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Conserved domains on  [gi|1709973135|ref|WP_143323612|]
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PAS domain-containing hybrid sensor histidine kinase/response regulator [Cognaticolwellia aestuarii]

Protein Classification

PAS domain-containing hybrid sensor histidine kinase/response regulator( domain architecture ID 13751957)

two-component hybrid sensor histidine kinase/response regulator with one or more PAS sensor and/or ligand binding domains

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11107 super family cl35992
hybrid sensory histidine kinase BarA; Provisional
386-934 1.66e-84

hybrid sensory histidine kinase BarA; Provisional


The actual alignment was detected with superfamily member PRK11107:

Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 291.37  E-value: 1.66e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 386 ELEQAKIKAEKASQIKTEFLSMMSHELRTPMNAVIGSLDL-----LQSTKQDYeakdlIDTAKTSAENLVFILNDILDIN 460
Cdd:PRK11107  278 ELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQtlktpLTPTQRDY-----LQTIERSANNLLAIINDILDFS 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 461 KIEAGKLDIEELTFSISEIVDNVIKVYIPVAIKSDITLNVVESPFLPHFVKGDAMRVRQILFNLIGNALKFTTTtkekkG 540
Cdd:PRK11107  353 KLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTES-----G 427
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 541 VVTLTIDEIEKNDYVSNVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRITLTSELN 620
Cdd:PRK11107  428 NIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPN 507
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 621 LGSTFDVDIPFWKSQETrAMDITELDSIHVKMVSFtIQDNEREMR-IKNHLIREGANVTSvTPPKDAISPEKSDVILIII 699
Cdd:PRK11107  508 RGSTFWFHLPLDLNPNP-IIDGLPTDCLAGKRLLY-VEPNSAAAQaTLDILSETPLEVTY-SPTLSQLPEAHYDILLLGL 584
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 700 NDLFKEE-ERLTALLHDIRQY-QNIIITLTTQD-------MERGRQK-----FNKTRLIniesltrRLLIEniYQTKQQS 765
Cdd:PRK11107  585 PVTFREPlTMLHERLAKAKSMtDFLILALPCHEqvlaeqlKQDGADAclskpLSHTRLL-------PALLE--PCHHKQP 655
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 766 LEINidnldldldldldldleqltavsdgTTNKAQKNIKqnnhklktgILVVEDNPMNQKLITMQLKNIGYHCDVADNGD 845
Cdd:PRK11107  656 PLLP-------------------------PTDESRLPLT---------VMAVDDNPANLKLIGALLEEQVEHVVLCDSGH 701
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 846 DGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvHNKTaiPIVAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLR 925
Cdd:PRK11107  702 QAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPH-NQNT--PIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLK 778

                  ....*....
gi 1709973135 926 TILKKWYPH 934
Cdd:PRK11107  779 QVLLRYKPG 787
KinE super family cl47428
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
114-639 1.77e-38

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: 150.51  E-value: 1.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 114 KSLSRLTDTISATNFGIWEYNINEKEATFSNKFKEIIQInTEQQLTWKMFINAIYIEDQLLFSNNLKTHINSLTPLNFEF 193
Cdd:COG5809    12 KSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGY-TEDELLGTNILDFLHPDDEKELREILKLLKEGESRDELEF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 194 RML-LENEIHWFSIKGETFFNDN-QPICTMGTLSDCSHRKKIVHELNNAIESNNIAMEISkvgtwyaelnlhNDWVWSWD 271
Cdd:COG5809    91 ELRhKNGKRLEFSSKLSPIFDQNgDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHS------------PDGIIVTD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 272 L---------LTRQMFGFEDKAPG---IDDFdkwatcLHPDDEMRVTSTLLNSLETGKIFSESFRAVLANGKTRYFIGRG 339
Cdd:COG5809   159 LdgriiyanpAACKLLGISIEELIgksILEL------IHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 340 rVRQNENNENYRIDGIFFDETpiqstqrklknlnlkleERVnertlELEQAKIKAEKASQIkTEFLSMMSHELRTPMNAV 419
Cdd:COG5809   233 -APIKKNGEVDGIVIIFRDIT-----------------ERK-----KLEELLRKSEKLSVV-GELAAGIAHEIRNPLTSL 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 420 IGSLDLLQSTKqDYEAKDLIDTAKTSAENLVFILNDILDINKIEAGKldIEEltFSISEIVDNVIKVYIPVAIKSDITLN 499
Cdd:COG5809   289 KGFIQLLKDTI-DEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIK--YEP--KDLNTLIEEVIPLLQPQALLKNVQIE 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 500 VVESPFLPhFVKGDAMRVRQILFNLIGNALKFTTTTkekkgvVTLTIDEIEKNDyvSNVNFKISDNGIGINKENQQNLFK 579
Cdd:COG5809   364 LELEDDIP-DILGDENQLKQVFINLLKNAIEAMPEG------GNITIETKAEDD--DKVVISVTDEGCGIPEERLKKLGE 434
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 580 PFTqaerstTRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIPFWKSQETRA 639
Cdd:COG5809   435 PFY------TTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQVSM 488
PRK09776 super family cl32410
putative diguanylate cyclase; Provisional
15-203 1.10e-03

putative diguanylate cyclase; Provisional


The actual alignment was detected with superfamily member PRK09776:

Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 43.12  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135   15 MLLIDSKGLIKAVNSALTKFLNVSADDIEQKYL--LEYFTPLENNPK---NTItnNSQIYIYASESRNINKimrlningn 89
Cdd:PRK09776   296 MALVGTEGQWLQVNKALCQFLGYSQEELRGLTFqqLTWPEDLNKDLQqveKLL--SGEINSYSMEKRYYRR--------- 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135   90 iSGQFYWVLLT----KEKNWQHDY---------------WEIEKSLSRLTDTISATNFGIWEYNINEKEATFSNKFKEII 150
Cdd:PRK09776   365 -DGEVVWALLAvslvRDTDGTPLYfiaqiedinelkrteQVNERLMERITLANEAGGIGIWEWDLKPNIISWDKRMFELY 443
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1709973135  151 QINTEQQLTWKMFINAIYIEDQLLFSNNLKTHINSLTPLNFEFRMLLENEIHW 203
Cdd:PRK09776   444 EIPPHIKPTWQVWYACLHPEDRQRVEKEIRDALQGRSPFKLEFRIVVKDGVRH 496
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
386-934 1.66e-84

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 291.37  E-value: 1.66e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 386 ELEQAKIKAEKASQIKTEFLSMMSHELRTPMNAVIGSLDL-----LQSTKQDYeakdlIDTAKTSAENLVFILNDILDIN 460
Cdd:PRK11107  278 ELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQtlktpLTPTQRDY-----LQTIERSANNLLAIINDILDFS 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 461 KIEAGKLDIEELTFSISEIVDNVIKVYIPVAIKSDITLNVVESPFLPHFVKGDAMRVRQILFNLIGNALKFTTTtkekkG 540
Cdd:PRK11107  353 KLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTES-----G 427
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 541 VVTLTIDEIEKNDYVSNVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRITLTSELN 620
Cdd:PRK11107  428 NIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPN 507
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 621 LGSTFDVDIPFWKSQETrAMDITELDSIHVKMVSFtIQDNEREMR-IKNHLIREGANVTSvTPPKDAISPEKSDVILIII 699
Cdd:PRK11107  508 RGSTFWFHLPLDLNPNP-IIDGLPTDCLAGKRLLY-VEPNSAAAQaTLDILSETPLEVTY-SPTLSQLPEAHYDILLLGL 584
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 700 NDLFKEE-ERLTALLHDIRQY-QNIIITLTTQD-------MERGRQK-----FNKTRLIniesltrRLLIEniYQTKQQS 765
Cdd:PRK11107  585 PVTFREPlTMLHERLAKAKSMtDFLILALPCHEqvlaeqlKQDGADAclskpLSHTRLL-------PALLE--PCHHKQP 655
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 766 LEINidnldldldldldldleqltavsdgTTNKAQKNIKqnnhklktgILVVEDNPMNQKLITMQLKNIGYHCDVADNGD 845
Cdd:PRK11107  656 PLLP-------------------------PTDESRLPLT---------VMAVDDNPANLKLIGALLEEQVEHVVLCDSGH 701
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 846 DGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvHNKTaiPIVAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLR 925
Cdd:PRK11107  702 QAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPH-NQNT--PIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLK 778

                  ....*....
gi 1709973135 926 TILKKWYPH 934
Cdd:PRK11107  779 QVLLRYKPG 787
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
304-630 1.96e-64

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 220.16  E-value: 1.96e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 304 RVTSTLLNSLETGKIFSESFRAVLANGKTRYFIGRGRVRQNENNENYRIDGIFFDETPIQSTQRKLKNLNLKLEERVNER 383
Cdd:COG0642    13 LLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 384 TLELEQAKIKAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDyEAKDLIDTAKTSAENLVFILNDILDINKIE 463
Cdd:COG0642    93 LLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELDE-EQREYLETILRSADRLLRLINDLLDLSRLE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 464 AGKLDIEELTFSISEIVDNVIKVYIPVAIKSDITLnVVESPFLPHFVKGDAMRVRQILFNLIGNALkfttTTKEKKGVVT 543
Cdd:COG0642   172 AGKLELEPEPVDLAELLEEVVELFRPLAEEKGIEL-ELDLPDDLPTVRGDPDRLRQVLLNLLSNAI----KYTPEGGTVT 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 544 LTIDeiEKNDYVSnvnFKISDNGIGINKENQQNLFKPFTQAERSttRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGS 623
Cdd:COG0642   247 VSVR--REGDRVR---ISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGT 319

                  ....*..
gi 1709973135 624 TFDVDIP 630
Cdd:COG0642   320 TFTVTLP 326
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
365-700 9.10e-64

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: 233.13  E-value: 9.10e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 365 TQRKLKNLNLKLEERVNERTLELE--------------QAKIKAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTK 430
Cdd:TIGR02956 414 VAQELQEHKESLEQLVAQRTQELAetnerlnaevknhaKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTG 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 431 QDYEAKDLIDTAKTSAENLVFILNDILDINKIEAGKLDIEELTFSISEIVDNVIKVYIPVAIKSDITLNVVESPFLPHFV 510
Cdd:TIGR02956 494 LTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWW 573
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 511 KGDAMRVRQILFNLIGNALkftttTKEKKGVVTLTIDEIEKndyvSNVNFKISDNGIGINKENQQNLFKPFTQAErsTTR 590
Cdd:TIGR02956 574 QGDGPRIRQVLINLVGNAI-----KFTDRGSVVLRVSLNDD----SSLLFEVEDTGCGIAEEEQATLFDAFTQAD--GRR 642
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 591 KYGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIPFWKSQETRAMDITELDSIHVKMVsFTIQDNEREMRI-KNH 669
Cdd:TIGR02956 643 RSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTVIDLPPQRV-LLVEDNEVNQMVaQGF 721
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1709973135 670 LIREGANVTSVTPPKDA---ISPEKSDVILIIIN 700
Cdd:TIGR02956 722 LTRLGHKVTLAESGQSAlecFHQHAFDLALLDIN 755
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
814-928 4.26e-44

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: 154.93  E-value: 4.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEavHNKTAIPIVA 893
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELE--GGGRRTPIIA 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTIL 928
Cdd:cd17546    79 LTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
114-639 1.77e-38

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: 150.51  E-value: 1.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 114 KSLSRLTDTISATNFGIWEYNINEKEATFSNKFKEIIQInTEQQLTWKMFINAIYIEDQLLFSNNLKTHINSLTPLNFEF 193
Cdd:COG5809    12 KSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGY-TEDELLGTNILDFLHPDDEKELREILKLLKEGESRDELEF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 194 RML-LENEIHWFSIKGETFFNDN-QPICTMGTLSDCSHRKKIVHELNNAIESNNIAMEISkvgtwyaelnlhNDWVWSWD 271
Cdd:COG5809    91 ELRhKNGKRLEFSSKLSPIFDQNgDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHS------------PDGIIVTD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 272 L---------LTRQMFGFEDKAPG---IDDFdkwatcLHPDDEMRVTSTLLNSLETGKIFSESFRAVLANGKTRYFIGRG 339
Cdd:COG5809   159 LdgriiyanpAACKLLGISIEELIgksILEL------IHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 340 rVRQNENNENYRIDGIFFDETpiqstqrklknlnlkleERVnertlELEQAKIKAEKASQIkTEFLSMMSHELRTPMNAV 419
Cdd:COG5809   233 -APIKKNGEVDGIVIIFRDIT-----------------ERK-----KLEELLRKSEKLSVV-GELAAGIAHEIRNPLTSL 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 420 IGSLDLLQSTKqDYEAKDLIDTAKTSAENLVFILNDILDINKIEAGKldIEEltFSISEIVDNVIKVYIPVAIKSDITLN 499
Cdd:COG5809   289 KGFIQLLKDTI-DEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIK--YEP--KDLNTLIEEVIPLLQPQALLKNVQIE 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 500 VVESPFLPhFVKGDAMRVRQILFNLIGNALKFTTTTkekkgvVTLTIDEIEKNDyvSNVNFKISDNGIGINKENQQNLFK 579
Cdd:COG5809   364 LELEDDIP-DILGDENQLKQVFINLLKNAIEAMPEG------GNITIETKAEDD--DKVVISVTDEGCGIPEERLKKLGE 434
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 580 PFTqaerstTRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIPFWKSQETRA 639
Cdd:COG5809   435 PFY------TTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQVSM 488
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
512-631 2.16e-27

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 107.35  E-value: 2.16e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135  512 GDAMRVRQILFNLIGNALKFTTTTkekkGVVTLTIDEIEKNdyvsnVNFKISDNGIGINKENQQNLFKPFTQAeRSTTRK 591
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEG----GRITVTLERDGDH-----VEITVEDNGPGIPPEDLEKIFEPFFRT-DKRSRK 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1709973135  592 YGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIPF 631
Cdd:smart00387  71 IGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPL 110
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
512-631 1.29e-25

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: 102.06  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 512 GDAMRVRQILFNLIGNALKFTTTTkekkGVVTLTIDEIEkndyvsNVNFKISDNGIGINKENQQNLFKPFTQAErstTRK 591
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKA----GEITVTLSEGG------ELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRG 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1709973135 592 YGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIPF 631
Cdd:pfam02518  68 GGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPL 107
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
389-630 1.03e-22

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 103.18  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 389 QAKI-KAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLqstkqdYEAKDLID-TAKTSAENLV-----F--ILNDILDI 459
Cdd:NF040691  258 QRQIrQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVI------HDSRDDFDpATARSAELLHteldrFesLLSDLLEI 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 460 NKIEAG--KLDIEELtfSISEIVDNVIKVYIPVAIKSDITLnVVESPFLPHFVKGDAMRVRQILFNLIGNALKFTTTTKE 537
Cdd:NF040691  332 SRFDAGaaELDVEPV--DLRPLVRRVVDALRQLAERAGVEL-RVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPV 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 538 kkgVVTLTIDEiekndyvSNVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRITLTS 617
Cdd:NF040691  409 ---VVTVAQDD-------TAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWG 478
                         250
                  ....*....|...
gi 1709973135 618 ELNLGSTFDVDIP 630
Cdd:NF040691  479 RPGQGSQFRLTLP 491
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
395-613 6.48e-13

