAQRLPEgmiLLEMAPMDNQRRLSQEQLQHAQQvaarDLVRGLAHEIKNPLGGLRGAAQLLS-KALPDpal 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  645 TQRSDVatINASSKNLLALINDVLDfskieagelelEQRPFQLQETLLD--LRAMFTTLALQKGLTLRIADAPEQTPPVL 722
Cdd:PRK11073   165 TEYTKV--IIEQADRLRNLVDRLLG-----------PQRPGTHVTESIHkvAERVVQLVSLELPDNVRLIRDYDPSLPEL 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  723 NGDSNRLKQILINLLNNAIKFTDE--GEVNLRISEyapASPSTVY-------LRFEVSDTGIGIPQTAQAKLFTPFMqae 793
Cdd:PRK11073   232 AHDPDQIEQVLLNIVRNALQALGPegGTITLRTRT---AFQLTLHgeryrlaARIDIEDNGPGIPPHLQDTLFYPMV--- 305
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2787114911  794 astSRKYGGTGLGLSIVKRLAELIGGAVFVQSTPGQgTQFTVDLP 838
Cdd:PRK11073   306 ---SGREGGTGLGLSIARNLIDQHSGKIEFTSWPGH-TEFSVYLP 346
PRK10337 PRK10337
sensor protein QseC; Provisional
563-835 1.08e-10

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 65.44  E-value: 1.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  563 WMLARGERVLDANGQPvyLRGTASDITTLKHQEKLLQEARMAAEAANH--AKSN--------FLSIMSHEIRTPLNAI-I 631
Cdd:PRK10337   180 VLLGRELAPLKKLALA--LRMRDPDSETPLNATGVPSEVRPLVEALNQlfARTHammvrerrFTSDAAHELRSPLAALkV 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  632 GTSYL-LGLDgltDTQRSDVATINASSKNLLA--LINDVLDFSKIEAGEL--ELEQRPFQ--LQETLLDLRAmfttLALQ 704
Cdd:PRK10337   258 QTEVAqLSDD---DPQARKKALLQLHAGIDRAtrLVDQLLTLSRLDSLDNlqDVAEIPLEdlLQSAVMDIYH----TAQQ 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  705 KGLTLRIaDAPEQtPPVLNGDSNRLKQILINLLNNAIKFTDEG-EVNLRISEYapaspstvylRFEVSDTGIGIPQTAQA 783
Cdd:PRK10337   331 AGIDVRL-TLNAH-PVIRTGQPLLLSLLVRNLLDNAIRYSPQGsVVDVTLNAR----------NFTVRDNGPGVTPEALA 398
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2787114911  784 KL----FTPFMQaEAStsrkygGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTV 835
Cdd:PRK10337   399 RIgerfYRPPGQ-EAT------GSGLGLSIVRRIAKLHGMNVSFGNAPEGGFEAKV 447
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
872-973 1.21e-10

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


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 59.74  E-value: 1.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQ-HPDVdaILMDLQMPEMDGCETTLQIRKRlsADVPILALT 950
Cdd:cd17614      1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEeQPDL--ILLDLMLPEKDGLEVCREVRKT--SNVPIIMLT 76
                           90       100
                   ....*....|....*....|...
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKP 973
Cdd:cd17614     77 AKDSEVDKVLGLELGADDYVTKP 99
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
872-985 1.37e-10

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: 59.67  E-value: 1.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDsEINLA-ITKRILECEGATVTLCNGGHQALKKlAQHPDVDAILMDLQMPEMDGCETTLQIRkRLSADVPILALT 950
Cdd:cd17615      2 VLVVDD-EPNITeLLSMALRYEGWDVETAADGAEALAA-AREFRPDAVVLDIMLPDMDGLEVLRRLR-ADGPDVPVLFLT 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKPVDPPALIQALRG 985
Cdd:cd17615     79 AKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRA 113
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
719-837 2.06e-10

Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 59.78  E-value: 2.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  719 PPVLNGDSNRLKQILINLLNNAIKFTDE-GEVNLRI-----------SEYAPASPST----VYLRFEVSDTGIGIPqtAQ 782
Cdd:cd16938      2 PDVVVGDERRVFQVLLHMLGNLLKMRNGgGNITFRVfleggsedrsdRDWGPWRPSMsdesVEIRFEVEINDSGSP--SI 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2787114911  783 AKLFTPfmqaeASTSRKYG----GTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDL 837
Cdd:cd16938     80 ESASMR-----NSLNRRYNlselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
729-838 2.13e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain.


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 58.55  E-value: 2.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFTDEgevNLRIseYAPASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFMQAEasTSRKYGGTGLGLS 808
Cdd:cd16923      1 LQRVFSNLLSNAIKYSPE---NTRI--YITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGD--NSRNTEGAGLGLS 73
                           90       100       110
                   ....*....|....*....|....*....|
gi 2787114911  809 IVKRLAELIGGAVFVQSTpGQGTQFTVDLP 838
Cdd:cd16923     74 IAKAIIELHGGSASAEYD-DNHDLFKVRLP 102
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
1035-1117 4.17e-10

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 57.36  E-value: 4.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911 1035 ELLNEFFEENASCLSQLEAMLGKQAWDEAARVAHHIAGQAGNLGATALYQAAKAMELGCKQKAVGLEP-LLLELQRAYTE 1113
Cdd:pfam01627    1 ELLELFLEEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLLREGELPLDPeLLEALRDLLEA 80

                   ....
gi 2787114911 1114 LSGG 1117
Cdd:pfam01627   81 LRAA 84
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
725-835 4.64e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals.


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 57.86  E-value: 4.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  725 DSNRLKQILINLLNNAIKFTDEGEvNLRISEYAPASpstvYLRFEVSDTGIGIPQTAQAKLFTPFMQAEasTSRKYGG-T 803
Cdd:cd16975      1 DTLLLSRALINIISNACQYAPEGG-TVSISIYDEEE----YLYFEIWDNGHGFSEQDLKKALELFYRDD--TSRRSGGhY 73
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2787114911  804 GLGLSIVKRLAELIGGAVFVQSTPGQGTQFTV 835
Cdd:cd16975     74 GMGLYIAKNLVEKHGGSLIIENSQKGGAEVTV 105
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
872-984 4.68e-10

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: 58.27  E-value: 4.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVV-DDSEINLAItKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRlSADVPILALT 950
Cdd:cd17624      1 ILLVeDDALLGDGL-KTGLRKAGYAVDWVRTGAEAEAALASGP-YDLVILDLGLPDGDGLDLLRRWRRQ-GQSLPVLILT 77
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:cd17624     78 ARDGVDDRVAGLDAGADDYLVKPFALEELLARLR 111
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
871-983 9.34e-10

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: 57.07  E-value: 9.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRLsADVPILALT 950
Cdd:cd17563      2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEK-PDYAVLDLRLGGDSGLDLIPPLRALQ-PDARIVVLT 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2787114911  951 aG----ATTTEkdrALASGMNGFLTKPVDPPALIQAL 983
Cdd:cd17563     80 -GyasiATAVE---AIKLGADDYLAKPADADEILAAL 112
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
871-980 1.63e-09

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 56.63  E-value: 1.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHpDVDAILMDLQMPEMDGCETTLQIRKRlsADVPILALT 950
Cdd:cd17619      2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQ-DIDLVLLDINLPGKDGLSLTRELREQ--SEVGIILVT 78
                           90       100       110
                   ....*....|....*....|....*....|
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKPVDPPALI 980
Cdd:cd17619     79 GRDDEVDRIVGLEIGADDYVTKPFNPRELL 108
orf27 CHL00148
Ycf27; Reviewed
864-985 1.63e-09

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 59.73  E-value: 1.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  864 TQTLKQVHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQIRKrlSA 942
Cdd:CHL00148     1 TMENSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEqPDL--VILDVMMPKLDGYGVCQEIRK--ES 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2787114911  943 DVPILALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALRG 985
Cdd:CHL00148    77 DVPIIMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRS 119
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
871-925 1.69e-09

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: 54.50  E-value: 1.69e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2787114911   871 HVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMP 925
Cdd:smart00448    2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEK-PDLILLDIMMP 55
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
872-976 1.70e-09

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: 56.61  E-value: 1.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKL----------AQHPDVDAILMDLQMPEMDGCETTLQIrKRLS 941
Cdd:cd17581      1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeedssnFNEPKVNMIITDYCMPGMTGYDLLKKV-KESS 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2787114911  942 A--DVPILALTAGATTTEKDRALASGMNGFLTKPVDP 976
Cdd:cd17581     80 AlkEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKL 116
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
725-838 1.98e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Azorhizobium caulinodans NtrY; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Azorhizobium caulinodans ORS571 NtrY of the NtrY-NtrX TCS, which is involved in nitrogen fixation and metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also have PAS sensor domains.