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 72.17  E-value: 6.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 395 EKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEAKDLiDTAKTSAENLVFILNDILDINKIEAGKLDIEELTF 474
Cdd:NF012163  234 EKNEQMRRDFMADISHELRTPLAVLRAELEAIQDGIRKFTPESL-DSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASV 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 475 SISEIVDNVIKVYIPVAIKSDITLNvVESPFLPhFVKGDAMRVRQILFNLIGNALkfttTTKEKKGVVTLTIDEIEKndy 554
Cdd:NF012163  313 DLVPLLEVEGGAFRERFASAGLELE-VSLPDSS-LVFGDRDRLMQLFNNLLENSL----RYTDSGGSLHISASQRPK--- 383
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1709973135 555 vsNVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRI 613
Cdd:NF012163  384 --EVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTL 440
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
410-630 6.73e-12

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 68.10  E-value: 6.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 410 HELRTPMNAVIGSLD-LLQSTKQDYEA--KDLIDtaktSAENLVFILNDILDINKIEAG--KLDIEELTFsiSEIVDNVI 484
Cdd:NF012226  147 HELRTPITILQGRLQgILDGVFEPDPAlfKSLLN----QVEGLSHLVEDLRTLSLVENQqlRLNYESVDL--KDSIEKVL 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 485 KVYIPVAIKSDIT--LNVVESPflphfVKGDAMRVRQILFNLIGNALkftttTKEKKGVVTLTiDEIEKNDYVsnvnFKI 562
Cdd:NF012226  221 KMFEDRLEQAQLTivLNLTATP-----VFCDRRRIEQVLIALIDNAI-----RYANAGKLKIS-SSVIQDDWI----LQI 285
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709973135 563 SDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRITLTSElNLGSTFDVDIP 630
Cdd:NF012226  286 EDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEYSNS-QGNSVFTIKLP 352
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
267-355 7.19e-12

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: 62.36  E-value: 7.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 267 VWSWDLLTRQMFGFEdkaPG--IDDFDKWATCLHPDDEMRVTSTLLNSLETGKIFSESFRAVLANGKTRYFIGRGRVRQN 344
Cdd:pfam08447   1 IIYWSPRFEEILGYT---PEelLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRD 77
                          90
                  ....*....|.
gi 1709973135 345 ENNENYRIDGI 355
Cdd:pfam08447  78 ENGKPVRVIGV 88
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
154-383 7.66e-08

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 56.60  E-value: 7.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135  154 TEQQLTWKMFINAiyieDQLLFSNNLKTHINSltplnfeFRMllenEIHWFSIKGETFF----------NDNQPICTMGT 223
Cdd:PRK09776   327 TFQQLTWPEDLNK----DLQQVEKLLSGEINS-------YSM----EKRYYRRDGEVVWallavslvrdTDGTPLYFIAQ 391
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135  224 LSDCSHRKKIVHELNNAIESNNIAMEISKVGTWyaELNLHNDwVWSWDlltRQMFGFEDKAPGID-DFDKWATCLHPDDE 302
Cdd:PRK09776   392 IEDINELKRTEQVNERLMERITLANEAGGIGIW--EWDLKPN-IISWD---KRMFELYEIPPHIKpTWQVWYACLHPEDR 465
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135  303 MRVTSTLLNSLETGKIFSESFRAVLANGkTRYFIGRGRVRQNENNENYRIDGIFFDETPIqstqrklKNLNLKL-EERvn 381
Cdd:PRK09776   466 QRVEKEIRDALQGRSPFKLEFRIVVKDG-VRHIRALANRVLNKDGEVERLLGINMDMTEV-------RQLNEALfQEK-- 535

                   ..
gi 1709973135  382 ER 383
Cdd:PRK09776   536 ER 537
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
15-203 1.10e-03

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 43.12  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135   15 MLLIDSKGLIKAVNSALTKFLNVSADDIEQKYL--LEYFTPLENNPK---NTItnNSQIYIYASESRNINKimrlningn 89
Cdd:PRK09776   296 MALVGTEGQWLQVNKALCQFLGYSQEELRGLTFqqLTWPEDLNKDLQqveKLL--SGEINSYSMEKRYYRR--------- 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135   90 iSGQFYWVLLT----KEKNWQHDY---------------WEIEKSLSRLTDTISATNFGIWEYNINEKEATFSNKFKEII 150
Cdd:PRK09776   365 -DGEVVWALLAvslvRDTDGTPLYfiaqiedinelkrteQVNERLMERITLANEAGGIGIWEWDLKPNIISWDKRMFELY 443
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1709973135  151 QINTEQQLTWKMFINAIYIEDQLLFSNNLKTHINSLTPLNFEFRMLLENEIHW 203
Cdd:PRK09776   444 EIPPHIKPTWQVWYACLHPEDRQRVEKEIRDALQGRSPFKLEFRIVVKDGVRH 496
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
386-934 1.66e-84

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 291.37  E-value: 1.66e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 386 ELEQAKIKAEKASQIKTEFLSMMSHELRTPMNAVIGSLDL-----LQSTKQDYeakdlIDTAKTSAENLVFILNDILDIN 460
Cdd:PRK11107  278 ELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQtlktpLTPTQRDY-----LQTIERSANNLLAIINDILDFS 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 461 KIEAGKLDIEELTFSISEIVDNVIKVYIPVAIKSDITLNVVESPFLPHFVKGDAMRVRQILFNLIGNALKFTTTtkekkG 540
Cdd:PRK11107  353 KLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTES-----G 427
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 541 VVTLTIDEIEKNDYVSNVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRITLTSELN 620
Cdd:PRK11107  428 NIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPN 507
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 621 LGSTFDVDIPFWKSQETrAMDITELDSIHVKMVSFtIQDNEREMR-IKNHLIREGANVTSvTPPKDAISPEKSDVILIII 699
Cdd:PRK11107  508 RGSTFWFHLPLDLNPNP-IIDGLPTDCLAGKRLLY-VEPNSAAAQaTLDILSETPLEVTY-SPTLSQLPEAHYDILLLGL 584
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 700 NDLFKEE-ERLTALLHDIRQY-QNIIITLTTQD-------MERGRQK-----FNKTRLIniesltrRLLIEniYQTKQQS 765
Cdd:PRK11107  585 PVTFREPlTMLHERLAKAKSMtDFLILALPCHEqvlaeqlKQDGADAclskpLSHTRLL-------PALLE--PCHHKQP 655
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 766 LEINidnldldldldldldleqltavsdgTTNKAQKNIKqnnhklktgILVVEDNPMNQKLITMQLKNIGYHCDVADNGD 845
Cdd:PRK11107  656 PLLP-------------------------PTDESRLPLT---------VMAVDDNPANLKLIGALLEEQVEHVVLCDSGH 701
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 846 DGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvHNKTaiPIVAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLR 925
Cdd:PRK11107  702 QAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPH-NQNT--PIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLK 778

                  ....*....
gi 1709973135 926 TILKKWYPH 934
Cdd:PRK11107  779 QVLLRYKPG 787
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
379-928 8.55e-73

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 258.37  E-value: 8.55e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 379 RVN-ERTL-ELEQAkikAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEAKDLIDTAKTSAENLVFILNDI 456
Cdd:PRK10841  426 RVKmEESLqEMAQA---AEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDI 502
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 457 LDINKIEAGKLDIEELTFSISEIVDNVIKVYIPVAIKSDITLNVVESPFLPHFVKGDAMRVRQILFNLIGNALkftttTK 536
Cdd:PRK10841  503 LDFSKIESEQLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAI-----KF 577
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 537 EKKGVVTLTIdeIEKNDYVSnvnFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRITLT 616
Cdd:PRK10841  578 TDTGCIVLHV--RVDGDYLS---FRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVD 652
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 617 SELNLGSTFDVDIPFWKSQETRamdITELDSIHVKMVSFTIQDNEREMRIKNHLIREGANVTSVTPPKdaisPEKSDVil 696
Cdd:PRK10841  653 SEPGMGSQFTIRIPLYGAQYPQ---KKGVEGLQGKRCWLAVRNASLEQFLETLLQRSGIQVQRYEGQE----PTPEDV-- 723
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 697 IIINDLFKEEERLTALLHDIRQYQNIiitltTQDMERGRQKFNKTRLINIEsltrrLLIENIYQTkqqsleinidnldld 776
Cdd:PRK10841  724 LITDDPVQKKWQGRAVITFCRRHIGI-----PLEIAPGEWVHSTATPHELP-----ALLARIYRI--------------- 778
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 777 ldldldldlEQLTAVSDGTTNKAQKNIKQNNHKLktgILVVEDNPMNQKLITMQLKNIGYHCDVADNGDD--GKIKWQSG 854
Cdd:PRK10841  779 ---------ELESDDSANALPSTDKAVSDNDDMM---ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDalNVLSKNHI 846
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709973135 855 DykLIITDCHMPIMDGYEMTRGIRELeavhNKTaIPIVAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTIL 928
Cdd:PRK10841  847 D--IVLTDVNMPNMDGYRLTQRLRQL----GLT-LPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVLKQTL 913
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
304-630 1.96e-64

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 220.16  E-value: 1.96e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 304 RVTSTLLNSLETGKIFSESFRAVLANGKTRYFIGRGRVRQNENNENYRIDGIFFDETPIQSTQRKLKNLNLKLEERVNER 383
Cdd:COG0642    13 LLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 384 TLELEQAKIKAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDyEAKDLIDTAKTSAENLVFILNDILDINKIE 463
Cdd:COG0642    93 LLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELDE-EQREYLETILRSADRLLRLINDLLDLSRLE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 464 AGKLDIEELTFSISEIVDNVIKVYIPVAIKSDITLnVVESPFLPHFVKGDAMRVRQILFNLIGNALkfttTTKEKKGVVT 543
Cdd:COG0642   172 AGKLELEPEPVDLAELLEEVVELFRPLAEEKGIEL-ELDLPDDLPTVRGDPDRLRQVLLNLLSNAI----KYTPEGGTVT 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 544 LTIDeiEKNDYVSnvnFKISDNGIGINKENQQNLFKPFTQAERSttRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGS 623
Cdd:COG0642   247 VSVR--REGDRVR---ISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGT 319

                  ....*..
gi 1709973135 624 TFDVDIP 630
Cdd:COG0642   320 TFTVTLP 326
PRK15347 PRK15347
two component system sensor kinase;
376-928 2.75e-64

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 234.15  E-value: 2.75e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 376 LEERVNERTLELEQAKIKAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEAKDLIDTAKTSAENLVFILND 455
Cdd:PRK15347  373 LENKVAERTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINN 452
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 456 ILDINKIEAGKLDIEELTFSISEIVDNVIKVYIPVAIKSDITLNVVESPFLPHFVKGDAMRVRQILFNLIGNALkftttT 535
Cdd:PRK15347  453 LLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAV-----K 527
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 536 KEKKGVVTLTIDEIEKNDYvsnvnFKISDNGIGINKENQQNLFKPFTQAERSTtrkyGGTGLGLAICGKLSNLMGGRITL 615
Cdd:PRK15347  528 FTETGGIRLRVKRHEQQLC-----FTVEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKMMGGELTL 598
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 616 TSELNLGSTFDVDIPFwksqetraMDITELDSIHVKMVSftiqdnerEMRIKNHLIREGAnvtsvTPPKDAISPEKSDvi 695
Cdd:PRK15347  599 FSTPGVGSCFSLVLPL--------NEYAPPEPLKGELSA--------PLALHRQLSAWGI-----TCQPGHQNPALLD-- 655
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 696 liiiNDLFKEEERLTALLHDIRQyqniiitlttqdmergrqkfnktrliniesltrrllieniyqtkqqsleinidnldl 775
Cdd:PRK15347  656 ----PELAYLPGRLYDLLQQIIQ--------------------------------------------------------- 674
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 776 dldldldldleqltavsdGTTNKAQKNIKQNNHKLKtgILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGD 855
Cdd:PRK15347  675 ------------------GAPNEPVINLPLQPWQLQ--ILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHR 734
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709973135 856 YKLIITDCHMPIMDGYEMTRGIRELEAVHNkTAIPIVAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTIL 928
Cdd:PRK15347  735 FDLVLMDIRMPGLDGLETTQLWRDDPNNLD-PDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARAL 806
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
365-700 9.10e-64

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: 233.13  E-value: 9.10e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 365 TQRKLKNLNLKLEERVNERTLELE--------------QAKIKAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTK 430
Cdd:TIGR02956 414 VAQELQEHKESLEQLVAQRTQELAetnerlnaevknhaKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTG 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 431 QDYEAKDLIDTAKTSAENLVFILNDILDINKIEAGKLDIEELTFSISEIVDNVIKVYIPVAIKSDITLNVVESPFLPHFV 510
Cdd:TIGR02956 494 LTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWW 573
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 511 KGDAMRVRQILFNLIGNALkftttTKEKKGVVTLTIDEIEKndyvSNVNFKISDNGIGINKENQQNLFKPFTQAErsTTR 590
Cdd:TIGR02956 574 QGDGPRIRQVLINLVGNAI-----KFTDRGSVVLRVSLNDD----SSLLFEVEDTGCGIAEEEQATLFDAFTQAD--GRR 642
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 591 KYGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIPFWKSQETRAMDITELDSIHVKMVsFTIQDNEREMRI-KNH 669
Cdd:TIGR02956 643 RSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTVIDLPPQRV-LLVEDNEVNQMVaQGF 721
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1709973135 670 LIREGANVTSVTPPKDA---ISPEKSDVILIIIN 700
Cdd:TIGR02956 722 LTRLGHKVTLAESGQSAlecFHQHAFDLALLDIN 755
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
386-630 6.34e-61

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 207.07  E-value: 6.34e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 386 ELEQAKIKAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEAK--DLIDTAKTSAENLVFILNDILDINKIE 463
Cdd:COG2205     1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLSPEErrELLEIIRESAERLLRLIEDLLDLSRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 464 AGKLDIEELTFSISEIVDNVIKVYIPVAIKSDITLNVVESPFLPhFVKGDAMRVRQILFNLIGNALkfttTTKEKKGVVT 543
Cdd:COG2205    81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELP-LVYADPELLEQVLANLLDNAI----KYSPPGGTIT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 544 LTIDEIEKndyvsNVNFKISDNGIGINKENQQNLFKPFTQAERstTRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGS 623
Cdd:COG2205   156 ISARREGD-----GVRISVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGT 228

                  ....*..
gi 1709973135 624 TFDVDIP 630
Cdd:COG2205   229 TFTVTLP 235
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
300-630 1.44e-55

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 197.47  E-value: 1.44e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 300 DDEMRVTSTLLNSLETGKIFSESFRAVLANGKTRYFIGRGRVRQNENNENYRIDGIFFDETPIQSTQRKLKNLNLKLEER 379
Cdd:COG5002    64 LLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLL 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 380 VNERTLELEQAKIKAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQS--TKQDYEAKDLIDTAKTSAENLVFILNDIL 457
Cdd:COG5002   144 GLLLLAAVERDITELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDgaADDPEERREYLEIILEEAERLSRLVNDLL 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 458 DINKIEAGKLDIEELTFSISEIVDNVIKVYIPVAIKSDITLnVVESPFLPHFVKGDAMRVRQILFNLIGNALKFTTTTke 537
Cdd:COG5002   224 DLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIEL-ELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEG-- 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 538 kkGVVTLTIDEIEKNdyvsnVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRITLTS 617
Cdd:COG5002   301 --GTITVSLREEDDQ-----VRISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVES 373
                         330
                  ....*....|...
gi 1709973135 618 ELNLGSTFDVDIP 630
Cdd:COG5002   374 EPGKGTTFTITLP 386
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
814-928 4.26e-44

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: 154.93  E-value: 4.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEavHNKTAIPIVA 893
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELE--GGGRRTPIIA 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTIL 928
Cdd:cd17546    79 LTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
517-631 1.97e-41

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: 147.25  E-value: 1.97e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 517 VRQILFNLIGNALKFTTTtkekkGVVTLTIDEIEKNDYVSNVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTG 596
Cdd:cd16922     1 LRQILLNLLGNAIKFTEE-----GEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTG 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1709973135 597 LGLAICGKLSNLMGGRITLTSELNLGSTFDVDIPF 631
Cdd:cd16922    76 LGLAISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
230-630 7.09e-41

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 158.02  E-value: 7.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 230 RKKIVHELNNAIESNNIAMEISKVGTWYAELNLHNDWVWSWDLLTRQMFGFEDKAPGIDDFDKWATCLHPDDEMRVTSTL 309
Cdd:COG4251   120 LLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLL 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 310 LNSLETGKIFSESFRAVLANGKTRYFIGRGRVRQNENNENYRIDGIFFDETPIQSTQRKLknLNLKLEERVNERTLELEQ 389
Cdd:COG4251   200 LLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRL--ELEELEEELEERTAELER 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 390 AKikAEKAsqiktEFLSMMSHELRTPMNAVIGSLDLLQ---STKQDYEAKDLIDTAKTSAENLVFILNDILDINKIEAGK 466
Cdd:COG4251   278 SN--EELE-----QFAYVASHDLREPLRKISGFSQLLEedyGDKLDEEGREYLERIRDAAERMQALIDDLLAYSRVGRQE 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 467 LDIEelTFSISEIVDNVIKVYIPVAIKSDITLNVVEspfLPHfVKGDAMRVRQILFNLIGNALKFTTTTKEkkGVVTLTI 546
Cdd:COG4251   351 LEFE--PVDLNELLEEVLEDLEPRIEERGAEIEVGP---LPT-VRGDPTLLRQVFQNLISNAIKYSRPGEP--PRIEIGA 422
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 547 dEIEKNDYVsnvnFKISDNGIGINKENQQNLFKPFTQAerSTTRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFD 626
Cdd:COG4251   423 -EREGGEWV----FSVRDNGIGIDPEYAEKIFEIFQRL--HSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFY 495

                  ....
gi 1709973135 627 VDIP 630
Cdd:COG4251   496 FTLP 499
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
814-931 1.15e-40

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: 145.76  E-value: 1.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVHNktaIPIVA 893
Cdd:COG0784     8 ILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPD---IPIIA 84
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTILKKW 931
Cdd:COG0784    85 LTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRL 122
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
386-935 9.31e-40

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 158.57  E-value: 9.31e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 386 ELEQAKIKAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEAKDLIDTAKTSAENLVFILNDILDINKIEAG 465
Cdd:PRK11091  268 ERKRYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERR 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 466 KLDIEELTFSISEIVDNVIKVYIPVAIKSDITLNVVESPFLPHFVKGDAMRVRQILFNLIGNALkftttTKEKKGVVTLT 545
Cdd:PRK11091  348 KLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAV-----KFTQQGGVTVR 422
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 546 IdEIEKNDyvsNVNFKISDNGIGINKENQQNLFKPFTQAERST-TRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGST 624
Cdd:PRK11091  423 V-RYEEGD---MLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHgGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSC 498
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 625 FDVdipfwksqetramditeldSIHVKMVSFTIQDNEREmriknhlireganvtsvtppkdaispeksdviliiindlfk 704
Cdd:PRK11091  499 FTL-------------------TIHAPAVAEEVEDAFDE----------------------------------------- 518
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 705 EEERLTALlhdirqyqniiitlttqdmergrqkfnktrliniesltrrllieniyqtkqqsleinidnldldldldldld 784
Cdd:PRK11091  519 DDMPLPAL------------------------------------------------------------------------ 526
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 785 leqltavsdgttnkaqknikqnnhklktGILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCH 864
Cdd:PRK11091  527 ----------------------------NILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQ 578
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709973135 865 MPIMDGYEMTRGIRELEAVHNKTaiPIVAVTgAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTILKK-WYPHE 935
Cdd:PRK11091  579 LPDMTGLDIARELRERYPREDLP--PLVALT-ANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIKKfWDTQD 647
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
363-687 2.28e-39

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 158.14  E-value: 2.28e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 363 QSTQRKLKNLNLKLEERVNERTLELE-------QAKIKAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEA 435
Cdd:PRK11466  399 RSNVHALNRHREQLAAQVKARTAELQelviehrQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQ 478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 436 KDLIDTAKTSAENLVFILNDILDINKIEAG--KLDIEELTFSISEIVDNVIKV------YIPVAIKSDItlnvveSPFLP 507
Cdd:PRK11466  479 RDDLRAITDSGESLLTILNDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLmsgrvkGRPIRLATDI------ADDLP 552
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 508 HFVKGDAMRVRQILFNLIGNALkftttTKEKKGVVTLTIDEIEKNDYVSnvnfkISDNGIGINKENQQNLFKPFTQAers 587
Cdd:PRK11466  553 TALMGDPRRIRQVITNLLSNAL-----RFTDEGSIVLRSRTDGEQWLVE-----VEDSGCGIDPAKLAEIFQPFVQV--- 619
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 588 tTRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIPFWK----SQETRAMDITeLDSIHVKMvsftIQDNERE 663
Cdd:PRK11466  620 -SGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVatapVPKTVNQAVR-LDGLRLLL----IEDNPLT 693
                         330       340
                  ....*....|....*....|....*
gi 1709973135 664 MRIKNHLIR-EGANVTSVTPPKDAI 687
Cdd:PRK11466  694 QRITAEMLNtSGAQVVAVGNAAQAL 718
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
114-639 1.77e-38

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: 150.51  E-value: 1.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 114 KSLSRLTDTISATNFGIWEYNINEKEATFSNKFKEIIQInTEQQLTWKMFINAIYIEDQLLFSNNLKTHINSLTPLNFEF 193
Cdd:COG5809    12 KSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGY-TEDELLGTNILDFLHPDDEKELREILKLLKEGESRDELEF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 194 RML-LENEIHWFSIKGETFFNDN-QPICTMGTLSDCSHRKKIVHELNNAIESNNIAMEISkvgtwyaelnlhNDWVWSWD 271
Cdd:COG5809    91 ELRhKNGKRLEFSSKLSPIFDQNgDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHS------------PDGIIVTD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 272 L---------LTRQMFGFEDKAPG---IDDFdkwatcLHPDDEMRVTSTLLNSLETGKIFSESFRAVLANGKTRYFIGRG 339
Cdd:COG5809   159 LdgriiyanpAACKLLGISIEELIgksILEL------IHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 340 rVRQNENNENYRIDGIFFDETpiqstqrklknlnlkleERVnertlELEQAKIKAEKASQIkTEFLSMMSHELRTPMNAV 419
Cdd:COG5809   233 -APIKKNGEVDGIVIIFRDIT-----------------ERK-----KLEELLRKSEKLSVV-GELAAGIAHEIRNPLTSL 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 420 IGSLDLLQSTKqDYEAKDLIDTAKTSAENLVFILNDILDINKIEAGKldIEEltFSISEIVDNVIKVYIPVAIKSDITLN 499
Cdd:COG5809   289 KGFIQLLKDTI-DEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIK--YEP--KDLNTLIEEVIPLLQPQALLKNVQIE 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 500 VVESPFLPhFVKGDAMRVRQILFNLIGNALKFTTTTkekkgvVTLTIDEIEKNDyvSNVNFKISDNGIGINKENQQNLFK 579
Cdd:COG5809   364 LELEDDIP-DILGDENQLKQVFINLLKNAIEAMPEG------GNITIETKAEDD--DKVVISVTDEGCGIPEERLKKLGE 434
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 580 PFTqaerstTRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIPFWKSQETRA 639
Cdd:COG5809   435 PFY------TTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQVSM 488
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
814-925 5.42e-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: 122.71  E-value: 5.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVHNktaIPIVA 893
Cdd:COG3706     4 ILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTAD---IPIIF 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLR 925
Cdd:COG3706    81 LTALDDEEDRARALEAGADDYLTKPFDPEELL 112
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
387-932 2.00e-31

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 133.32  E-value: 2.00e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135  387 LEQAKIKAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEAK-DLIDTAKTSAENLVFILNDILDINKIEAG 465
Cdd:PRK09959   698 LEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIESG 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135  466 KLDIEELTFSISEIVDNVIKVYIPVAIKSDITLNVvESPFLPHF-VKGDAMRVRQILFNLIGNALkftttTKEKKGVVTL 544
Cdd:PRK09959   778 NYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSC-SSTFPDHYlVKIDPQAFKQVLSNLLSNAL-----KFTTEGAVKI 851
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135  545 TIDEIEKNDYVSNVNFKISDNGIGINKENQQNLFKPFTQAerSTTRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGST 624
Cdd:PRK09959   852 TTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQT--SAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTT 929
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135  625 FDVDIPFWKSQETRAMditeldsihvkmvsftiqdneremriknhlirEGANVTSVTPPKdaispeksdviliiindlfk 704
Cdd:PRK09959   930 FTITIPVEISQQVATV--------------------------------EAKAEQPITLPE-------------------- 957
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135  705 eeerltallhdirqyqniiitlttqdmergrqkfnktrliniesltrrllieniyqtkqqsleinidnldldldldldld 784
Cdd:PRK09959       --------------------------------------------------------------------------------
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135  785 leqltavsdgttnkaqknikqnnhklKTGILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCH 864
Cdd:PRK09959   958 --------------------------KLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVN 1011
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709973135  865 MPIMDGYEMTRGIREleavhNKTAIPIVAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTILKKWY 932
Cdd:PRK09959  1012 MPNMDGFELTRKLRE-----QNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLH 1074
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
319-637 2.06e-31

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 126.88  E-value: 2.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 319 FSESFRAVLANGKTryFIGRGRVRQNENNENYRIDGIFfdeTPIQSTQRKLKNLnlkLEERVNERTLELEQAKIKAEKAS 398
Cdd:COG3852    62 LRELLERALAEGQP--VTEREVTLRRKDGEERPVDVSV---SPLRDAEGEGGVL---LVLRDITERKRLERELRRAEKLA 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 399 QIKtEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEAKDLIDTAKTSAENLVFILNDILDINKIEAGKLDieelTFSISE 478
Cdd:COG3852   134 AVG-ELAAGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPERE----PVNLHE 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 479 IVDNVIKVyIPVAIKSDITLNVVESPFLPHfVKGDAMRVRQILFNLIGNALKFTTTTkekkGVVTLT-----IDEIEKND 553
Cdd:COG3852   209 VLERVLEL-LRAEAPKNIRIVRDYDPSLPE-VLGDPDQLIQVLLNLVRNAAEAMPEG----GTITIRtrverQVTLGGLR 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 554 YVSNVNFKISDNGIGINKENQQNLFKPFTqaersTTRKyGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIPFWK 633
Cdd:COG3852   283 PRLYVRIEVIDNGPGIPEEILDRIFEPFF-----TTKE-KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQ 356

                  ....
gi 1709973135 634 SQET 637
Cdd:COG3852   357 AEEE 360
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
333-630 6.70e-29

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 119.52  E-value: 6.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 333 RYFIGRGRVRQNENNENYRIDGIFFDETPIQSTQRKLKNLNLKLEERVNERtLELEQAKIKAEKASQIKtEFLSMMSHEL 412
Cdd:COG4191    76 LRLLLLLGLLLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEEL-RELQEQLVQSEKLAALG-ELAAGIAHEI 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 413 RTPMNAVIGSLDLLQSTKQDY----EAKDLIDTAKTSAENLVFILNDILDINKieAGKLDIEEltFSISEIVDNVIKVYI 488
Cdd:COG4191   154 NNPLAAILGNAELLRRRLEDEpdpeELREALERILEGAERAAEIVRSLRAFSR--RDEEEREP--VDLNELIDEALELLR 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 489 PVAIKSDITLNVVESPFLPHfVKGDAMRVRQILFNLIGNALKFTTTTKEkkGVVTLTIDEieKNDYVSnvnFKISDNGIG 568
Cdd:COG4191   230 PRLKARGIEVELDLPPDLPP-VLGDPGQLEQVLLNLLINAIDAMEEGEG--GRITISTRR--EGDYVV---ISVRDNGPG 301
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709973135 569 INKENQQNLFKPFTqaersTTRKYG-GTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIP 630
Cdd:COG4191   302 IPPEVLERIFEPFF-----TTKPVGkGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLP 359
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
304-636 1.61e-27

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: 116.60  E-value: 1.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 304 RVTSTLLNSLETGKI-FSESFRAVLANGKTRYFIGRGRVR---QNENNENYRIDGIFFDETPIQSTQRKLKNLNLKLEER 379
Cdd:COG5000    90 RYLETILENLPAGVIvLDADGRITLANPAAERLLGIPLEEligKPLEELLPELDLAELLREALERGWQEEIELTRDGRRT 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 380 VNERTLELEQ-----------AKIKAEKASQIKtEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEAKD------LIDTA 442
Cdd:COG5000   170 LLVRASPLRDdgyvivfdditELLRAERLAAWG-ELARRIAHEIKNPLTPIQLSAERLRRKLADKLEEDredlerALDTI 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 443 KTSAENLVFILNDILDINKIEAGKLDieelTFSISEIVDNVIKVYIPVAIKSDITLNVVESPFLPhFVKGDAMRVRQILF 522
Cdd:COG5000   249 IRQVDRLKRIVDEFLDFARLPEPQLE----PVDLNELLREVLALYEPALKEKDIRLELDLDPDLP-EVLADRDQLEQVLI 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 523 NLIGNALKFTTTTkekkGVVTLTIDEIEkndyvSNVNFKISDNGIGINKENQQNLFKPFTqaersTTRKyGGTGLGLAIC 602
Cdd:COG5000   324 NLLKNAIEAIEEG----GEIEVSTRRED-----GRVRIEVSDNGPGIPEEVLERIFEPFF-----TTKP-KGTGLGLAIV 388
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1709973135 603 GKLSNLMGGRITLTSELNLGSTFDVDIPFWKSQE 636
Cdd:COG5000   389 KKIVEEHGGTIELESRPGGGTTFTIRLPLAEEAE 422
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
512-631 2.16e-27

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 107.35  E-value: 2.16e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135  512 GDAMRVRQILFNLIGNALKFTTTTkekkGVVTLTIDEIEKNdyvsnVNFKISDNGIGINKENQQNLFKPFTQAeRSTTRK 591
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEG----GRITVTLERDGDH-----VEITVEDNGPGIPPEDLEKIFEPFFRT-DKRSRK 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1709973135  592 YGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIPF 631
Cdd:smart00387  71 IGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPL 110
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
814-930 6.93e-26