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 56.01  E-value: 1.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  725 DSNRLKQILINLLNNAI-----KFTDEGEVNLRISEYAPASPSTVylrfeVSDTGIGIPQTAQAKLFTPFMqaeaSTSRK 799
Cdd:cd16944      1 DTTQISQVLTNILKNAAeaiegRPSDVGEVRIRVEADQDGRIVLI-----VCDNGKGFPREMRHRATEPYV----TTRPK 71
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2787114911  800 ygGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16944     72 --GTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
871-984 3.43e-09

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 58.67  E-value: 3.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILE-CEGAT-VTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKrLSADVPILA 948
Cdd:COG3279      3 KILIVDDEPLARERLERLLEkYPDLEvVGEASNGEEALELLEEHK-PDLVFLDIQMPGLDGFELARQLRE-LDPPPPIIF 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2787114911  949 LTAgatttEKDRAL-ASGMN--GFLTKPVDPPALIQALR 984
Cdd:COG3279     81 TTA-----YDEYALeAFEVNavDYLLKPIDEERLAKALE 114
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
872-984 3.53e-09

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 58.66  E-value: 3.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQhpDVDAILMDLQMPEMDGCETTLQIRKRlsADVPILALTA 951
Cdd:PRK10955     4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD--SIDLLLLDVMMPKKNGIDTLKELRQT--HQTPVIMLTA 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2787114911  952 GATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:PRK10955    80 RGSELDRVLGLELGADDYLPKPFNDRELVARIR 112
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
729-838 3.57e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Brucella abortus BvrS and Sinorhizobium meliloti ChvG; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Brucella abortus BvrS of the BvrR-BvrS two-component regulatory system (TCS), which controls cell invasion and intracellular survival, as well as Sinorhizobium meliloti and Agrobacterium tumefaciens ChvG of the ChvI-ChvG TCS necessary for endosymbiosis and pathogenicity in plants. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), an accessory HAMP sensor domain, a periplasmic stimulus-sensing domain, and some also have a sensor N-terminal transmembrane domain.


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 55.66  E-value: 3.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFT--DEGEVNLRiseyapASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFMqAEASTSRKYG-GTGL 805
Cdd:cd16953      1 LGQVLRNLIGNAISFSppDTGRITVS------AMPTGKMVTISVEDEGPGIPQEKLESIFDRFY-TERPANEAFGqHSGL 73
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2787114911  806 GLSIVKRLAELIGGAVFVQ--STPGQ--GTQFTVDLP 838
Cdd:cd16953     74 GLSISRQIIEAHGGISVAEnhNQPGQviGARFTVQLP 110
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
868-973 3.74e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 59.78  E-value: 3.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  868 KQVHVMVVDDSEINLAITKRILECE-GATV--TLCNGGhQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQI-RKRlsa 942
Cdd:PRK00742     2 MKIRVLVVDDSAFMRRLISEILNSDpDIEVvgTAPDGL-EAREKIKKLnPDV--ITLDVEMPVMDGLDALEKImRLR--- 75
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  943 DVPIL---ALT-AGATTTEkdRALASGMNGFLTKP 973
Cdd:PRK00742    76 PTPVVmvsSLTeRGAEITL--RALELGAVDFVTKP 108
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
364-467 3.83e-09

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 55.33  E-value: 3.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  364 GVWIWDLRDNTLIWDERMFELYGIphlatSQAVDYGM-WASRVHPNDLEMAESRVKNLLENKGLYDPEFRIILPDGSIRY 442
Cdd:cd00130      4 GVIVLDLDGRILYANPAAEQLLGY-----SPEELIGKsLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIW 78
                           90       100
                   ....*....|....*....|....*
gi 2787114911  443 IQANAFLERDELGAATHVVGLNQDV 467
Cdd:cd00130     79 VLVSLTPIRDEGGEVIGLLGVVRDI 103
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
872-975 4.75e-09

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 60.25  E-value: 4.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRlSADVPILALTA 951
Cdd:PRK11361     7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIH-PDVVLMDIRMPEMDGIKALKEMRSH-ETRTPVILMTA 84
                           90       100
                   ....*....|....*....|....
gi 2787114911  952 GATTTEKDRALASGMNGFLTKPVD 975
Cdd:PRK11361    85 YAEVETAVEALRCGAFDYVIKPFD 108
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
311-842 5.47e-09

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 59.92  E-value: 5.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  311 GARKLDHYSMGLEQQVEERTKRLSESEARHRELAQLAERSGQRLFKATRAASLGVWIWDLRDNTLIWDERMFELYGIPHL 390
Cdd:COG3920      1 LLLALLLLLLLALAALLLLAALLLLAAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  391 ATSQAVDYGMWASRVHPNDLEMAESRVKNLLENKGLYDPEFRIILPDGSIRYIQANAFLERDELGAATHVVGLNQDVTLL 470
Cdd:COG3920     81 LLALLVLLLLLLLAAAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAAL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  471 RQSQVDLKEAQRIAKVGSWRFDINKQHVEWSEELYRMFGADPKGPALNLEQQAAIFTPESWQRLEPAIASAVEDGTPYEI 550
Cdd:COG3920    161 LLLAEELAALRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  551 ELQFTRSDGSMGWMLARGERVLDANGQPVYLRGTASDITTLKHQEKLLQEARMAAEAA----NH-AKSNF---LSIMSHE 622
Cdd:COG3920    241 LERRRRARGLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKELLlrelHHrVKNNLqvvSSLLRLQ 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  623 IRTPLNAIIgtsyllgLDGLTDTQRsdvaTINAssknlLALINDVL----DFSKIEAGELeleqrpfqLQETLLDLRAMF 698
Cdd:COG3920    321 ARRADDPEA-------REALEESQN----RIQA-----LALVHELLyqseDWEGVDLRDY--------LRELLEPLRDSY 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  699 TTLALQkgLTLRIADA---PEQTPPVLngdsnrlkqILIN-LLNNAIKF----TDEGEVNLRISEYAPaspstvYLRFEV 770
Cdd:COG3920    377 GGRGIR--IELDGPDVelpADAAVPLG---------LILNeLVTNALKHaflsGEGGRIRVSWRREDG------RLRLTV 439
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2787114911  771 SDTGIGIPQTAQAKlftpfmqaeastsrkyGGTGLGLSIVKRLAELIGGAvfVQSTPGQGTQFTVDLPFATH 842
Cdd:COG3920    440 SDNGVGLPEDVDPP----------------ARKGLGLRLIRALVRQLGGT--LELDRPEGTRVRITFPLAEL 493
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
872-984 5.53e-09

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: 54.90  E-value: 5.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKL-AQHPDVdaILMDLQMPEMDGCETTLQIRKRlSADVPILALT 950
Cdd:cd17555      3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFrSEQPDL--VLCDLRMPEMDGLEVLKQITKE-SPDTPVIVVS 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKPV-DPPALIQALR 984
Cdd:cd17555     80 GAGVMSDAVEALRLGAWDYLTKPIeDLAVLEHAVR 114
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
871-1000 5.70e-09