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: 106.79  E-value: 6.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVHNktaIPIVA 893
Cdd:COG3437     9 VLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRD---IPVIF 85
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTILKK 930
Cdd:COG3437    86 LTALADPEDRERALEAGADDYLTKPFDPEELLARVRN 122
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
512-631 1.29e-25

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: 102.06  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 512 GDAMRVRQILFNLIGNALKFTTTTkekkGVVTLTIDEIEkndyvsNVNFKISDNGIGINKENQQNLFKPFTQAErstTRK 591
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKA----GEITVTLSEGG------ELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRG 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1709973135 592 YGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIPF 631
Cdd:pfam02518  68 GGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPL 107
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
814-929 3.12e-25

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: 104.27  E-value: 3.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvhnktAIPIVA 893
Cdd:COG0745     4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPS-----DIPIIM 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTILK 929
Cdd:COG0745    79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIR 114
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
814-929 4.09e-25

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 100.69  E-value: 4.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVhnktaIPIVA 893
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPT-----TPVII 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTILK 929
Cdd:pfam00072  76 LTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
389-630 1.03e-22

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 103.18  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 389 QAKI-KAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLqstkqdYEAKDLID-TAKTSAENLV-----F--ILNDILDI 459
Cdd:NF040691  258 QRQIrQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVI------HDSRDDFDpATARSAELLHteldrFesLLSDLLEI 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 460 NKIEAG--KLDIEELtfSISEIVDNVIKVYIPVAIKSDITLnVVESPFLPHFVKGDAMRVRQILFNLIGNALKFTTTTKE 537
Cdd:NF040691  332 SRFDAGaaELDVEPV--DLRPLVRRVVDALRQLAERAGVEL-RVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPV 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 538 kkgVVTLTIDEiekndyvSNVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRITLTS 617
Cdd:NF040691  409 ---VVTVAQDD-------TAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWG 478
                         250
                  ....*....|...
gi 1709973135 618 ELNLGSTFDVDIP 630
Cdd:NF040691  479 RPGQGSQFRLTLP 491
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
814-930 1.67e-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: 93.37  E-value: 1.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDG--KIKWQSGDykLIITDCHMPIMDGYEMTRGIRELEAVHNktaIPI 891
Cdd:cd17548     2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEAleIARKEKPD--LILMDIQLPGMDGLEATRLLKEDPATRD---IPV 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1709973135 892 VAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTILKK 930
Cdd:cd17548    77 IALTAYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
517-629 2.07e-22

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 92.67  E-value: 2.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 517 VRQILFNLIGNALkfttTTKEKKGVVTLTIDEIEKNDYVSnvnfkISDNGIGINKENQQNLFKPFTQAERSttRKYGGTG 596
Cdd:cd00075     1 LEQVLSNLLDNAL----KYSPPGGTIEISLRQEGDGVVLE-----VEDNGPGIPEEDLERIFERFYRGDKS--REGGGTG 69
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1709973135 597 LGLAICGKLSNLMGGRITLTSELNLGSTFDVDI 629
Cdd:cd00075    70 LGLAIVRRIVEAHGGRITVESEPGGGTTFTVTL 102
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
815-918 2.73e-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: 92.29  E-value: 2.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 815 LVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvhnktAIPIVAV 894
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPP-----DIPVIVL 75
                          90       100
                  ....*....|....*....|....
gi 1709973135 895 TGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd00156    76 TAKADEEDAVRALELGADDYLVKP 99
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
399-629 4.04e-20

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: 92.66  E-value: 4.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 399 QIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQ--DYEAKDLIDTAKTSAENLVFILNDILDINKIEAGKLDIEELTFSI 476
Cdd:TIGR02966 112 QMRRDFVANVSHELRTPLTVLRGYLETLADGPDedPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDM 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 477 SEIVDNVIKvyiPVAIKSD-----ITLNVVESPflphFVKGDAMRVRQILFNLIGNALkfttTTKEKKGVVTLTIDEIEK 551
Cdd:TIGR02966 192 PALLDHLRD---EAEALSQgknhqITFEIDGGV----DVLGDEDELRSAFSNLVSNAI----KYTPEGGTITVRWRRDGG 260
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709973135 552 ndyvsNVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDI 629
Cdd:TIGR02966 261 -----GAEFSVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFIF 333
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
410-630 2.56e-19

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 93.11  E-value: 2.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 410 HELRTPMNAVIGSLDLLQSTKQDyeakdlidtaKTSAENLVFILNDILDINKIeagkldIEELTF------------SIS 477
Cdd:PRK11360  399 HEIRNPLTAIRGYVQIWRQQTSD----------PPSQEYLSVVLREVDRLNKV------IDQLLEfsrpresqwqpvSLN 462
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 478 EIVDNVIKVYIPVAIKSDITLNVVESPFLPhFVKGDAMRVRQILFNLIGNALKFTTTTkekkGVVTLTIdEIEKNDyvsN 557
Cdd:PRK11360  463 ALVEEVLQLFQTAGVQARVDFETELDNELP-PIWADPELLKQVLLNILINAVQAISAR----GKIRIRT-WQYSDG---Q 533
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709973135 558 VNFKISDNGIGINKENQQNLFKPFTqaerstTRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIP 630
Cdd:PRK11360  534 VAVSIEDNGCGIDPELLKKIFDPFF------TTKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLP 600
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
815-918 3.99e-19

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: 83.23  E-value: 3.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 815 LVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhNKTAIPIVAV 894
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLRE-----KGSDIPIIML 75
                          90       100
                  ....*....|....*....|....*.
gi 1709973135 895 TgaAMTGDSQ--HCYDSGMNDFVSKP 918
Cdd:cd17574    76 T--AKDEEEDkvLGLELGADDYITKP 99
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
154-630 4.65e-19

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: 91.72  E-value: 4.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 154 TEQQLTWKMFINAIYIEDQLLFSNNLKTHINSLTPLNFEFRMLLENEIHWFSIKGETFFNDNQPIcTMGTLSDCSHRKKI 233
Cdd:COG5805    70 TSEEIIGKTIFDFLEKEYHYRVKTRIERLQKGYDVVMIEQIYCKDGELIYVEVKLFPIYNQNGQA-AILALRDITKKKKI 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 234 -------VHELNNAIE-SNNIAMEISKVGTW-YAelnlhNDWVWswdlltrQMFGFEDKaPGIDDfdKWATCLHPDDEMR 304
Cdd:COG5805   149 eeilqeqEERLQTLIEnSPDLICVIDTDGRIlFI-----NESIE-------RLFGAPRE-ELIGK--NLLELLHPCDKEE 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 305 VTSTLLNSLETGKIFSESFRAVLANGKTRYFIGRGRVRQNENNENYRIDGIFFDetpiqSTQRKlknlnlkleervnert 384
Cdd:COG5805   214 FKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRD-----ITEKK---------------- 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 385 lELEQAKIKAEKASqIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEakDLIDTAKTSAENLVFILNDILDINKIEA 464
Cdd:COG5805   273 -EAEELMARSEKLS-IAGQLAAGIAHEIRNPLTSIKGFLQLLQPGIEDKE--EYFDIMLSELDRIESIISEFLALAKPQA 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 465 GKLDieelTFSISEIVDNVIKVYIPVAIKSDITLNVVESPFLPhFVKGDAMRVRQILFNLIGNALKFTTTTKekkgvvTL 544
Cdd:COG5805   349 VNKE----KENINELIQDVVTLLETEAILHNIQIRLELLDEDP-FIYCDENQIKQVFINLIKNAIEAMPNGG------TI 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 545 TIDEIEKNDYVSnvnFKISDNGIGINKENQQNLFKPFTqaerstTRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGST 624
Cdd:COG5805   418 TIHTEEEDNSVI---IRVIDEGIGIPEERLKKLGEPFF------TTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTT 488

                  ....*.
gi 1709973135 625 FDVDIP 630
Cdd:COG5805   489 FTITLP 494
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
376-630 6.60e-19

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


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 90.31  E-value: 6.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 376 LEERVNERtLELEQAKIKAEKAsQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTK-QDYEAKDLIDTAKTSAENLVFILN 454
Cdd:COG5806   178 LIENLIEN-ILLRKELQRAEKL-EVVSELAASIAHEVRNPLTVVRGFIQLLQEPElSDEKRKQYIRIALEELDRAEAIIT 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 455 DILDINKIEAGKLDIeeltFSISEIVDNVIKVYIPVAIKSDITLNV-VESPFlphFVKGDAMRVRQILFNLIGNALKFTT 533
Cdd:COG5806   256 DYLTFAKPQPEKLEK----IDVSEELEHVIDVLSPYANMNNVEIQTeLEPGL---YIEGDRQKLQQCLINIIKNGIEAMP 328
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 534 TTkekkGVVTLTIdEIEKNDYVsnvnFKISDNGIGINKENQQNLFKPFTqaerSTTRKygGTGLGLAICGKLSNLMGGRI 613
Cdd:COG5806   329 NG----GTLTIDV-SIDKNKVI----ISIKDTGVGMTKEQLERLGEPYF----STKEK--GTGLGTMVSYRIIEAMNGTI 393
                         250
                  ....*....|....*..
gi 1709973135 614 TLTSELNLGSTFDVDIP 630
Cdd:COG5806   394 RVESEVGKGTTFTITLP 410
PRK09303 PRK09303
histidine kinase;
374-634 5.17e-18

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 86.93  E-value: 5.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 374 LKLEERVnertLELEQAKIKAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEAKD-------LIDTAKTSA 446
Cdd:PRK09303  128 LQLSDEL----FVLRQENETLLEQLKFKDRVLAMLAHDLRTPLTAASLALETLELGQIDEDTELkpalieqLQDQARRQL 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 447 ENLVFILNDILdinkiEAGKLDIEELTF--------SIS-EIVDNVIKVYI--PVAIKSDITLNvvespfLPHfVKGDAM 515
Cdd:PRK09303  204 EEIERLITDLL-----EVGRTRWEALRFnpqkldlgSLCqEVILELEKRWLakSLEIQTDIPSD------LPS-VYADQE 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 516 RVRQILFNLIGNALkfttTTKEKKGVVTLTIdeIEKNDyvSNVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKygGT 595
Cdd:PRK09303  272 RIRQVLLNLLDNAI----KYTPEGGTITLSM--LHRTT--QKVQVSICDTGPGIPEEEQERIFEDRVRLPRDEGTE--GY 341
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1709973135 596 GLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIPFWKS 634
Cdd:PRK09303  342 GIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTLPVYRG 380
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
814-919 1.08e-17

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: 79.08  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDG--KIKWQSGDykLIITDCHMPIMDGYEMTRGIRELEAVhnkTAIPI 891
Cdd:cd17538     2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEAlaLAEEELPD--LILLDVMMPGMDGFEVCRRLKEDPET---RHIPV 76
                          90       100
                  ....*....|....*....|....*...
gi 1709973135 892 VAVTGAAMTGDSQHCYDSGMNDFVSKPI 919
Cdd:cd17538    77 IMITALDDREDRIRGLEAGADDFLSKPI 104
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
814-926 2.51e-17

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: 78.64  E-value: 2.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYhCDVADNGD--DGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvhnKTAIPI 891
Cdd:cd17551     3 ILIVDDNPTNLLLLEALLRSAGY-LEVVSFTDprEALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPG---LEDVPI 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1709973135 892 VAVTGaamTGDSQHCY---DSGMNDFVSKPIQQSDLRT 926
Cdd:cd17551    79 VMITA---DTDREVRLralEAGATDFLTKPFDPVELLA 113
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
814-931 2.70e-17

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 79.24  E-value: 2.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYH--CDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhNKTAIPI 891
Cdd:COG4565     6 VLIVEDDPMVAELLRRYLERLPGFevVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRA-----RGPDVDV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1709973135 892 VAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTILKKW 931
Cdd:COG4565    81 IVITAARDPETVREALRAGVVDYLIKPFTFERLREALERY 120
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
401-465 7.32e-17

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 75.68  E-value: 7.32e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709973135  401 KTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEAKDLIDTAKTSAENLVFILNDILDINKIEAG 465
Cdd:smart00388   2 KREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
401-465 9.15e-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: 75.33  E-value: 9.15e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709973135 401 KTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEAKDLIDTAKTSAENLVFILNDILDINKIEAG 465
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
814-930 1.03e-16

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: 83.47  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvhnktAIPIVA 893
Cdd:COG2204     5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDP-----DLPVIL 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTILKK 930
Cdd:COG2204    80 LTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVER 116
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
380-696 7.13e-16

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 82.67  E-value: 7.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 380 VNERtleLEQAKIKAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEAKDLIDTAKTSAENLVFILNDILDI 459
Cdd:PRK10618  432 VNKK---LQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLL 508
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 460 NKIEAGKLDIEELTFSISEIVDNVIKVYIPVAIKSDITL-NVVESPFLPHFVkGDAMRVRQILFNLIGNALkftttTKEK 538
Cdd:PRK10618  509 NMLETQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLlIHNHLKAEQLRI-GDRDALRKILLLLLNYAI-----TTTA 582
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 539 KGVVTLTIDeiEKNDYVSNVNFKISDNGIGINKENQQNLFKPF---TQAERsttrkYG-GTGLGLAICGKLSNLMGGRIT 614
Cdd:PRK10618  583 YGKITLEVD--QDESSPDRLTIRILDTGAGVSIKELDNLHFPFlnqTQGDR-----YGkASGLTFFLCNQLCRKLGGHLT 655
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 615 LTSELNLGSTFDVDIPFwKSQETRAMDITE--LDSIHVKMvsfTIQDNEREMRIKNHLIREGANVtsVTPPKDAISPEkS 692
Cdd:PRK10618  656 IKSREGLGTRYSIHLKM-LAADPEVEEEEEklLDGVTVLL---DITSEEVRKIVTRQLENWGATC--ITPDERLISQE-Y 728

                  ....
gi 1709973135 693 DVIL 696
Cdd:PRK10618  729 DIFL 732
PRK10490 PRK10490
sensor protein KdpD; Provisional
388-652 9.27e-16

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 82.01  E-value: 9.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 388 EQAKIKAEKaSQIKTEFLSMMSHELRTPMNAVIG-----SLDLLQS----TKQDYEAKDLIdtakTSAENLVfilNDILD 458
Cdd:PRK10490  652 EQARLASER-EQLRNALLAALSHDLRTPLTVLFGqaeilTLDLASEgsphARQASEIRQQV----LNTTRLV---NNLLD 723
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 459 INKIEAGKLDIEELTFSISEIVDNVIKVYIPVAIKSDITLNVVESPFLPHfvkGDAMRVRQILFNLIGNALKFTTTTkek 538
Cdd:PRK10490  724 MARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGHPINLSLPEPLTLIH---VDGPLFERVLINLLENAVKYAGAQ--- 797
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 539 kgvVTLTIDEIEKNDyvsNVNFKISDNGIGINKENQQNLFKPFTQAERSTTrkYGGTGLGLAICGKLSNLMGGRITLTSE 618
Cdd:PRK10490  798 ---AEIGIDAHVEGE---RLQLDVWDNGPGIPPGQEQLIFDKFARGNKESA--IPGVGLGLAICRAIVEVHGGTIWAENR 869
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1709973135 619 LNLGSTFDVDIPfwksQETramdITELDSIHVKM 652
Cdd:PRK10490  870 PEGGACFRVTLP----LET----PPELEEFHEDM 895
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
814-928 1.63e-15