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: 56.85  E-value: 5.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCEtTLQIRKRLSADVPILALT 950
Cdd:COG4567      6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAP-PDYAVLDLRLGDGSGLD-LIEALRERDPDARIVVLT 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2787114911  951 aG----ATTTEkdrALASGMNGFLTKPVDPPALIQALRGQVDLHPQNPPEHNSA 1000
Cdd:COG4567     84 -GyasiATAVE---AIKLGADDYLAKPADADDLLAALERAEGDAPAPPENPMSL 133
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
872-990 7.32e-09

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: 54.90  E-value: 7.32e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLA-QHPDVdaILMDLQMPEMDGCETTLQIRKRlSADVPILALT 950
Cdd:cd17572      1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSdQPPDV--VLLDLKLPDMSGMEILKWIQER-SLPTSVIVIT 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKPVDPPALIQALRGQVDLH 990
Cdd:cd17572     78 AHGSVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHR 117
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
872-987 8.23e-09

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: 54.72  E-value: 8.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAItKRILECEGATVTLCNGGHQALKkLAQHPDVDAILMDLQMPEMDGCETTLQIRKrLSADVPILALTA 951
Cdd:cd17616      2 LLIEDDSATAQSI-ELMLKSEGFNVYTTDLGEEGLD-LGKLYDYDIILLDLNLPDMSGYEVLRTLRL-AKVKTPILILSG 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2787114911  952 GATTTEKDRALASGMNGFLTKPVDPPALIQALRGQV 987
Cdd:cd17616     79 LADIEDKVKGLGFGADDYMTKPFHKDELVARIHAIV 114
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
871-976 1.15e-08

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: 54.31  E-value: 1.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDsEINLA-ITKRILECEGATVTLCNGGHQALKKLAQHPDvDAILMDLQMPEMDGCETTLQIRKrlSADVPILAL 949
Cdd:cd19938      1 RILIVED-EPKLAqLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPP-DLILLDLMLPGTDGLTLCREIRR--FSDVPIIMV 76
                           90       100
                   ....*....|....*....|....*....
gi 2787114911  950 TagATTTEKDR--ALASGMNGFLTKPVDP 976
Cdd:cd19938     77 T--ARVEEIDRllGLELGADDYICKPYSP 103
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
61-186 2.36e-08

first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350341 [Multi-domain]  Cd Length: 125  Bit Score: 53.72  E-value: 2.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911   61 LNDINTLLSILAQRYRDYPSKSQDTLYNLESQIRRELPFYQVALRIVVANAKGEQLLNTGKARDEQQNLpnLIDRKFYQR 140
Cdd:cd18773      1 LEEADLLLRSLASALEALAALGSADREELQALLRRLLERNPEISGIYVVDADGRVVASSDRDPGGGDDD--DDRDRFWYQ 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2787114911  141 AIAGERGLMYEGPVPAKLDATWSIIMARPMVGSQGDFQGMVIAILP 186
Cdd:cd18773     79 AAKATGKLVISEPYISRVTGKPVITLSRPIRDADGRFIGVVGADID 124
PLN03029 PLN03029
type-a response regulator protein; Provisional
863-974 4.21e-08

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 55.04  E-value: 4.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  863 TTQTLKQVHVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPD-------------------VDAILMDLQ 923
Cdd:PLN03029     2 GITTESQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHEDdrsnpdtpsvspnshqeveVNLIITDYC 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2787114911  924 MPEMDGCETTLQIRKRLS-ADVPILALTAGATTTEKDRALASGMNGFLTKPV 974
Cdd:PLN03029    82 MPGMTGYDLLKKIKESSSlRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPV 133
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
872-986 6.15e-08

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 52.00  E-value: 6.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAItKRILECEGATVTLCNGGHQALKKLAQHpDVDAILMDLQMPEMDGCETTLQIRKrlSADVPILALTA 951
Cdd:cd17622      4 LLVEDDPKLARLI-ADFLESHGFNVVVEHRGDRALEVIARE-KPDAVLLDIMLPGIDGLTLCRDLRP--KYQGPILLLTA 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  952 GATTTEKDRALASGMNGFLTKPVDPPALIQALRGQ 986
Cdd:cd17622     80 LDSDIDHILGLELGADDYVVKPVEPAVLLARLRAL 114
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
872-973 6.25e-08

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: 52.11  E-value: 6.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCEtTLQIRKRLSADVPILALTA 951
Cdd:cd17550      1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERR-PDLVLLDIWLPDMDGLE-LLKEIKEKYPDLPVIMISG 78
                           90       100
                   ....*....|....*....|..
gi 2787114911  952 GATTTEKDRALASGMNGFLTKP 973
Cdd:cd17550     79 HGTIETAVKATKLGAYDFIEKP 100
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
876-975 6.31e-08

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: 51.89  E-value: 6.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  876 DDSEINLaITKRILECEGATVTLCNGGHQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQIRKRLsADVPILALTAGAT 954
Cdd:cd19919      8 DDSSIRW-VLERALAGAGLTVTSFENAQEALAALASSqPDV--LISDIRMPGMDGLALLAQIKQRH-PDLPVIIMTAHSD 83
                           90       100
                   ....*....|....*....|....
gi 2787114911  955 TtekDRALASGMNG---FLTKPVD 975
Cdd:cd19919     84 L---DSAVSAYQGGafeYLPKPFD 104
PAS COG2202
PAS domain [Signal transduction mechanisms];
325-477 6.95e-08

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 55.03  E-value: 6.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  325 QVEERtkrLSESEARHRELAQlaersgqrlfkatrAASLGVWIWDLRDNTLIWDERMFELYGIphlaTSQAVDYGMWASR 404
Cdd:COG2202    127 RAEEA---LRESEERLRLLVE--------------NAPDGIFVLDLDGRILYVNPAAEELLGY----SPEELLGKSLLDL 185
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2787114911  405 VHPNDLEMAESRVKNLLENKG-LYDPEFRIILPDGSIRYIQANAFLERDElGAATHVVGLNQDVTLLRQSQVDL 477
Cdd:COG2202    186 LHPEDRERLLELLRRLLEGGReSYELELRLKDGDGRWVWVEASAVPLRDG-GEVIGVLGIVRDITERKRAEEAL 258
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
871-984 7.26e-08

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: 53.95  E-value: 7.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKL-AQHPDVdaILMDLQMPEMDGCEttLQIR-KRLSADVPILA 948
Cdd:COG4566      1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALdPDRPGC--LLLDVRMPGMSGLE--LQEElAARGSPLPVIF 76
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2787114911  949 LTAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:COG4566     77 LTGHGDVPMAVRAMKAGAVDFLEKPFDDQALLDAVR 112
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
872-974 8.29e-08

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: 51.19  E-value: 8.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPDVDAILMDLQMP-EMDGCETTLQIRKRLSaDVPILALT 950
Cdd:cd18161      1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDIDLLVTDVIMPgGMNGSQLAEEARRRRP-DLKVLLTS 79
                           90       100
                   ....*....|....*....|....
gi 2787114911  951 AGATTTEKDRALASGMNgFLTKPV 974
Cdd:cd18161     80 GYAENAIEGGDLAPGVD-VLSKPF 102
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
872-973 9.82e-08

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: 51.04  E-value: 9.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHpDVDAILMDLQMPEMDGCETTLQIRKRlsADVPILALTA 951
Cdd:cd17621      1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRA-GADIVLLDLMLPGLSGTEVCRQLRAR--SNVPVIMVTA 77
                           90       100
                   ....*....|....*....|..
gi 2787114911  952 GATTTEKDRALASGMNGFLTKP 973
Cdd:cd17621     78 KDSEIDKVVGLELGADDYVTKP 99
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
902-992 1.06e-07

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 53.88  E-value: 1.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  902 GHQALKkLAQHPDVDAILMDLQMPEMDGCETTLQIR-KRLSADVPILALtagaTTTEKD--RALASGMNGFLTKPVDPPA 978
Cdd:PRK10651    41 GEQGIE-LAESLDPDLILLDLNMPGMNGLETLDKLReKSLSGRIVVFSV----SNHEEDvvTALKRGADGYLLKDMEPED 115
                           90
                   ....*....|....*...
gi 2787114911  979 LIQALR----GQVDLHPQ 992
Cdd:PRK10651   116 LLKALQqaaaGEMVLSEA 133
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
870-957 1.09e-07

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: 51.82  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  870 VHVMVVDDSEINLAITKRILECEG--ATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIrkrLSA-DVPI 946
Cdd:COG2197      2 IRVLIVDDHPLVREGLRALLEAEPdiEVVGEAADGEEALELLEELR-PDVVLLDIRMPGMDGLEALRRL---LTPrEREV 77
                           90
                   ....*....|..
gi 2787114911  947 LALTA-GATTTE 957
Cdd:COG2197     78 LRLLAeGLSNKE 89
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
872-973 1.15e-07

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 50.84  E-value: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAItKRILECEGATVTLCNGGHQALKKLAQ-HPDVdaILMDLQMPEMDGCETTLQIRKR-LSADVPILAL 949
Cdd:cd19927      2 LLVDDDPGIRLAV-KDYLEDQGFTVIAASNGLEALDLLNQyIPDL--IISDIIMPGVDGYSLLGKLRKNaDFDTIPVIFL 78
                           90       100
                   ....*....|....*....|....
gi 2787114911  950 TAGATTTEKDRALASGMNGFLTKP 973
Cdd:cd19927     79 TAKGMTSDRIKGYNAGCDGYLSKP 102
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
729-839 1.49e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 55.41  E-value: 1.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKF-----TDEGEVNLRISEYAPaspstvYLRFEVSDTGIGIPQTAQAKLFTPFmqaeastSRKYGGT 803
Cdd:COG2972    337 PKLILQPLVENAIEHgiepkEGGGTIRISIRKEGD------RLVITVEDNGVGMPEEKLEKLLEEL-------SSKGEGR 403
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2787114911  804 GLGLSIV-KRLAELIGGA--VFVQSTPGQGTQFTVDLPF 839
Cdd:COG2972    404 GIGLRNVrERLKLYYGEEygLEIESEPGEGTTVTIRIPL 442
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
872-984 1.66e-07

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: 50.74  E-value: 1.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRkRLSADVPILALTA 951
Cdd:cd19934      1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEP-YDLVVLDLGLPGMDGLSVLRRWR-SEGRATPVLILTA 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2787114911  952 GATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:cd19934     79 RDSWQDKVEGLDAGADDYLTKPFHIEELLARLR 111
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
867-976 1.70e-07

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 53.43  E-value: 1.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  867 LKQVHVMVVDDSEinlAITKRI---LECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRkRLSAD 943
Cdd:PRK11083     1 MQQPTILLVEDEQ---AIADTLvyaLQSEGFTVEWFERGLPALDKLRQQP-PDLVILDVGLPDISGFELCRQLL-AFHPA 75
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  944 VPILALTagATTTEKDR--ALASGMNGFLTKPVDP 976
Cdd:PRK11083    76 LPVIFLT--ARSDEVDRlvGLEIGADDYVAKPFSP 108
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
872-973 3.35e-07

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: 49.37  E-value: 3.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRlsADVPILALTA 951
Cdd:cd19936      1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARP-PDLAILDIKMPRMDGMELLQRLRQK--STLPVIFLTS 77
                           90       100
                   ....*....|....*....|..
gi 2787114911  952 GATTTEKDRALASGMNGFLTKP 973
Cdd:cd19936     78 KDDEIDEVFGLRMGADDYITKP 99
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
870-984 3.44e-07

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


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 50.48  E-value: 3.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  870 VHVMVVDDSEINLAITKRILECE-GATVTLCNGGHQALKKLAQ-HPDVdaILMDLQMPEMDGCETTLQIR-KRLSADVPI 946
Cdd:cd17575      1 IMVLLVDDQAIIGEAVRRALADEeDIDFHYCSDPTEAIEVASQiKPTV--ILQDLVMPGVDGLTLVRFFRaNPATRDIPI 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2787114911  947 LALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:cd17575     79 IVLSTKEEPEVKSEAFALGANDYLVKLPDKIELVARIR 116
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
871-986 4.47e-07

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: 49.68  E-value: 4.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDsEINLA-ITKRILECEGATVTLCNGGHQALKKLAQHPDvDAILMDLQMPEMDGCETTLQIRKRlsADVPILAL 949
Cdd:cd19939      1 RILIVED-ELELArLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQP-SLVVLDIMLPGMDGLTVCREVREH--SHVPILML 76
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2787114911  950 TagATTTEKDRALA--SGMNGFLTKPVDPPALIQALRGQ 986
Cdd:cd19939     77 T--ARTEEMDRVLGleMGADDYLCKPFSPRELLARVRAL 113
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
871-980 5.41e-07

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: 49.56  E-value: 5.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEinlAITKRI---LECEGATVTLCNGGHQALKKLAQHPDvDAILMDLQMPEMDGCETTLQIRKR-LSADVPI 946
Cdd:cd17618      2 TILIVEDEP---AIREMIafnLERAGFDVVEAEDAESAVNLIVEPRP-DLILLDWMLPGGSGIQFIRRLKRDeMTRDIPI 77
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2787114911  947 LALTAGATTTEKDRALASGMNGFLTKPVDPPALI 980
Cdd:cd17618     78 IMLTARGEEEDKVRGLEAGADDYITKPFSPRELV 111
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
715-835 5.70e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG. PhoQ is the histidine kinase (HK) of the PhoP-PhoQ two-component regulatory system (TCS), which responds to the levels of Mg2+ and Ca2+, controls virulence, mediates the adaptation to Mg2+-limiting environments, and regulates numerous cellular activities. Providencia stuartii AarG is a putative sensor kinase which controls the expression of the 2'-N-acetyltransferase and an intrinsic multiple antibiotic resistance (Mar) response in Providencia stuartii. The AarG product is similar to PhoQ in that it is able to restore wild-type levels of resistance to a Salmonella typhimurium phoQ mutant. However, the expression of the 2'-N-acetyltransferase gene and of aarP (a gene encoding a transcriptional activator of 2'-N-acetyltransferase) are not significantly affected by the levels of Mg2+ or Ca2+. Most proteins in this group contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory HAMP sensor domain, and some have an intracellular membrane -interaction PhoQ sensor domain.


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 49.94  E-value: 5.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  715 PEQTPPvlnGDSNRLKQILINLLNNAIKFTDEgevNLRISeyapASPSTVYLRFEVSDTGIGIPQTAQAKLFTPFMQAEA 794
Cdd:cd16954     27 PELRFP---GERNDLMELLGNLLDNACKWCLE---FVEVT----ARQTDGGLHLIVDDDGPGVPESQRSKIFQRGQRLDE 96
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2787114911  795 STSrkygGTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTV 835
Cdd:cd16954     97 QRP----GQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEV 133
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
1032-1090 6.17e-07

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 48.40  E-value: 6.17e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 2787114911  1032 FFVELLNEFFEENASCLSQLEAMLGKQAWDEAARVAHHIAGQAGNLGATALYQAAKAME 1090
Cdd:smart00073    5 LFREELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLE 63
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
678-838 7.11e-07