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: 73.26  E-value: 1.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVHNktaIPIVA 893
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLAN---TPAIA 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTIL 928
Cdd:cd17580    78 LTGYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
379-715 1.79e-15

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 81.26  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 379 RVNERTLELEQAKIKAEKASQIKTeFLSMMSHELRTPMNAVIGSLDLLQST-KQDYEAKDLIDTAKTSAENLVFILNDIL 457
Cdd:PRK13837  429 RLETERDALERRLEHARRLEAVGT-LASGIAHNFNNILGAILGYAEMALNKlARHSRAARYIDEIISAGARARLIIDQIL 507
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 458 DINKieagKLDIEELTFSISEIVDNVIKVyIPVAIKSDITLNVVESPfLPHFVKGDAMRVRQILFNLIGNAlkftTTTKE 537
Cdd:PRK13837  508 AFGR----KGERNTKPFDLSELVTEIAPL-LRVSLPPGVELDFDQDQ-EPAVVEGNPAELQQVLMNLCSNA----AQAMD 577
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 538 KKGVVTLTIDEIE--KNDYVSN--------VNFKISDNGIGINKENQQNLFKPFTqaersTTRKyGGTGLGLAICGKLSN 607
Cdd:PRK13837  578 GAGRVDISLSRAKlrAPKVLSHgvlppgryVLLRVSDTGAGIDEAVLPHIFEPFF-----TTRA-GGTGLGLATVHGIVS 651
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 608 LMGGRITLTSELNLGSTFDVDIPFWKSQETRAMDITELDSIHV---KMVSFTIQDNEREMRIKNHLIREGAN-VTSVTPP 683
Cdd:PRK13837  652 AHAGYIDVQSTVGRGTRFDVYLPPSSKVPVAPQAFFGPGPLPRgrgETVLLVEPDDATLERYEEKLAALGYEpVGFSTLA 731
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1709973135 684 K--DAIS--PEKSDviLIIINDLFKEEERLTALLHD 715
Cdd:PRK13837  732 AaiAWISkgPERFD--LVLVDDRLLDEEQAAAALHA 765
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
814-930 2.13e-15

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: 73.14  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGY-HCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIReleAVHNKTAIPIV 892
Cdd:cd19923     3 VLVVDDFSTMRRIIKNLLKELGFnNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIR---ADGALSHLPVL 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1709973135 893 AVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTILKK 930
Cdd:cd19923    80 MVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEK 117
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
376-630 6.50e-15

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: 78.20  E-value: 6.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 376 LEERVNERTL--ELEQAKI-------KAEKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEA-KDLIDTAKTS 445
Cdd:TIGR01386 207 LDQRLDPSRApaELRELAQsfnamlgRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQVALSQPRTGEEyREVLESNLEE 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 446 AENLVFILNDILDINKIEAGKLDIEELTFSISEIVDNVIKVYIPVAIKSDITLNVVESPFLPhfvkGDAMRVRQILFNLI 525
Cdd:TIGR01386 287 LERLSRMVSDMLFLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEGLVR----GDPQMFRRAISNLL 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 526 GNALkfttTTKEKKGVVTLTIDEIEkndyvSNVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKL 605
Cdd:TIGR01386 363 SNAL----RHTPDGGTITVRIERRS-----DEVRVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSI 433
                         250       260
                  ....*....|....*....|....*
gi 1709973135 606 SNLMGGRITLTSeLNLGSTFDVDIP 630
Cdd:TIGR01386 434 MEAHGGRASAES-PDGKTRFILRFP 457
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
812-918 1.28e-14

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 71.01  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 812 TGILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDG-KIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleaVHNKTAIP 890
Cdd:cd17544     1 IKVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEAlEVLEQHPDIKLVITDYNMPEMDGFELVREIRK---KYSRDQLA 77
                          90       100
                  ....*....|....*....|....*...
gi 1709973135 891 IVAVTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd17544    78 IIGISASGDNALSARFIKAGANDFLTKP 105
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
814-930 1.89e-14

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: 70.41  E-value: 1.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVHNktaIPIVA 893
Cdd:cd17562     3 ILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKF---TPILM 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTILKK 930
Cdd:cd17562    80 LTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKK 116
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
814-924 4.28e-14

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: 69.36  E-value: 4.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELeavhnKTAIPIVA 893
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLA-----KVKTPILI 75
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL 924
Cdd:cd17616    76 LSGLADIEDKVKGLGFGADDYMTKPFHKDEL 106
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
814-918 5.50e-14

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: 68.65  E-value: 5.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQL-KNIGYH-CDVADNGDDG--KIKWQSGDykLIITDCHMPIMDGYEMTRGIRELeavhnKTAI 889
Cdd:COG4753     2 VLIVDDEPLIREGLKRILeWEAGFEvVGEAENGEEAleLLEEHKPD--LVITDINMPGMDGLELLEAIREL-----DPDT 74
                          90       100
                  ....*....|....*....|....*....
gi 1709973135 890 PIVAVTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:COG4753    75 KIIILSGYSDFEYAQEAIKLGADDYLLKP 103
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
814-919 7.00e-14

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: 68.31  E-value: 7.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDG--KIKWQSGDykLIITDCHMPIMDGYEMtrgIRELEAVHNKTAIPI 891
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQAlqRAQAEPPD--LILLDVMMPGMDGFEV---CRRLKADPATRHIPV 75
                          90       100
                  ....*....|....*....|....*...
gi 1709973135 892 VAVTGAAMTGDSQHCYDSGMNDFVSKPI 919
Cdd:cd19920    76 IFLTALTDTEDKVKGFELGAVDYITKPF 103
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
300-630 8.19e-14

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 74.50  E-value: 8.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 300 DDEMRVTS------TLLNSLETGKIFSESFRAVLANGKT-RYFIGRGRVrqnennenyridgIFFDETPIQSTQRKLKN- 371
Cdd:COG3290   101 DRDGRITLindaarRLLGLDAIGRPIDEVLAEVLETGERdEEILLNGRV-------------LVVNRVPIRDDGRVVGAv 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 372 LNLKLEERVNERTLELEQAKIKAEKasqiktefLSMMSHELRTPMNAVIGsldLLQsTKQDYEAKDLIDT-AKTSAENLV 450
Cdd:COG3290   168 ATFRDRTELERLEEELEGVKELAEA--------LRAQRHDFRNHLHTISG---LLQ-LGEYDEALEYIDEiSEELQELID 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 451 FILNDILDInkieagkldieeltfsiseIVDNVIKVYIPVAIKSDITLNVVESPFLPHFVKGDAMRVRqILFNLIGNALK 530
Cdd:COG3290   236 SLLSRIGNP-------------------VLAALLLGKAARARERGIDLTIDIDSDLPDLPLSDTDLVT-ILGNLLDNAIE 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 531 FTTTTKEKKGVVTLTIDEiEKNDYVsnvnFKISDNGIGINKENQQNLFKPftqaeRSTTRKYGGTGLGLAICGKLSNLMG 610
Cdd:COG3290   296 AVEKLPEEERRVELSIRD-DGDELV----IEVEDSGPGIPEELLEKIFER-----GFSTKLGEGRGLGLALVKQIVEKYG 365
                         330       340
                  ....*....|....*....|
gi 1709973135 611 GRITLTSELNLGSTFDVDIP 630
Cdd:COG3290   366 GTIEVESEEGEGTVFTVRLP 385
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
814-918 1.72e-13

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: 67.40  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQ---------SGDYKLIITDCHMPIMDGYEMTRGIRELEAVH 884
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLEnlakegndlSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1709973135 885 NktaIPIVAVTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd19924    81 N---IPVILNSSLSGEFSRARGKKVGADAYLAKF 111
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
398-461 2.08e-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: 65.70  E-value: 2.08e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709973135 398 SQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYE-AKDLIDTAKTSAENLVFILNDILDINK 461
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEeQREYLERIREEAERLLRLINDLLDLSR 65
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
517-630 3.33e-13

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: 66.58  E-value: 3.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 517 VRQILFNLIGNALKFTTTTKEKKGVVTLTIDEIEKNDYVSnvnfkisDNGIGINKENQQNLFKPFtqaERSTTR-KYGGT 595
Cdd:cd16921     1 LGQVLTNLLGNAIKFRRPRRPPRIEVGAEDVGEEWTFYVR-------DNGIGIDPEYAEKVFGIF---QRLHSReEYEGT 70
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1709973135 596 GLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIP 630
Cdd:cd16921    71 GVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
814-918 3.65e-13

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: 66.31  E-value: 3.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMtrgIRELEAVHNKTaiPIVA 893
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEV---LRRLRAAGKQT--PVLM 75
                          90       100
                  ....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd19935    76 LTARDSVEDRVKGLDLGADDYLVKP 100
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
395-613 6.48e-13

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 72.17  E-value: 6.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 395 EKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQSTKQDYEAKDLiDTAKTSAENLVFILNDILDINKIEAGKLDIEELTF 474
Cdd:NF012163  234 EKNEQMRRDFMADISHELRTPLAVLRAELEAIQDGIRKFTPESL-DSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASV 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 475 SISEIVDNVIKVYIPVAIKSDITLNvVESPFLPhFVKGDAMRVRQILFNLIGNALkfttTTKEKKGVVTLTIDEIEKndy 554
Cdd:NF012163  313 DLVPLLEVEGGAFRERFASAGLELE-VSLPDSS-LVFGDRDRLMQLFNNLLENSL----RYTDSGGSLHISASQRPK--- 383
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1709973135 555 vsNVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRI 613
Cdd:NF012163  384 --EVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTL 440
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
815-918 8.22e-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: 65.71  E-value: 8.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 815 LVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhNKTAIPIVAV 894
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLRE-----EGIETPVLLL 75
                          90       100
                  ....*....|....*....|....
gi 1709973135 895 TGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd17625    76 TALDAVEDRVKGLDLGADDYLPKP 99
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
814-918 1.30e-12

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: 64.83  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSG-DYKLIITDCHMPIMDGYEMTRGIRELEAvhnktAIPIV 892
Cdd:cd18160     2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGkDIDIVVTDIVMPEMDGIELAREARKIDP-----DVKIL 76
                          90       100
                  ....*....|....*....|....*.
gi 1709973135 893 AVTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd18160    77 FISGGAAAAPELLSDAVGDNATLKKP 102
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
404-630 1.96e-12

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: 71.31  E-value: 1.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 404 FLSMMSHELRTPMNAVIGSLDLLQSTKQDYEAKDLIDTAKTSAENLVFILNDILDINKIEAGKLDIEELTFSISEIVDNV 483
Cdd:TIGR03785 488 MSSRLSHELRTPVAVVRSSLENLELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSEVLSGC 567
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 484 IKVYIPVAIKSDITLNVVESPFLPHfvkGDAMRVRQILFNLIGNALkfttTTKEKKGVVTLTIDEIEKNDYVSnvnfkIS 563
Cdd:TIGR03785 568 MQGYQMTYPPQRFELNIPETPLVMR---GSPELIAQMLDKLVDNAR----EFSPEDGLIEVGLSQNKSHALLT-----VS 635
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709973135 564 DNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRITLTSEL-NLGSTFDVDIP 630
Cdd:TIGR03785 636 NEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRISLP 703
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
814-931 2.41e-12

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: 64.74  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCD--VADNGDDGkIKW--QSGDYK------LIITDCHMPIMDGYEMTRGIRELEAV 883
Cdd:cd17557     2 ILLVEDNPGDAELIQEAFKEAGVPNElhVVRDGEEA-LDFlrGEGEYAdaprpdLILLDLNMPRMDGFEVLREIKADPDL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1709973135 884 HNktaIPIVAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL----RTILKKW 931
Cdd:cd17557    81 RR---IPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFveaiRSLGEYW 129
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
814-918 5.39e-12

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: 63.27  E-value: 5.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIReleavHNKTAIPIVA 893
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWR-----RQGQSLPVLI 75
                          90       100
                  ....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd17624    76 LTARDGVDDRVAGLDAGADDYLVKP 100
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
507-615 6.66e-12

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: 63.19  E-value: 6.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 507 PHFVKGDAMRVRQILFNLIGNALkfttTTKEKKGVVTLTIDEIEkndyvsNVNFKISDNGIGINKENQQNLFKPFTqaeR 586
Cdd:cd16940     4 DIQVQGDALLLFLLLRNLVDNAV----RYSPQGSRVEIKLSADD------GAVIRVEDNGPGIDEEELEALFERFY---R 70
                          90       100
                  ....*....|....*....|....*....
gi 1709973135 587 STTRKYGGTGLGLAICGKLSNLMGGRITL 615
Cdd:cd16940    71 SDGQNYGGSGLGLSIVKRIVELHGGQIFL 99
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
410-630 6.73e-12

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 68.10  E-value: 6.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 410 HELRTPMNAVIGSLD-LLQSTKQDYEA--KDLIDtaktSAENLVFILNDILDINKIEAG--KLDIEELTFsiSEIVDNVI 484
Cdd:NF012226  147 HELRTPITILQGRLQgILDGVFEPDPAlfKSLLN----QVEGLSHLVEDLRTLSLVENQqlRLNYESVDL--KDSIEKVL 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 485 KVYIPVAIKSDIT--LNVVESPflphfVKGDAMRVRQILFNLIGNALkftttTKEKKGVVTLTiDEIEKNDYVsnvnFKI 562
Cdd:NF012226  221 KMFEDRLEQAQLTivLNLTATP-----VFCDRRRIEQVLIALIDNAI-----RYANAGKLKIS-SSVIQDDWI----LQI 285
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709973135 563 SDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRITLTSElNLGSTFDVDIP 630
Cdd:NF012226  286 EDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEYSNS-QGNSVFTIKLP 352
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
267-355 7.19e-12

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: 62.36  E-value: 7.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 267 VWSWDLLTRQMFGFEdkaPG--IDDFDKWATCLHPDDEMRVTSTLLNSLETGKIFSESFRAVLANGKTRYFIGRGRVRQN 344
Cdd:pfam08447   1 IIYWSPRFEEILGYT---PEelLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRD 77
                          90
                  ....*....|.
gi 1709973135 345 ENNENYRIDGI 355
Cdd:pfam08447  78 ENGKPVRVIGV 88
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
814-927 8.00e-12

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: 63.15  E-value: 8.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNG-----------DDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEA 882
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGkraleflgledEEDSSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1709973135 883 VHNktaIPIVAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTI 927
Cdd:cd17581    81 LKE---IPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLADVKRL 122
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
814-928 9.29e-12

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: 62.80  E-value: 9.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDD--GKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVHNKTAipI 891
Cdd:cd19933     3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEEclNLLASAEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPL--I 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1709973135 892 VAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTIL 928
Cdd:cd19933    81 VALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
814-918 1.13e-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: 61.80  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELeavhnkTAIPIVA 893
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREW------SAVPVIV 74
                          90       100
                  ....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd17620    75 LSARDEESDKIAALDAGADDYLTKP 99
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
814-918 1.59e-11