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 53.30  E-value: 7.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  678 LELEQRPFQLQETLLD-LRAMFTT------------LALQKGLTLRIADAPE--QTPPVLngDSNRLKQILINLLNNAIK 742
Cdd:PRK15053   369 LEMVQGESQAQQQLIDsLREAFADrqvagllfgkvqRARELGLKMVIVPGSQlsQLPPGL--DSTEFAAIVGNLLDNAFE 446
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  743 F---TDEGevNLRISEYAPASPSTVYLrfEVSDTGIGIPQTAQAKLFTpfmQAEASTSRKYGGTGLGLSIVKRLAELIGG 819
Cdd:PRK15053   447 AslrSDEG--NKIVELFLSDEGDDVVI--EVADQGCGVPESLRDKIFE---QGVSTRADEPGEHGIGLYLIASYVTRCGG 519
                          170
                   ....*....|....*....
gi 2787114911  820 AVFVQSTPGQGTQFTVDLP 838
Cdd:PRK15053   520 VITLEDNDPCGTLFSIFIP 538
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
549-589 1.43e-06

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 46.02  E-value: 1.43e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 2787114911   549 EIELQFTRSDGSMGWMLARGERVLDANGQPVYLRGTASDIT 589
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDIT 41
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
871-975 2.48e-06

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: 47.44  E-value: 2.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILECEGATVTLCNGGHQaLKKLAQHPDVDAILMDLQMPEMDGCETTLQIRKRlsADVPILaLT 950
Cdd:cd17594      1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAE-EARLMLHRRVDLVLLDLRLGQESGLDLLRTIRAR--SDVPII-II 76
                           90       100
                   ....*....|....*....|....*..
gi 2787114911  951 AGATTTEKDR--ALASGMNGFLTKPVD 975
Cdd:cd17594     77 SGDRRDEIDRvvGLELGADDYLAKPFG 103
PRK10693 PRK10693
two-component system response regulator RssB;
902-974 2.48e-06

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 50.76  E-value: 2.48e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2787114911  902 GHQALKKLAQ-HPDVdaILMDLQMPEMDGCETTLQIRKRlSADVPILALTAGATTTEKDRALASGMNGFLTKPV 974
Cdd:PRK10693     6 GVDALELLGGfTPDL--IICDLAMPRMNGIEFVEHLRNR-GDQTPVLVISATENMADIAKALRLGVQDVLLKPV 76
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
889-984 2.50e-06

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: 47.65  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  889 LECEGATVTLCNGGHQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQIRKRLSaDVPILALTAGATTTEKDRALASGMN 967
Cdd:cd19930     20 LEDDLEVVAQASNGQEALRLVLKHsPDV--AILDIEMPGRTGLEVAAELREELP-DTKVLIVTTFGRPGYFRRALAAGVD 96
                           90
                   ....*....|....*..
gi 2787114911  968 GFLTKPVDPPALIQALR 984
Cdd:cd19930     97 GYVLKDRPIEELADAIR 113
PRK10766 PRK10766
two-component system response regulator TorR;
871-980 2.95e-06

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 49.65  E-value: 2.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILECEGATVTLCNGGHQaLKKLAQHPDVDAILMDLQMPEMDGCETTLQIRKRlsADVPILALT 950
Cdd:PRK10766     4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAG-MREIMQNQHVDLILLDINLPGEDGLMLTRELRSR--STVGIILVT 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKPVDPPALI 980
Cdd:PRK10766    81 GRTDSIDRIVGLEMGADDYVTKPLELRELL 110
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
736-842 3.00e-06

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 50.00  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  736 LLNNAIKftdegevnlriseYAPASPSTVYL-------RFEVSDTGIGIPQTAQAklftpfmqaeastsrkygGTGLGLS 808
Cdd:COG4585    170 ALTNALK-------------HAGATRVTVTLevddgelTLTVRDDGVGFDPEAAP------------------GGGLGLR 218
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2787114911  809 IVKRLAELIGGAVFVQSTPGQGTQFTVDLPFATH 842
Cdd:COG4585    219 GMRERAEALGGTLTIGSAPGGGTRVRATLPLAAA 252
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
769-838 3.12e-06

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases; This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain.


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 48.73  E-value: 3.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  769 EVSDTGIGIP-----QTAQAK-------------------LFTP-FMQAEASTSrkYGGTGLGLSIVKRLAELIGGAVFV 823
Cdd:cd16916     86 EVSDDGRGIDrekirEKAIERglitadeaatlsddevlnlIFAPgFSTAEQVTD--VSGRGVGMDVVKRSIESLGGTIEV 163
                           90
                   ....*....|....*
gi 2787114911  824 QSTPGQGTQFTVDLP 838
Cdd:cd16916    164 ESEPGQGTTFTIRLP 178
PRK10610 PRK10610
chemotaxis protein CheY;
868-983 3.83e-06

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 47.28  E-value: 3.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  868 KQVHVMVVDDSEINLAITKRILECEG-ATVTLCNGGHQALKKLaQHPDVDAILMDLQMPEMDGCETTLQIRKRLS-ADVP 945
Cdd:PRK10610     4 KELKFLVVDDFSTMRRIVRNLLKELGfNNVEEAEDGVDALNKL-QAGGFGFVISDWNMPNMDGLELLKTIRADGAmSALP 82
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2787114911  946 ILALTAGATTTEKDRALASGMNGFLTKPVDPPALIQAL 983
Cdd:PRK10610    83 VLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKL 120
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
872-974 5.96e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 49.88  E-value: 5.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGA-TVTLCNG-GHQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQIRKRlsADVPILA 948
Cdd:PRK12555     3 IGIVNDSPLAVEALRRALARDPDhEVVWVATdGAQAVERCAAQpPDV--ILMDLEMPRMDGVEATRRIMAE--RPCPILI 78
                           90       100       110
                   ....*....|....*....|....*....|
gi 2787114911  949 LTA----GATTTEkdRALASGMNGFLTKPV 974
Cdd:PRK12555    79 VTSlterNASRVF--EAMGAGALDAVDTPT 106
PRK15479 PRK15479
transcriptional regulator TctD;
905-984 6.05e-06

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 48.56  E-value: 6.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  905 ALKKLAQHPDVDAILMDLQMPEMDGCETTLQIRKRlSADVPILALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:PRK15479    35 AADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKR-GQTLPVLLLTARSAVADRVKGLNVGADDYLPKPFELEELDARLR 113
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
430-468 6.19e-06

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 44.10  E-value: 6.19e-06
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 2787114911   430 EFRIILPDGSIRYIQANAFLERDELGAATHVVGLNQDVT 468
Cdd:smart00086    3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDIT 41
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
871-984 6.73e-06

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: 46.43  E-value: 6.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILECEGATVTLCNGGHQALKklAQHPDVDA-ILMDLQMPEMDGcettLQIRKRLSA---DVPI 946
Cdd:cd17537      2 TVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLA--AAPPDQPGcLVLDVRMPGMSG----LELQDELLArgsNIPI 75
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2787114911  947 LALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:cd17537     76 IFITGHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIE 113
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
871-1031 6.94e-06

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 48.31  E-value: 6.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEINLAITKRILECEGA--TVTLCNGGHQALKkLAQHPDVDAILMDLQMPEMDGCEtTLQIRKRLSADVPILA 948
Cdd:PRK10403     8 QVLIVDDHPLMRRGVRQLLELDPGfeVVAEAGDGASAID-LANRLDPDVILLDLNMKGMSGLD-TLNALRRDGVTAQIII 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  949 LTAGATTTEKDRALASGMNGFLTKPVDPPALIQALRGQVDLHPQNPPEHNSAMNTTEP---ANDPWPKLPGIDLDHAKNI 1025
Cdd:PRK10403    86 LTVSDASSDVFALIDAGADGYLLKDSDPEVLLEAIRAGAKGSKVFSERVNQYLREREMfgaEEDPFSVLTERELDVLHEL 165

                   ....*.
gi 2787114911 1026 TLGDAN 1031
Cdd:PRK10403   166 AQGLSN 171
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
872-989 9.50e-06

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: 46.21  E-value: 9.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILEcEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRLSAdvPILALTA 951
Cdd:cd17596      3 ILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEW-VQVILCDQRMPGTTGVEFLKEVRERWPE--VVRIIIS 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2787114911  952 GATTTEkdrALASGMNG-----FLTKPVDPPALIQALRGQVDL 989
Cdd:cd17596     79 GYTDSE---DIIAGINEagiyqYLTKPWHPDQLLLTVRNAARL 118
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
872-984 1.13e-05

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: 45.80  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEG--ATVTLCNGGHQALKkLAQHPDVDAILMDLQMPEMDGCETTLQIRKRlSADVPILAL 949
Cdd:cd19931      1 VLLIDDHPLLRKGIKQLIELDPdfTVVGEASSGEEGIE-LAERLDPDLILLDLNMKGMSGLDTLKALREE-GVSARIVIL 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  950 TAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:cd19931     79 TVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALK 113
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
870-983 1.38e-05

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 45.31  E-value: 1.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  870 VHVMVVDD----SEINLAITKRIlecEGATVT-LCNGGHQALKKLaQHPDVDAILMDLQMPEMDGCETTLQIRKRlSADV 944
Cdd:cd19925      1 INVLIVEDdpmvAEIHRAYVEQV---PGFTVIgTAGTGEEALKLL-KERQPDLILLDIYLPDGNGLDLLRELRAA-GHDV 75
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2787114911  945 PILALTAGATTTEKDRALASGMNGFLTKPVDPPALIQAL 983
Cdd:cd19925     76 DVIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRL 114
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
872-987 2.00e-05

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


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 45.00  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEgATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRkrlSAD----VPIL 947
Cdd:cd17539      1 VLLVDDRPSSAERIAAMLSSE-HEVVVEADPDEALFRAAEGP-FDLVIVSLALEDFDGLRLCSQLR---SLErtrqLPIL 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2787114911  948 ALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALRGQV 987
Cdd:cd17539     76 AVADPGDRGRLIRALEIGVNDYLVRPIDPNELLARVRTQI 115
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
737-838 3.31e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 43.31  E-value: 3.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  737 LNNAIKFTDEGEVNLRISEyapaSPSTVYLRfeVSDTGIGIPQTAQAklftpfmqaeastsrkyGGTGLGLSIVKRLAEL 816
Cdd:cd16917      9 LTNALKHAGASRVRVTLSY----TADELTLT--VVDDGVGFDGPAPP-----------------GGGGFGLLGMRERAEL 65
                           90       100
                   ....*....|....*....|..
gi 2787114911  817 IGGAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16917     66 LGGTLTIGSRPGGGTRVTARLP 87
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
736-838 4.42e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis LytS and Staphylococcus aureus LytS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and a GAF sensor domain; most contain a DUF3816 domain.


Pssm-ID: 340433 [Multi-domain]  Cd Length: 106  Bit Score: 43.57  E-value: 4.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  736 LLNNAIK--FTDEGEVN-LRISeyapASPSTVYLRFEVSDTGIGIPQTAQAKL-FTPFmqaeasTSRKygGTGLGL-SIV 810
Cdd:cd16957      9 LVENAIRhaFPKRKENNeVRVV----VKKDQHKVHVSVSDNGQGIPEERLDLLgKTTV------TSEK--GTGTALeNLN 76
                           90       100       110
                   ....*....|....*....|....*....|
gi 2787114911  811 KRLAELIG--GAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16957     77 RRLIGLFGseACLHIESEVHGGTEVWFVIP 106
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
872-985 8.89e-05

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 45.09  E-value: 8.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQhPDVDAILMDLQMPEMDGCETTLQI-RKRLSADVPILALT 950
Cdd:PRK10161     5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNE-PWPDLILLDWMLPGGSGIQFIKHLkRESMTRDIPVVMLT 83
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKPVDPPALIQALRG 985
Cdd:PRK10161    84 ARGEEEDRVRGLETGADDYITKPFSPKELVARIKA 118
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
729-831 9.12e-05

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 44.25  E-value: 9.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFTdegeVNLRISEYAPASPSTVYLR-------FEVSDTGIGIPQTAQAKLFTpFMQAEASTSRKY- 800
Cdd:cd16929     44 LYYILFELLKNAMRAT----VESHGDDSDDLPPIKVTVAkgdedltIKISDRGGGIPREDLARLFS-YMYSTAPQPSLDd 118
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2787114911  801 -------------GGTGLGLSIVKRLAELIGGAVFVQSTPGQGT 831
Cdd:cd16929    119 fsdlisgtqpsplAGFGYGLPMSRLYAEYFGGDLDLQSMEGYGT 162
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
872-986 9.66e-05

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: 43.04  E-value: 9.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQIRKRLSadVPILALT 950
Cdd:cd18159      1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFkPDL--VLLDINLPYFDGFYWCREIRQISN--VPIIFIS 76
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2787114911  951 AGATTTEKDRALASGMNGFLTKPVDPPALIQALRGQ 986
Cdd:cd18159     77 SRDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAI 112
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
802-839 1.22e-04

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 45.94  E-value: 1.22e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2787114911  802 GTGLGLSIVKRLAELIGGAVFVQSTPGQGTQFTVDLPF 839
Cdd:COG0643    381 GRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPL 418
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
723-821 2.11e-04

Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana Phytochrome A, B, C, D and E; This family includes the histidine kinase-like ATPase (HATPase) domains of plant red/far-red photoreceptors, the phytochromes, and includes the Arabidopsis thaliana phytochrome family phyA-phyE. Following red light absorption, biologically inactive forms of phytochromes convert to active forms, which rapidly convert back to inactive forms upon far-red light irradiation. Phytochromes can be considered as having an N-terminal photosensory region to which a bilin chromophore is bound, and a C-terminal output region, which includes the HATPase domain represented here, and is involved in dimerization and presumably contributes to relaying the light signal to downstream signaling events.


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 41.87  E-value: 2.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  723 NGDSNRLKQILINLLNNAIKFT--DEGEVNLRISEYAPASPSTV---YLRFEVSDTGIGIPQTAQAKLFtpfmqaeaSTS 797
Cdd:cd16932      1 YGDQIRLQQVLADFLLNAVRFTpsPGGWVEIKVSPTKKQIGDGVhviHLEFRITHPGQGLPEELVQEMF--------EEN 72
                           90       100
                   ....*....|....*....|....
gi 2787114911  798 RKYGGTGLGLSIVKRLAELIGGAV 821
Cdd:cd16932     73 QWTTQEGLGLSISRKLVKLMNGDV 96
PRK11517 PRK11517
DNA-binding response regulator HprR;
872-990 2.40e-04

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 43.73  E-value: 2.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKkLAQHPDVDAILMDLQMPEMDGCETTLQIRKrlSADVPILALTA 951
Cdd:PRK11517     3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLY-LALKDDYALIILDIMLPGMDGWQILQTLRT--AKQTPVICLTA 79
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2787114911  952 GATTTEKDRALASGMNGFLTKPVDPPALIQALRGQVDLH 990
Cdd:PRK11517    80 RDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQH 118
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
723-835 2.96e-04

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 41.59  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  723 NGDSNRLKQILINLLNNAIKFTDEGEVNLRISeyapASPSTVYLRFEVSDTGIGIPQTAQAklftpfMQAEASTSrkyGG 802
Cdd:cd16934     20 EVRQAEIATAVTELARNLLKHAGGGQVLLEVV----AEGGRVALEILAVDQGPGIADVDEA------LRDGFSTG---GG 86
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2787114911  803 TGLGLSIVKRLAEliggaVF-VQSTPGQGTQFTV 835
Cdd:cd16934     87 LGLGLGGVRRLAD-----EFdLHSAPGRGTVVVA 115
PRK13560 PRK13560
hypothetical protein; Provisional
400-480 3.15e-04

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 45.05  E-value: 3.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  400 MWASRVHPNDLEMAESRVKNLLEnKGL--YDPEFRIILPDGSIRYIQANAFLERDELGAATHVVGLNQDVTLLRQSQVDL 477
Cdd:PRK13560   520 MFAAIIHPADLEQVAAEVAEFAA-QGVdrFEQEYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVIDISERKHAEEKI 598