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 61.62  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGkikWQSGDYK---LIITDCHMPIMDGYEMTRGIRELEAVhnkTAIP 890
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEA---LDLLNQYipdLIISDIIMPGVDGYSLLGKLRKNADF---DTIP 74
                          90       100
                  ....*....|....*....|....*...
gi 1709973135 891 IVAVTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd19927    75 VIFLTAKGMTSDRIKGYNAGCDGYLSKP 102
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
814-866 1.64e-11

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: 59.89  E-value: 1.64e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1709973135  814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMP 866
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
501-627 1.85e-11

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: 62.15  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 501 VESPFLPHFVKGDAMRVRQILFNLIGNALKFTTTTKekkgVVTLTIDEIEKNDYVSnvnfkISDNGIGINKENQQNLFKP 580
Cdd:cd16947     5 INIPDRPIYANANTEALQRILKNLISNAIKYGSDGK----FLGMTLREDEKHVYID-----IWDKGKGISETEKDHVFER 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1709973135 581 FTQAERSTTRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDV 627
Cdd:cd16947    76 LYTLEDSRNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTV 122
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
395-614 3.76e-11

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 66.58  E-value: 3.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 395 EKASQIKTEFLSMMSHELRTPMNAVIGSLDLLQS--TKQDYEAkdlIDTAKTSAENLVFILNDILDINKIEAGKLDIEEL 472
Cdd:PRK10549  234 EKNEQMRRDFMADISHELRTPLAVLRGELEAIQDgvRKFTPES---VASLQAEVGTLTKLVDDLHQLSLSDEGALAYRKT 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 473 TFSISEIVDNVIKVYIPVAIKSDITLNVVESPFLPHFvkGDAMRVRQILFNLIGNALKFTTTTKekkgvvTLTIDEIEKN 552
Cdd:PRK10549  311 PVDLVPLLEVAGGAFRERFASRGLTLQLSLPDSATVF--GDPDRLMQLFNNLLENSLRYTDSGG------SLHISAEQRD 382
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709973135 553 DYVSnVNFKisDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRIT 614
Cdd:PRK10549  383 KTLR-LTFA--DSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRII 441
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
513-630 3.86e-11

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: 60.97  E-value: 3.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 513 DAMRVRQILFNLIGNALKFTTTTkekkGVVTLTIDEIEKNDYVsnvnFKISDNGIGINKENQQNLFKPFTQAERSTTRKY 592
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDG----GRIRCILEKFRLNRFL----LTVSDSGPGIPPNLREEIFERFRQGDGSSTRAH 72
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1709973135 593 GGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIP 630
Cdd:cd16925    73 GGTGLGLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
814-924 4.08e-11

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: 60.76  E-value: 4.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvhnktAIPIVA 893
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGR-----ATPVLI 75
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL 924
Cdd:cd19934    76 LTARDSWQDKVEGLDAGADDYLTKPFHIEEL 106
PRK11517 PRK11517
DNA-binding response regulator HprR;
814-934 6.83e-11

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 62.99  E-value: 6.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVhnktaiPIVA 893
Cdd:PRK11517    3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT------PVIC 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL----RTILKKWYPH 934
Cdd:PRK11517   77 LTARDSVDDRVRGLDSGANDYLVKPFSFSELlarvRAQLRQHHAL 121
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
513-613 7.88e-11

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: 59.78  E-value: 7.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 513 DAMRVRQILFNLIGNALKFTTTTkekkGVVTLTIDEIEKNdyvsnVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKY 592
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTG----GKLRIRAAQTPQE-----VRLDVEDSAPGVSDDQLARLFERFYRVESSRNRAS 71
                          90       100
                  ....*....|....*....|.
gi 1709973135 593 GGTGLGLAICGKLSNLMGGRI 613
Cdd:cd16946    72 GGSGLGLAICHNIALAHGGTI 92
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
814-928 8.06e-11

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: 59.91  E-value: 8.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvhnktAIPIVA 893
Cdd:cd17555     3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESP-----DTPVIV 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQqsDLRTIL 928
Cdd:cd17555    78 VSGAGVMSDAVEALRLGAWDYLTKPIE--DLAVLE 110
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
517-615 9.71e-11

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: 59.38  E-value: 9.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 517 VRQILFNLIGNALKFTTTtkekkgvvtltidEIEKNDYVSN--VNFKISDNGIGINKENQQNLFKPFTQAERSttRKYGG 594
Cdd:cd16950     1 LKRVLSNLVDNALRYGGG-------------WVEVSSDGEGnrTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSG 65
                          90       100
                  ....*....|....*....|.
gi 1709973135 595 TGLGLAICGKLSNLMGGRITL 615
Cdd:cd16950    66 TGLGLAIVQRISDAHGGSLTL 86
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
517-630 1.08e-10

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: 59.33  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 517 VRQILFNLIGNALKFTTTTKEKKGVVTLTIdEIEKNDYVSnvnFKISDNGIGINKENQQNLFKPFTqaerstTRKYGGTG 596
Cdd:cd16920     1 IQQVLINLVRNGIEAMSEGGCERRELTIRT-SPADDRAVT---ISVKDTGPGIAEEVAGQLFDPFY------TTKSEGLG 70
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1709973135 597 LGLAICGKLSNLMGGRITLTSELNLGSTFDVDIP 630
Cdd:cd16920    71 MGLSICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
515-630 1.12e-10

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: 59.36  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 515 MRVRQILFNLIGNALKFTTttkekkGVVTLTIDeieKNDYVSNVNFKISDNGIGINKENQQNLFKPFTqaersTTRKYG- 593
Cdd:cd16943     2 SQLNQVLLNLLVNAAQAME------GRGRITIR---TWAHVDQVLIEVEDTGSGIDPEILGRIFDPFF-----TTKPVGe 67
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1709973135 594 GTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIP 630
Cdd:cd16943    68 GTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILP 104
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
372-630 1.85e-10

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 64.26  E-value: 1.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 372 LNLKLEervNERTLELE-------QAKIKAEKASQIKT------EFLSMMSHELRTPMNAVIGSLDLLQstKQDYEA--- 435
Cdd:PRK11006  165 LTLVLN---NGRHLEIRvmpytegQLLMVARDVTQMHQlegarrNFFANVSHELRTPLTVLQGYLEMMQ--DQPLEGalr 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 436 KDLIDTAKTSAENLVFILNDILDINKIEAGKldieelTFSISEIVDnvikvyIPVAI-------------KSDITLNVVE 502
Cdd:PRK11006  240 EKALHTMREQTQRMEGLVKQLLTLSKIEAAP------TIDLNEKVD------VPMMLrvlereaqtlsqgKHTITFEVDN 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 503 SpfLPhfVKGDAMRVRQILFNLIGNAlkfttttkekkgvVTLTID----EIEKNDYVSNVNFKISDNGIGINKENQQNLF 578
Cdd:PRK11006  308 S--LK--VFGNEDQLRSAISNLVYNA-------------VNHTPEgthiTVRWQRVPQGAEFSVEDNGPGIAPEHIPRLT 370
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1709973135 579 KPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIP 630
Cdd:PRK11006  371 ERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLP 422
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
513-630 1.97e-10

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: 58.70  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 513 DAMRVRQILFNLIGNALKFTTTTKEKKGVVTLTIdeieKNDYVSNVNFKISDNGIGINKENQQNLFKPFTqaersTTRKy 592
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEGRPSDVGEVRIRV----EADQDGRIVLIVCDNGKGFPREMRHRATEPYV-----TTRP- 70
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1709973135 593 GGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIP 630
Cdd:cd16944    71 KGTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
814-924 2.09e-10

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: 58.88  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVHNktaIPIVA 893
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKD---IPVIL 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL 924
Cdd:cd17598    78 LTTLSDPRDVIRGLECGADNFITKPYDEKYL 108
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
378-630 2.72e-10

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 63.65  E-value: 2.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 378 ERVNERTLELEQAKIKAEKASQIKTeFLSMMSHELRTPMNAVIGSLDLL-QSTKQDYEAKDLIDTAKTSAENLVFILNDI 456
Cdd:PRK10364  215 RRYLRSRQLLQDEMKRKEKLVALGH-LAAGVAHEIRNPLSSIKGLAKYFaERAPAGGEAHQLAQVMAKEADRLNRVVSEL 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 457 LDINKIEagkldieELTFS---ISEIVDNVIKVYIPVAIKSDITLNVVESPFLPhFVKGDAMRVRQILFNLIGNALKFTT 533
Cdd:PRK10364  294 LELVKPT-------HLALQavdLNDLINHSLQLVSQDANSREIQLRFTANDTLP-EIQADPDRLTQVLLNLYLNAIQAIG 365
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 534 TTkekkGVVTLTIDEIEKNdyvsnVNFKISDNGIGINKENQQNLFKPFTqaerstTRKYGGTGLGLAICGKLSNLMGGRI 613
Cdd:PRK10364  366 QH----GVISVTASESGAG-----VKISVTDSGKGIAADQLEAIFTPYF------TTKAEGTGLGLAVVHNIVEQHGGTI 430
                         250
                  ....*....|....*..
gi 1709973135 614 TLTSELNLGSTFDVDIP 630
Cdd:PRK10364  431 QVASQEGKGATFTLWLP 447
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
361-630 3.48e-10

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 63.64  E-value: 3.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 361 PIQSTQRKLKNLNLK-LEERVNERT--LELEQAKI-------KAEKASQIKTEFLSMMSHELRTPM-NAVIGSLDLLQST 429
Cdd:PRK09835  212 PIRSVSRQIQNITSKdLDVRLDPQTvpIELEQLVLsfnhmieRIEDVFTRQSNFSADIAHEIRTPItNLITQTEIALSQS 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 430 KQDYEAKDLIDTAKTSAENLVFILNDILDINKIEAGKLDIEELTFSISEIVDNVIKVYIPVAIKSDITLNVVESPflpHF 509
Cdd:PRK09835  292 RSQKELEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPEKKMLDLADEVGKVFDFFEAWAEERGVELRFVGDP---CQ 368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 510 VKGDAMRVRQILFNLIGNALKFTTTTKEkkgvVTLTIDEIEkndyvSNVNFKISDNGIGINKENQQNLFKPFTQAERSTT 589
Cdd:PRK09835  369 VAGDPLMLRRAISNLLSNALRYTPAGEA----ITVRCQEVD-----HQVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQ 439
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1709973135 590 RKYGGTGLGLAICGKLSNLMGGRITLTSELNlGSTFDVDIP 630
Cdd:PRK09835  440 RKGEGSGIGLAIVKSIVVAHKGTVAVTSDAR-GTRFVISLP 479
PRK10610 PRK10610
chemotaxis protein CheY;
815-930 4.39e-10

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 58.45  E-value: 4.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 815 LVVEDNPMNQKLITMQLKNIGYH-CDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVhnkTAIPIVA 893
Cdd:PRK10610    9 LVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAM---SALPVLM 85
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTILKK 930
Cdd:PRK10610   86 VTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNK 122
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
814-896 4.61e-10

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: 57.62  E-value: 4.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELeavhnKTAIPIVA 893
Cdd:cd17554     3 ILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREK-----KPDLPVII 77

                  ...
gi 1709973135 894 VTG 896
Cdd:cd17554    78 CTA 80
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
814-928 6.83e-10

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: 59.59  E-value: 6.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYH-CDVADNGDD--GKIKWQSGDykLIITDCHMPIMDGYEMTRGIREleavhnKTAIP 890
Cdd:COG3707     6 VLVVDDEPLRRADLREGLREAGYEvVAEAADGEDavELVRELKPD--LVIVDIDMPDRDGLEAARQISE------ERPAP 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1709973135 891 IVAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTIL 928
Cdd:COG3707    78 VILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPAL 115
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
405-601 7.04e-10

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 62.26  E-value: 7.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 405 LSMMSHELRTPMNAVIGSLDLLqsTKQDYEAKDL--IDTaktSAENLVFILNDILDINKIEAgKLDIEELTFSISEIVDN 482
Cdd:PRK09470  247 LSDISHELRTPLTRLQLATALL--RRRQGESKELerIET---EAQRLDSMINDLLVLSRNQQ-KNHLERETFKANSLWSE 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 483 VIKVYIPVAIKSDITLNVVESPfLPHFVKGDAMRVRQILFNLIGNALKFTTTTKekkgVVTLTIDEiekndyvSNVNFKI 562
Cdd:PRK09470  321 VLEDAKFEAEQMGKSLTVSAPP-GPWPINGNPNALASALENIVRNALRYSHTKI----EVAFSVDK-------DGLTITV 388
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1709973135 563 SDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAI 601
Cdd:PRK09470  389 DDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAI 427
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
380-622 1.10e-09

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 62.01  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 380 VNERTLELEQ---AKIKAEKASQ------IKTEFL-----SMMS--HELRTP---MNAVIGSLDLLQSTKQDYEAKDLID 440
Cdd:COG4192   396 AIEKTQELETeieERKRIEKNLRqtqdelIQAAKMavvgqTMTSlaHELNQPlnaMSMYLFSAKKALEQENYAQLPTSLD 475
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 441 TAKTSAENLVFILNDILDINKIEAGKL---DIEELTFSISEIVDNVIKvyipvaiKSDITLNVVEspflPHFVKGDAMRV 517
Cdd:COG4192   476 KIEGLIERMDKIIKSLRQFSRKSDTPLqpvDLRQVIEQAWELVESRAK-------PQQITLHIPD----DLMVQGDQVLL 544
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 518 RQILFNLIGNALKFTTTTKekkgVVTLTIDEIEKNDYVSnvnfkISDNGIGINkeNQQNLFKPFTqaerstTRKYGGTGL 597
Cdd:COG4192   545 EQVLVNLLVNALDAVATQP----QISVDLLSNAENLRVA-----ISDNGNGWP--LVDKLFTPFT------TTKEVGLGL 607
                         250       260
                  ....*....|....*....|....*
gi 1709973135 598 GLAICGKLSNLMGGRITLTSELNLG 622
Cdd:COG4192   608 GLSICRSIMQQFGGDLYLASTLERG 632
PLN03029 PLN03029
type-a response regulator protein; Provisional
814-924 2.73e-09

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 58.51  E-value: 2.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNG-----------DDGKI---------KWQSGDYKLIITDCHMPIMDGYEM 873
Cdd:PLN03029   11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGskalkflglheDDRSNpdtpsvspnSHQEVEVNLIITDYCMPGMTGYDL 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1709973135 874 TRGIRELEAVHNktaIPIVAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL 924
Cdd:PLN03029   91 LKKIKESSSLRN---IPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDL 138
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
517-629 3.02e-09

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: 55.16  E-value: 3.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 517 VRQILFNLIGNALKFTTTTKEKKGVVTLtidEIEKNDYVSNVnfkiSDNGIGINKENQQNLFKPFTqaersTTRKYG-GT 595
Cdd:cd16976     1 IQQVLMNLLQNALDAMGKVENPRIRIAA---RRLGGRLVLVV----RDNGPGIAEEHLSRVFDPFF-----TTKPVGkGT 68
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1709973135 596 GLGLAICGKLSNLMGGRITLTSELNLGSTFDVDI 629
Cdd:cd16976    69 GLGLSISYGIVEEHGGRLSVANEEGAGARFTFDL 102
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
814-924 3.46e-09