                   ...
gi 2787114911  478 KEA 480
Cdd:PRK13560   599 KAA 601
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
872-973 3.44e-04

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: 40.98  E-value: 3.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRLsADVPILALTA 951
Cdd:cd19926      1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEP-YDLCLTDMRLPDGSGLELVQHIQQRL-PQTPVAVITA 78
                           90       100
                   ....*....|....*....|..
gi 2787114911  952 GATTTEKDRALASGMNGFLTKP 973
Cdd:cd19926     79 YGSLDTAIEALKAGAFDFLTKP 100
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
903-975 3.44e-04

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 43.33  E-value: 3.44e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2787114911  903 HQALKKLAQHPdVDAILMDLQMPEMDGCeTTLQIRKRLSADVPILALTAGATTTEKDRALASGMNGFLTKPVD 975
Cdd:PRK09935    39 RITIDYLRTRP-VDLIIMDIDLPGTDGF-TFLKRIKQIQSTVKVLFLSSKSECFYAGRAIQAGANGFVSKCND 109
HEV_ORF1 pfam02444
Hepatitis E virus ORF-2 (Putative capsid protein); The Hepatitis E virus (HEV) genome is a ...
945-1019 4.39e-04

Hepatitis E virus ORF-2 (Putative capsid protein); The Hepatitis E virus (HEV) genome is a single-stranded, positive-sense RNA molecule of approximately 7.5 kb. Three open reading frames (ORF) were identified within the HEV genome: ORF1 encodes non-structural proteins, ORF2 encodes the putative structural protein(s), and ORF3 encodes a protein of unknown function. ORF2 contains a consensus signal peptide sequence at its amino terminus and a capsid-like region with a high content of basic amino acids similar to that seen with other virus capsid proteins.


Pssm-ID: 280583  Cd Length: 114  Bit Score: 41.27  E-value: 4.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  945 PILALTAGATTTEKDRALASGMNGFLTKPVDPPALIQA--------LRGQVDLHPQNPPEHNSAMNTTEPANDPWPKLpg 1016
Cdd:pfam02444   27 PVSRLAAAVGGAAAVPAVVSGVTGLILSPSQSPIFIQPtpsppmspLRPGLDLVFANPPDHSAPLGVTRPSAPPLPHV-- 104

                   ...
gi 2787114911 1017 IDL 1019
Cdd:pfam02444  105 VDL 107
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
902-976 4.54e-04

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 43.14  E-value: 4.54e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2787114911  902 GHQALKKLAQHPDvDAILMDLQMPEMDGCETTLQIRkRLSaDVPILALTagATTTEKDR--ALASGMNGFLTKPVDP 976
Cdd:PRK10710    43 GDEVLPYVRQTPP-DLILLDLMLPGTDGLTLCREIR-RFS-DIPIVMVT--AKIEEIDRllGLEIGADDYICKPYSP 114
PRK15369 PRK15369
two component system response regulator;
916-972 4.61e-04

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 42.76  E-value: 4.61e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2787114911  916 DAILMDLQMPEMDGCETTLQIRKRLSaDVPILALTAGATTTEKDRALASGMNGFLTK 972
Cdd:PRK15369    51 DIVILDLGLPGMNGLDVIPQLHQRWP-AMNILVLTARQEEHMASRTLAAGALGYVLK 106
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
873-975 5.32e-04

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 44.09  E-value: 5.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  873 MVVDDSEINLaITKRILECEGATVTLCNGGHQALKKLAQH-PDVdaILMDLQMPEMDGCETTLQIRKRlSADVPILALTA 951
Cdd:PRK10923     8 VVDDDSSIRW-VLERALAGAGLTCTTFENGNEVLEALASKtPDV--LLSDIRMPGMDGLALLKQIKQR-HPMLPVIIMTA 83
                           90       100
                   ....*....|....*....|....
gi 2787114911  952 GATTTEKDRALASGMNGFLTKPVD 975
Cdd:PRK10923    84 HSDLDAAVSAYQQGAFDYLPKPFD 107
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
694-839 6.50e-04

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 40.67  E-value: 6.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  694 LRAMFTTLALQKGLTLRIADapeqtppvlngdsnRLKQILINLLNNAIK----FTDEGEVNLRISEYAPAspstvyLRFE 769
Cdd:COG2172     14 ARRAVRALLRELGLDEDDAD--------------DLVLAVSEAVTNAVRhaygGDPDGPVEVELELDPDG------LEIE 73
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  770 VSDTGIGIPQTAQAKLFTPFmqaeastsrkyGGTGLGLSIVKRLAEliggAVFVQSTPGqGTQFTVDLPF 839
Cdd:COG2172     74 VRDEGPGFDPEDLPDPYSTL-----------AEGGRGLFLIRRLMD----EVEYESDPG-GTTVRLVKRL 127
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
873-983 6.61e-04

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 42.19  E-value: 6.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  873 MVVDDSEINLAITKRILECEGATVT--LCNGGH--QALKKLAqhPDVdaILMDLQMPEMDGCETTLQIRKRLSADVpILA 948
Cdd:PRK09958     4 IIIDDHPLAIAAIRNLLIKNDIEILaeLTEGGSavQRVETLK--PDI--VIIDVDIPGVNGIQVLETLRKRQYSGI-III 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2787114911  949 LTAGATTTEKDRALASGMNGFLTKPVDPPALIQAL 983
Cdd:PRK09958    79 VSAKNDHFYGKHCADAGANGFVSKKEGMNNIIAAI 113
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
364-467 1.26e-03

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 39.71  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  364 GVWIWDLRDNTLIWDERMFELYGIPhlaTSQAVDYGMWASRVHPNDLEMAESRVKNLLENKGLYDPEFRIILPDGSIRYI 443
Cdd:pfam00989   13 GIFVVDEDGRILYVNAAAEELLGLS---REEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRVPDGRPRHV 89
                           90       100
                   ....*....|....*....|....
gi 2787114911  444 QANAFLERDELGAATHVVGLNQDV 467
Cdd:pfam00989   90 EVRASPVRDAGGEILGFLGVLRDI 113
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
869-996 1.29e-03

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 41.71  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  869 QVHVMVVDDSEINLAITKRILECEGATV----TLCNGghqALKKLAQHPDVdaILMDLQMPEMDGCETTLQIRKrLSAdV 944
Cdd:PRK10529     1 MTNVLIVEDEQAIRRFLRTALEGDGMRVfeaeTLQRG---LLEAATRKPDL--IILDLGLPDGDGIEFIRDLRQ-WSA-I 73
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2787114911  945 PILALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALRGQVDLHPQNPPE 996
Cdd:PRK10529    74 PVIVLSARSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRHSATPAP 125
PRK10336 PRK10336
two-component system response regulator QseB;
872-993 1.33e-03

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 41.42  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAItKRILECEGATVTLCNGGHQALKKLAQHPdVDAILMDLQMPEMDGCETTLQIRKRLSADvPILALTA 951
Cdd:PRK10336     4 LLIEDDMLIGDGI-KTGLSKMGFSVDWFTQGRQGKEALYSAP-YDAVILDLTLPGMDGRDILREWREKGQRE-PVLILTA 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2787114911  952 GATTTEKDRALASGMNGFLTKP---VDPPALIQAL-------------RGQVDLHPQN 993
Cdd:PRK10336    81 RDALAERVEGLRLGADDYLCKPfalIEVAARLEALmrrtngqasnelrHGNVMLDPGK 138
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
873-938 1.52e-03

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: 39.18  E-value: 1.52e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2787114911  873 MVVDDSEINLAITKRILECE--GATVTLCNGGHQALKKLaQHPDVDAILMDLQMPEMDGCETTLQIRK 938
Cdd:cd17565      2 YIVDDDKNIIKILSDIIEDDdlGEVVGEADNGAQAYDEI-LFLQPDIVLIDLLMPGMDGIQLVRKLKD 68
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
872-987 1.57e-03

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: 39.46  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGATVTLCNGGHQALKKLAQHPDvDAILMDLQMPEMDGCEtTLQIRKRLSADVPILALTA 951
Cdd:cd17553      3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERP-DLVLLDMKIPGMDGIE-ILKRMKVIDENIRVIIMTA 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2787114911  952 GATTTEKDRALASGMNGFLTKPVDPPALIQALRGQV 987
Cdd:cd17553     81 YGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
902-977 2.31e-03

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 39.63  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  902 GHQALKKLAQ----HPDVDAILMDLQMPEMDGCEtTLQIRKRLSADVPILALTAGATTTEKDRALAS-GMNGFLTKPVDP 976
Cdd:cd17595     36 GAEALDALKElklrGEAVALFLVDQRMPEMDGVE-FLEKAMELFPEAKRVLLTAYADTDAAIRAINDvQLDYYLLKPWDP 114

                   .
gi 2787114911  977 P 977
Cdd:cd17595    115 P 115
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
729-838 2.65e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Erythrobacter litoralis blue light-activated histidine kinase 2; This domain family includes the histidine kinase-like ATPase (HATPase) domain of blue light-activated histidine kinase 2 of Erythrobacter litoralis (EL346). Signaling commonly occurs within HK dimers, however EL346 functions as a monomer. Also included in this family are the HATPase domains of ethanolamine utilization sensory transduction histidine kinase (EutW), whereby regulation of ethanolamine, a carbon and nitrogen source for gut bacteria, results in autophosphorylation and subsequent phosphoryl transfer to a response regulator (EutV) containing an RNA-binding domain. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory PAS sensor domain, while some have an N-terminal histidine kinase domain.


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 39.32  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  729 LKQILINLLNNAIKFTDEGEVNLRISEyapaspSTVYLRFEVSDTGIGIPQTaqaklFTPFMQAEastsrkyggtgLGLS 808
Cdd:cd16951     44 VNELLQNALKHAFSDREGGTITIRSVV------DGDYLRITVIDDGVGLPQD-----EDWPNKGS-----------LGLQ 101
                           90       100       110
                   ....*....|....*....|....*....|
gi 2787114911  809 IVKRLAELIGGAVFVQSTPGQGTQFTVDLP 838
Cdd:cd16951    102 IVRSLVEGELKAFLEVQSAENGTRVNIDIP 131
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
352-422 2.91e-03

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 37.38  E-value: 2.91e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2787114911   352 QRLFKATRAASLGVWIWDLRDNTLIWDERMFELYGIphlatSQAVDYGM-WASRVHPNDLEMAESRVKNLLE 422
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGY-----SPEELIGKsLLELIHPEDRERVQEALQRLLS 67
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
498-589 3.15e-03

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 38.21  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  498 VEWSEELYRMFGADPKGpALNLEQQAAIFTPESWQRLEPAIAsavEDGTPYEIELQFTRSDGSMGWMLARGERVLDANGQ 577
Cdd:pfam13426    5 IYVNDAALRLLGYTREE-LLGKSITDLFAEPEDSERLREALR---EGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDGGE 80
                           90
                   ....*....|..
gi 2787114911  578 PVYLRGTASDIT 589
Cdd:pfam13426   81 LVGIIAILRDIT 92
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
194-282 3.67e-03

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350342 [Multi-domain]  Cd Length: 89  Bit Score: 37.81  E-value: 3.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  194 FEMAELGENGVINLRTDDLSQVVRYPPAqgdalGVGNKKVPTKVTELLGNSPDQHQLVFEAASQlDGIERLYVYQKLSTS 273
Cdd:cd18774      6 LSSIKLGETGYAFLVDSDGTILAHPPKE-----LVGKGKSLDDLALLAALLLAGESGTFEYTSD-DGVERLVAYRPVPGT 79

                   ....*....
gi 2787114911  274 PFWLSVGLS 282
Cdd:cd18774     80 PWVVVVGVP 88
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
484-598 4.99e-03

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 38.04  E-value: 4.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  484 AKVGSWRFDINKQHVEWSEELYRMFG---ADPKGpaLNLEQqaaIFTPESWQRLEpAIASAVEDGT--PYEIELQFTRSD 558
Cdd:TIGR00229   12 SPDAIIVIDLEGNILYVNPAFEEIFGysaEELIG--RNVLE---LIPEEDREEVR-ERIERRLEGEpePVSEERRVRRKD 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2787114911  559 GSMGWMLARGERVLDANGQPVYLrGTASDITTLKHQEKLL 598
Cdd:TIGR00229   86 GSEIWVEVSVSPIRTNGGELGVV-GIVRDITERKEAEEAL 124
HATPase_c_5 pfam14501
GHKL domain; This family represents the structurally related ATPase domains of histidine ...
732-821 5.93e-03

GHKL domain; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 433996 [Multi-domain]  Cd Length: 102  Bit Score: 37.58  E-value: 5.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  732 ILINLLNNAI----KFTDEGEVNLRISEyapaSPSTVYLRFEVSDTGIgipQTAQAKLFtpfmqaeaSTSRKYGGTGLGL 807
Cdd:pfam14501    9 IFGNLLDNAIeacsKIDDNRFIRLKIRE----KQNFLIIRIENTYEGE---LKFEGKLP--------STKTKGDGHGIGL 73
                           90
                   ....*....|....
gi 2787114911  808 SIVKRLAELIGGAV 821
Cdd:pfam14501   74 KSIRRIVKKYGGNL 87
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
484-588 8.05e-03

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 37.23  E-value: 8.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  484 AKVGSWRFDINKQHVEWSEELYRMFGADPKgpalNLEQQ--AAIFTPESWQRLEPAIASAVEDGTPYEIELQFTRSDGSM 561
Cdd:cd00130      1 LPDGVIVLDLDGRILYANPAAEQLLGYSPE----ELIGKslLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSV 76
                           90       100
                   ....*....|....*....|....*..
gi 2787114911  562 GWMLARGERVLDANGQPVYLRGTASDI 588
Cdd:cd00130     77 IWVLVSLTPIRDEGGEVIGLLGVVRDI 103
fixJ PRK09390
response regulator FixJ; Provisional
871-984 8.33e-03

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 38.83  E-value: 8.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  871 HVMVVDDSEinlAITKRI---LECEGATVTLcnggHQ-ALKKLAQHPDVDA--ILMDLQMPEMDGCEttlqIRKRLSAD- 943
Cdd:PRK09390     5 VVHVVDDDE---AMRDSLaflLDSAGFEVRL----FEsAQAFLDALPGLRFgcVVTDVRMPGIDGIE----LLRRLKARg 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2787114911  944 --VPILALTAGATTTEKDRALASGMNGFLTKPVDPPALIQALR 984
Cdd:PRK09390    74 spLPVIVMTGHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIE 116
PRK10643 PRK10643
two-component system response regulator PmrA;
918-973 8.47e-03

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 39.25  E-value: 8.47e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2787114911  918 ILMDLQMPEMDGCETTLQIRKRlSADVPILALTAGATTTEKDRALASGMNGFLTKP 973
Cdd:PRK10643    48 VVLDLGLPDEDGLHLLRRWRQK-KYTLPVLILTARDTLEDRVAGLDVGADDYLVKP 102
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
872-983 8.66e-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: 37.42  E-value: 8.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114911  872 VMVVDDSEINLAITKRILECEGA-TVTLCNGGHQALKKLAQ-HPDVdaILMDLQMPEMDGCETtlqIRK----RLSADVP 945
Cdd:cd17530      3 VLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCnAPDI--IICDLKMPDMDGIEF---LRHlaesHSNAAVI 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2787114911  946 IL-ALTAGATTTEKDRALASGMN--GFLTKPVDPPALIQAL 983
Cdd:cd17530     78 LMsGLDGGILESAETLAGANGLNllGTLSKPFSPEELTELL 118
 
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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