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 55.55  E-value: 3.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhnKTAIPIVA 893
Cdd:cd17626     3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA------ESGVPIVM 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL 924
Cdd:cd17626    77 LTAKSDTVDVVLGLESGADDYVAKPFKPKEL 107
PRK10643 PRK10643
two-component system response regulator PmrA;
814-924 6.84e-09

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 56.97  E-value: 6.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhNKTAIPIVA 893
Cdd:PRK10643    3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQ-----KKYTLPVLI 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL 924
Cdd:PRK10643   78 LTARDTLEDRVAGLDVGADDYLVKPFALEEL 108
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
556-630 7.43e-09

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: 54.13  E-value: 7.43e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709973135 556 SNVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIP 630
Cdd:cd16952    31 SGARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKHVMSRHDARLLIASELGKGSRFTCLFP 105
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
814-924 7.95e-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: 54.32  E-value: 7.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhnKTAIPIVA 893
Cdd:cd17619     3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELRE------QSEVGIIL 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL 924
Cdd:cd17619    77 VTGRDDEVDRIVGLEIGADDYVTKPFNPREL 107
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
814-929 7.98e-09

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: 54.17  E-value: 7.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDG--KIKWQSGDYKLIITDCHMPIMDGYEMtrgireLEAVHNKTAIPI 891
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEAlsMLRENKDEFDLVITDVHMPDMDGFEF------LELIRLEMDLPV 74
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1709973135 892 VAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTILK 929
Cdd:cd17584    75 IMMSADGSTSTVMKGLAHGACDYLLKPVSIEDLKNIWQ 112
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
506-627 8.03e-09

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: 54.77  E-value: 8.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 506 LPHFVKGDAMRVRQILFNLIGNALKFTTTTKEKKGVVTLTIDEIEKNDYVSNVNFKISDNG-------IGINKENQQNLF 578
Cdd:cd16938     1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGGGNITFRVFLEGGSEDRSDRDWGPWRPSMSDEsveirfeVEINDSGSPSIE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1709973135 579 KPFTQAERSttRKYG----GTGLGLAICGKLSNLMGGRITLTSELNLGSTFDV 627
Cdd:cd16938    81 SASMRNSLN--RRYNlselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSL 131
PRK10604 PRK10604
sensor protein RstB; Provisional
409-619 8.94e-09

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 58.85  E-value: 8.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 409 SHELRTPMNAVIGSLDLLqstkqdyeakDLIDTAKTSAENLvfilndilDINKIEA--------GKLDIEELTFSISEI- 479
Cdd:PRK10604  220 AHELRTPLVRLRYRLEMS----------DNLSAAESQALNR--------DIGQLEAlieelltyARLDRPQNELHLSEPd 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 480 --------VDNVIKVYIPVAIKSDItlnvvesPFLPHFVKGDAMRVRQILFNLIGNALKFTTTTKEkkgvVTLTIDEiek 551
Cdd:PRK10604  282 lpawlsthLADIQAVTPEKTVRLDT-------PHQGDYGALDMRLMERVLDNLLNNALRYAHSRVR----VSLLLDG--- 347
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709973135 552 ndyvSNVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRITL-TSEL 619
Cdd:PRK10604  348 ----NQACLIVEDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCdESEL 412
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
814-918 9.24e-09

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: 54.18  E-value: 9.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVhnkTAIPIVA 893
Cdd:cd17618     3 ILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMT---RDIPIIM 79
                          90       100
                  ....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd17618    80 LTARGEEEDKVRGLEAGADDYITKP 104
envZ PRK09467
osmolarity sensor protein; Provisional
407-616 9.32e-09

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 58.77  E-value: 9.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 407 MM---SHELRTPMNAVIGSLDLLqSTKQDYEAKDlidtaktsaenlvfILNDILDINKIEAGKLD----IEELTFS---I 476
Cdd:PRK09467  232 LMagvSHDLRTPLTRIRLATEMM-SEEDGYLAES--------------INKDIEECNAIIEQFIDylrtGQEMPMEmadL 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 477 SEIVDNVIKVYIPvaIKSDITLNVVESPFLphfVKGDAMRVRQILFNLIGNALKFTTttkekkgvvtltiDEIEKNDYVS 556
Cdd:PRK09467  297 NALLGEVIAAESG--YEREIETALQPGPIE---VPMNPIAIKRALANLVVNAARYGN-------------GWIKVSSGTE 358
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709973135 557 N--VNFKISDNGIGINKENQQNLFKPFTQAErsTTRKYGGTGLGLAICGKLSNLMGGRITLT 616
Cdd:PRK09467  359 GkrAWFQVEDDGPGIPPEQLKHLFQPFTRGD--SARGSSGTGLGLAIVKRIVDQHNGKVELG 418
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
520-630 1.04e-08

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: 53.83  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 520 ILFNLIGNALKFTTTTKEKKGVVTLTIdeiekNDYVSNVNFKISDNGIGINKENQQNLFkpftqaERS-TTRKYGGTGLG 598
Cdd:cd16915     4 IVGNLIDNALDALAATGAPNKQVEVFL-----RDEGDDLVIEVRDTGPGIAPELRDKVF------ERGvSTKGQGERGIG 72
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1709973135 599 LAICGKLSNLMGGRITLTSELNLGSTFDVDIP 630
Cdd:cd16915    73 LALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
547-630 1.59e-08

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: 53.54  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 547 DEIEKNDYVSnvnFKISDNGIGINKENQQNLFKPFTqaersTTRKYG-GTGLGLAICGKLSNLMGGRITLTSELNLGSTF 625
Cdd:cd16919    40 RDLIPGNYVC---LEVSDTGSGMPAEVLRRAFEPFF-----TTKEVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTV 111

                  ....*
gi 1709973135 626 DVDIP 630
Cdd:cd16919   112 RIYLP 116
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
814-918 2.10e-08

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: 53.55  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYH--CDVADNGDDG--KIKWQSGDykLIITDCHMPIMDGYEMTRGIREleavhnKTAI 889
Cdd:cd17541     3 VLIVDDSAVMRKLLSRILESDPDIevVGTARDGEEAleKIKELKPD--VITLDIEMPVMDGLEALRRIMA------ERPT 74
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1709973135 890 PIVAVT-----GAAMTGDsqhCYDSGMNDFVSKP 918
Cdd:cd17541    75 PVVMVSslteeGAEITLE---ALELGAVDFIAKP 105
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
815-919 2.59e-08

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: 53.05  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 815 LVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvhnKTAIPIVAV 894
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPK---TSSIPIIML 77
                          90       100
                  ....*....|....*....|....*
gi 1709973135 895 TGAAMTGDSQHCYDSGMNDFVSKPI 919
Cdd:cd19937    78 TAKGEEFDKVLGLELGADDYITKPF 102
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
558-613 3.02e-08

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: 52.33  E-value: 3.02e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1709973135 558 VNFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLAICGKLSNLMGGRI 613
Cdd:cd16949    31 WTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAIEQHGGKI 86
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
521-630 3.13e-08

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: 52.43  E-value: 3.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 521 LFNLIGNALKFTTTTKekkgvvtltidEIEKNDYVSNVNFKISDNGIGINKENQQNLFKPFTQAERSTTRKYGGTGLGLA 600
Cdd:cd16939     5 LDNLLRNALRYAHRTV-----------RIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLA 73
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1709973135 601 ICGKLSNLMGGRITLT-SELNlGSTFDVDIP 630
Cdd:cd16939    74 IVHRVALWHGGHVECDdSELG-GACFRLTWP 103
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
814-934 6.62e-08

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 54.16  E-value: 6.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELeavhNKtAIPIVA 893
Cdd:PRK09836    3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSA----NK-GMPILL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL----RTILKKWYPH 934
Cdd:PRK09836   78 LTALGTIEHRVKGLELGADDYLVKPFAFAELlarvRTLLRRGAAV 122
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
154-383 7.66e-08

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 56.60  E-value: 7.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135  154 TEQQLTWKMFINAiyieDQLLFSNNLKTHINSltplnfeFRMllenEIHWFSIKGETFF----------NDNQPICTMGT 223
Cdd:PRK09776   327 TFQQLTWPEDLNK----DLQQVEKLLSGEINS-------YSM----EKRYYRRDGEVVWallavslvrdTDGTPLYFIAQ 391
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135  224 LSDCSHRKKIVHELNNAIESNNIAMEISKVGTWyaELNLHNDwVWSWDlltRQMFGFEDKAPGID-DFDKWATCLHPDDE 302
Cdd:PRK09776   392 IEDINELKRTEQVNERLMERITLANEAGGIGIW--EWDLKPN-IISWD---KRMFELYEIPPHIKpTWQVWYACLHPEDR 465
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135  303 MRVTSTLLNSLETGKIFSESFRAVLANGkTRYFIGRGRVRQNENNENYRIDGIFFDETPIqstqrklKNLNLKL-EERvn 381
Cdd:PRK09776   466 QRVEKEIRDALQGRSPFKLEFRIVVKDG-VRHIRALANRVLNKDGEVERLLGINMDMTEV-------RQLNEALfQEK-- 535

                   ..
gi 1709973135  382 ER 383
Cdd:PRK09776   536 ER 537
orf27 CHL00148
Ycf27; Reviewed
804-918 1.78e-07

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 53.18  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 804 KQNNHKLKtgILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleav 883
Cdd:CHL00148    1 TMENSKEK--ILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRK---- 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1709973135 884 hnKTAIPIVAVTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:CHL00148   75 --ESDVPIIMLTALGDVSDRITGLELGADDYVVKP 107
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
814-930 2.25e-07

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: 50.41  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDV---ADNGDDG--KIKWQSGDykLIITDCHMPIMDGYEMTRGIRELEAvhnktA 888
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIDWEELGFEVvgeAENGEEAleLIEEHKPD--IVITDIRMPGMDGLELIEKIRELYP-----D 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1709973135 889 IPIVAVTG--------AAMTgdsqhcydSGMNDFVSKPIQQSDLRTILKK 930
Cdd:cd17536    74 IKIIILSGyddfeyaqKAIR--------LGVVDYLLKPVDEEELEEALEK 115
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
814-930 2.82e-07

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: 49.84  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNiGYHCDV--ADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMtrgireLEAVH-NKTAIP 890
Cdd:cd17593     3 VLICDDSSMARKQLARALPA-DWDVEItfAENGEEALEILREGRIDVLFLDLTMPVMDGYEV------LEALPvEQLETK 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1709973135 891 IVAVTG----AAMtgdsQHCYDSGMNDFVSKPIQQSDLRTILKK 930
Cdd:cd17593    76 VIVVSGdvqpEAK----ERVLELGALAFLKKPFDPEKLAQLLEE 115
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
811-934 4.36e-07

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 53.50  E-value: 4.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 811 KTGILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvhnktAIP 890
Cdd:PRK10365    5 NIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNP-----AIP 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1709973135 891 IVAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDLRTILKKWYPH 934
Cdd:PRK10365   80 VLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAH 123
pleD PRK09581
response regulator PleD; Reviewed
814-919 5.84e-07

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 52.98  E-value: 5.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVHNktaIPIVA 893
Cdd:PRK09581    5 ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTH---IPVVM 81
                          90       100
                  ....*....|....*....|....*.
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPI 919
Cdd:PRK09581   82 VTALDDPEDRVRGLEAGADDFLTKPI 107
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
814-930 9.85e-07

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: 48.50  E-value: 9.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvhnktAIPIVA 893
Cdd:cd17615     2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGP-----DVPVLF 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSD----LRTILKK 930
Cdd:cd17615    77 LTAKDSVEDRIAGLTAGGDDYVTKPFSLEEvvarLRALLRR 117
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
814-932 1.08e-06

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: 48.46  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNiGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVHNktaIPIVA 893
Cdd:cd17539     1 VLLVDDRPSSAERIAAMLSS-EHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQ---LPILA 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL----RT-ILKKWY 932
Cdd:cd17539    77 VADPGDRGRLIRALEIGVNDYLVRPIDPNELlarvRTqIRRKRY 120
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
562-630 2.06e-06

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: 47.40  E-value: 2.06e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 562 ISDNGIGINKENQQNLFKPFTqaerstTRKYGGTGLGLAICGKLSNLMGGRITLTSElnLGST-FDVDIP 630
Cdd:cd16918    48 VIDNGPGIPPDLQDTIFYPMV------SGRENGTGLGLAIAQNIVSQHGGVIECDSQ--PGHTvFSVSLP 109
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
814-918 2.10e-06

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: 47.38  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhNKTAIPIVA 893
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRA-----AGNDLPILV 75
                          90       100
                  ....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd17627    76 LTARDSVSDRVAGLDAGADDYLVKP 100
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
814-918 2.52e-06

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: 46.96  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSG-DYKLIITDCHMP-IMDGYEMtrgIRELEAVHNKtaIPI 891
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPgGMNGSQL---AEEARRRRPD--LKV 75
                          90       100
                  ....*....|....*....|....*..
gi 1709973135 892 VAVTGAAMTGDSQHCYDSGMnDFVSKP 918
Cdd:cd18161    76 LLTSGYAENAIEGGDLAPGV-DVLSKP 101
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
814-920 3.27e-06

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: 46.98  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhnKTAIPIVA 893
Cdd:cd19939     2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVRE------HSHVPILM 75
                          90       100
                  ....*....|....*....|....*..
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQ 920
Cdd:cd19939    76 LTARTEEMDRVLGLEMGADDYLCKPFS 102
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
812-931 3.78e-06

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: 46.85  E-value: 3.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 812 TGILVVEDNPMNQKLITMQLKNI-GYH-CDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRelEAVHNKTAI 889
Cdd:cd19925     1 INVLIVEDDPMVAEIHRAYVEQVpGFTvIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELR--AAGHDVDVI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1709973135 890 PIVAVTGAAMTGDSQHCydsGMNDFVSKPIQQSDLRTILKKW 931
Cdd:cd19925    79 VVTAANDVETVREALRL---GVVDYLIKPFTFERLRQRLERY 117
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
814-930 4.38e-06

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: 46.50  E-value: 4.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHC-DVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvhNKTAIPIV 892
Cdd:cd17542     3 VLIVDDAAFMRMMLKDILTKAGYEVvGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDP--NAKVIMCS 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1709973135 893 AVTGAAMTGDsqhCYDSGMNDFVSKPIQQSDLRTILKK 930
Cdd:cd17542    81 AMGQEEMVKE---AIKAGAKDFIVKPFQPERVLEAVEK 115
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
494-639 4.58e-06

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 50.30  E-value: 4.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 494 SDITLNVVESPFLPhfvkgDAMRVRQ------ILFNLIGNALKFTTTTKEkkGVVTLTIdeiekndYVSN--VNFKISDN 565
Cdd:PRK11086  410 LGITLIISEDSQLP-----DSGDEDQvhelitILGNLIENALEAVGGEEG--GEISVSL-------HYRNgwLHCEVSDD 475
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709973135 566 GIGINKENQQNLFkpftqaERSTTRKYGGTGLGLAICGKLSNLMGGRITLTSELNLGSTFDVDIPfWKSQETRA 639
Cdd:PRK11086  476 GPGIAPDEIDAIF------DKGYSTKGSNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP-WDGERSNR 542
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
408-615 5.67e-06

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 49.84  E-value: 5.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 408 MSHELRTPMNAVIGSLDLLQSTKQDYEAKDLIDTAKTSAENLVFILNDILDINKIEAGKlDIEELT-FSISEIVDNVIKV 486
Cdd:PRK11100  263 LTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARLEQRQ-ELEVLEpVALAALLEELVEA 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 487 YIPVAIKSDITLNVVESPFLphfVKGDAMRVRQILFNLIGNALkfttTTKEKKGVVTLTIDeiEKNDYvsnVNFKISDNG 566
Cdd:PRK11100  342 REAQAAAKGITLRLRPDDAR---VLGDPFLLRQALGNLLDNAI----DFSPEGGTITLSAE--VDGEQ---VALSVEDQG 409
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1709973135 567 IGINKENQQNLFkpftqaER--STTRKYGG---TGLGLAICGKLSNLMGGRITL 615
Cdd:PRK11100  410 PGIPDYALPRIF------ERfySLPRPANGrksTGLGLAFVREVARLHGGEVTL 457
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
814-918 6.32e-06

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: 45.82  E-value: 6.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVHNktaIPIVA 893
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKD---TPIIM 77
                          90       100
                  ....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd17602    78 LTGKDGLVDRIRAKMAGASGYLTKP 102
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
814-918 8.33e-06

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: 45.27  E-value: 8.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhnKTAIPIVA 893
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRA------RSNVPVIM 74
                          90       100
                  ....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd17621    75 VTAKDSEIDKVVGLELGADDYVTKP 99
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
814-918 1.03e-05

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: 45.45  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhnKTAIPIVA 893
Cdd:cd19938     2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRR------FSDVPIIM 75
                          90       100
                  ....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd19938    76 VTARVEEIDRLLGLELGADDYICKP 100
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
814-880 1.31e-05

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: 45.09  E-value: 1.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREL 880
Cdd:cd17569     3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRER 69
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
814-924 1.51e-05

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: 45.11  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIReleavhNKTAIPIVA 893
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVR------KTSNVPIIM 74
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL 924
Cdd:cd17614    75 LTAKDSEVDKVLGLELGADDYVTKPFSNREL 105
PRK13557 PRK13557
histidine kinase; Provisional
814-924 1.99e-05

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 48.13  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDG-KIKWQSGDYKLIITDCHMP-IMDGYEMTRGIRELEAvhnktAIPI 891
Cdd:PRK13557  418 ILIVDDRPDVAELARMILEDFGYRTLVASNGREAlEILDSHPEVDLLFTDLIMPgGMNGVMLAREARRRQP-----KIKV 492
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1709973135 892 VAVTGAAMTGDSQHcyDSGMNDF--VSKPIQQSDL 924
Cdd:PRK13557  493 LLTTGYAEASIERT--DAGGSEFdiLNKPYRRAEL 525
PRK13560 PRK13560
hypothetical protein; Provisional
214-502 2.04e-05

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 48.52  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 214 DNQPICTMGTLSDCSHRKKIVHELNNAiesnNIAMEISKV--GTWYAELNlhndwvWSWDLLTRQM--FGFEDKA--PGI 287
Cdd:PRK13560  449 DGNIIGAIALLVDITERKQVEEQLLLA----NLIVENSPLvlFRWKAEEG------WPVELVSKNItqFGYEPDEfiSGK 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 288 DDFdkwATCLHPDDEMRVTSTLLNSLETG-KIFSESFRAVLANGKTRYFIGRGRVRQNENNENYRIDGIFFDetpiqSTQ 366
Cdd:PRK13560  519 RMF---AAIIHPADLEQVAAEVAEFAAQGvDRFEQEYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVID-----ISE 590
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 367 RKLKnlnlklEERVN----ERTLELEQAKIKAEKASQIKTEFLSMMSHELRTP--MNAVIGSLDLLQST----KQDYEAK 436
Cdd:PRK13560  591 RKHA------EEKIKaaltEKEVLLKEIHHRVKNNLQIISSLLDLQAEKLHDEeaKCAFAESQDRICAMalahEKLYQSE 664
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709973135 437 DLIDTAKTS-AENLVFILNDILDIN------KIEAGK--LDIEELT---FSISEIVDNVIKVYIPVAIKSDITLNVVE 502
Cdd:PRK13560  665 DLADIDFLDyIESLTAHLKNSFAIDfgridcKIDADDgcLDIDKAIpcgLIISELLSNALKHAFPDGAAGNIKVEIRE 742
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
545-630 2.39e-05

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: 43.91  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 545 TIDEIEKNDYVSNVNFKISDNGIGINKENQQNLFKPFTQAERSttRKYGGTGLGLAICGKLSNLMGGRITLTSElNLGST 624
Cdd:cd16923    20 TRIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLSIAKAIIELHGGSASAEYD-DNHDL 96

                  ....*.
gi 1709973135 625 FDVDIP 630
Cdd:cd16923    97 FKVRLP 102
PRK10816 PRK10816
two-component system response regulator PhoP;
814-918 2.53e-05

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 46.66  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhNKTAIPIVA 893
Cdd:PRK10816    3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRS-----NDVSLPILV 77
                          90       100
                  ....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:PRK10816   78 LTARESWQDKVEVLSAGADDYVTKP 102
PRK10766 PRK10766
two-component system response regulator TorR;
814-928 2.56e-05

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 46.57  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhnKTAIPIVA 893
Cdd:PRK10766    5 ILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRS------RSTVGIIL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIqqsDLRTIL 928
Cdd:PRK10766   79 VTGRTDSIDRIVGLEMGADDYVTKPL---ELRELL 110
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
404-616 3.69e-05

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 46.88  E-value: 3.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 404 FLSMMSHELRTPMNAVIGSLDLLQSTKQdYEAKDLI---DTAKTSAENL-----------------VFILNDILDINKIE 463
Cdd:PRK10755  140 FTADVAHELRTPLAGIRLHLELLEKQHH-IDVAPLIarlDQMMHTVEQLlqlaragqsfssghyqtVKLLEDVILPSQDE 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 464 agkldIEELtfsiseivdnvikvyipvAIKSDITLNVVESPfLPHFVKGDAMRVRQILFNLIGNAlkftTTTKEKKGVVT 543
Cdd:PRK10755  219 -----LSEM------------------LEQRQQTLLLPESA-ADITVQGDATLLRLLLRNLVENA----HRYSPEGSTIT 270
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709973135 544 LTIDEIEKNdyvsnVNFKISDNGIGINKENQQNLFKPFtqaeRSTTRKYGGTGLGLAICGKLSNLMGGRITLT 616
Cdd:PRK10755  271 IKLSQEDGG-----AVLAVEDEGPGIDESKCGELSKAF----VRMDSRYGGIGLGLSIVSRITQLHHGQFFLQ 334
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
814-918 5.67e-05

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 43.19  E-value: 5.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhNKTAIPIVA 893
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKE-----KHPSIVVIV 75
                          90       100
                  ....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd17573    76 LSDNPKTEQEIEAFKEGADDYIAKP 100
PRK15479 PRK15479
transcriptional regulator TctD;
814-930 5.80e-05

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 45.48  E-value: 5.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhNKTAIPIVA 893
Cdd:PRK15479    3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRK-----RGQTLPVLL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL----RTILKK 930
Cdd:PRK15479   78 LTARSAVADRVKGLNVGADDYLPKPFELEELdarlRALLRR 118
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
512-631 6.57e-05

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: 43.03  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 512 GDAMRVRQILFNLIGNALKFTTTTKEKKGV-VTLTIDEIEKNDYVSNVNFKISDNGIGINKENQQNLFKPftqaERSTTR 590
Cdd:cd16932     2 GDQIRLQQVLADFLLNAVRFTPSPGGWVEIkVSPTKKQIGDGVHVIHLEFRITHPGQGLPEELVQEMFEE----NQWTTQ 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1709973135 591 KyggtGLGLAICGKLSNLMGGRITLTSELNLgSTFDVDIPF 631
Cdd:cd16932    78 E----GLGLSISRKLVKLMNGDVRYLREAGR-SYFLITLEL 113
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
814-930 6.67e-05

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: 43.63  E-value: 6.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNP-----MNQkliTMQLKniGYHCDVADNGDDGkIKWQSGDYK-LIITDCHMPIMDGYEMTRGIRELEAvhnkt 887
Cdd:cd17549     1 VLLVDDDAdvreaLQQ---TLELA--GFRVRAFADAEEA-LAALSPDFPgVVISDIRMPGMDGLELLAQIRELDP----- 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1709973135 888 AIPIVAVTG--------AAMTgdsqhcydSGMNDFVSKPIQQSDLRTILKK 930
Cdd:cd17549    70 DLPVILITGhgdvpmavEAMR--------AGAYDFLEKPFDPERLLDVVRR 112
PRK15115 PRK15115
response regulator GlrR; Provisional
814-924 8.34e-05

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 45.98  E-value: 8.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvhnktAIPIVA 893
Cdd:PRK15115    8 LLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQP-----GMPVII 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL 924
Cdd:PRK15115   83 LTAHGSIPDAVAATQQGVFSFLTKPVDRDAL 113
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
814-929 8.35e-05

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: 42.78  E-value: 8.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYH-CDVADNGDDG--KIKWQSGDykLIITDCHMP-IMDGYEMTRGIREleavhnKTAI 889
Cdd:cd17534     3 ILIVEDEAIIALDLKEILESLGYEvVGIADSGEEAieLAEENKPD--LILMDINLKgDMDGIEAAREIRE------KFDI 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1709973135 890 PIVAVTG---AAMTGDSQHCYDSGmndFVSKPIQQSDLRTILK 929
Cdd:cd17534    75 PVIFLTAysdEETLERAKETNPYG---YLVKPFNERELKAAIE 114
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
814-924 1.28e-04

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: 42.40  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPmnqkLITMQLKNI----GYhcDVADNGDDGKI-----KWQSGDykLIITDCHMPIMDGYEMTRGIRELEAVh 884
Cdd:cd19932     3 VLIAEDEA----LIRMDLREMleeaGY--EVVGEASDGEEavelaKKHKPD--LVIMDVKMPRLDGIEAAKIITSENIA- 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1709973135 885 nktaiPIVAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL 924
Cdd:cd19932    74 -----PIVLLTAYSQQDLVERAKEAGAMAYLVKPFSESDL 108
glnL PRK11073
nitrogen regulation protein NR(II);
504-617 1.32e-04

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 45.07  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 504 PFLPHFVKgDAMRVRQILFNLIGNALKFTTTTKEKKGVVTLTIDE--IEKNDYVSNVNFKISDNGIGINKENQQNLFKPF 581
Cdd:PRK11073  226 PSLPELAH-DPDQIEQVLLNIVRNALQALGPEGGTITLRTRTAFQltLHGERYRLAARIDIEDNGPGIPPHLQDTLFYPM 304
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1709973135 582 TQAersttrKYGGTGLGLAICGKLSNLMGGRITLTS 617
Cdd:PRK11073  305 VSG------REGGTGLGLSIARNLIDQHSGKIEFTS 334
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
812-924 1.71e-04

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 44.02  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 812 TGILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELeavhnkTAIPI 891
Cdd:PRK10529    2 TNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQW------SAIPV 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1709973135 892 VAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL 924
Cdd:PRK10529   76 IVLSARSEESDKIAALDAGADDYLSKPFGIGEL 108
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
814-918 1.91e-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: 41.37  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvhnktAIPIVA 893
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLP-----QTPVAV 75
                          90       100
                  ....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd19926    76 ITAYGSLDTAIEALKAGAFDFLTKP 100
PAS COG2202
PAS domain [Signal transduction mechanisms];
5-237 2.49e-04

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 43.86  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135   5 LRLLHNNTFPMLLIDSKGLIKAVNSALTKFLNVSADDIEQKYLLEYFTPLENN--PKNTITNNSQIYIYASESRNINK-- 80
Cdd:COG2202    14 RALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDefLELLRAALAGGGVWRGELRNRRKdg 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135  81 ---------IMRLNINGNISGqFYWVL--LTKEKNWQHdywEIEKSLSRLTDTISATNFGIWEYNINEKEATFSNKFKEI 149
Cdd:COG2202    94 slfwvelsiSPVRDEDGEITG-FVGIArdITERKRAEE---ALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEEL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 150 IQInTEQQLTWKMFINAIYIEDQLLFSNNLKTHI-NSLTPLNFEFRML-LENEIHWFSIKGETFFNDNQPICTMGTLSDC 227
Cdd:COG2202   170 LGY-SPEELLGKSLLDLLHPEDRERLLELLRRLLeGGRESYELELRLKdGDGRWVWVEASAVPLRDGGEVIGVLGIVRDI 248
                         250
                  ....*....|
gi 1709973135 228 SHRKKIVHEL 237
Cdd:COG2202   249 TERKRAEEAL 258
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
814-924 2.50e-04

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: 41.34  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPmnqkLITMQLKNI-GYHCDV-----ADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAvhnkt 887
Cdd:cd17535     1 VLIVDDHP----LVREGLRRLlESEPDIevvgeAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYP----- 71
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1709973135 888 AIPIVAVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL 924
Cdd:cd17535    72 DLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEEL 108
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
814-930 3.03e-04

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: 41.14  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhnKTAIPIVA 893
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRK------TSQVPVLM 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL----RTILKK 930
Cdd:cd17623    75 LTARGDDIDRILGLELGADDYLPKPFNPRELvariRAILRR 115
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
814-933 3.09e-04

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 43.52  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDgKIKW-QSGDYKLIITDCHMPIMDGYEMTRGIRELeavhnkTAIPIV 892
Cdd:PRK10710   13 ILIVEDEPKLGQLLIDYLQAASYATTLLSHGDE-VLPYvRQTPPDLILLDLMLPGTDGLTLCREIRRF------SDIPIV 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1709973135 893 AVTGAAMTGDSQHCYDSGMNDFVSKPIQQSDL----RTILKKWYP 933
Cdd:PRK10710   86 MVTAKIEEIDRLLGLEIGADDYICKPYSPREVvarvKTILRRCKP 130
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
814-924 3.24e-04

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: 41.21  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhnKTAIPIVA 893
Cdd:cd17622     3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRP------KYQGPILL 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1709973135 894 VTgaAMTGDSQHC--YDSGMNDFVSKPIQQSDL 924
Cdd:cd17622    77 LT--ALDSDIDHIlgLELGADDYVVKPVEPAVL 107
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
159-224 3.82e-04

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: 40.40  E-value: 3.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709973135 159 TWKMFINAiyiEDQLLFSNNLKTHINSLTPLNFEFRMLLEN-EIHWFSIKGETFFNDN-QPICTMGTL 224
Cdd:pfam08447  25 SWLDLVHP---DDRERVREALWEALKGGEPYSGEYRIRRKDgEYRWVEARARPIRDENgKPVRVIGVA 89
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
814-918 4.95e-04

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: 40.61  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNI-GYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMtrgIRELEAvHNKT-AIPI 891
Cdd:cd17552     4 ILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLAT---LKKLQA-NPETqSIPV 79
                          90       100
                  ....*....|....*....|....*..
gi 1709973135 892 VAVTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd17552    80 ILLTAKAQPSDRQRFASLGVAGVIAKP 106
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
814-881 5.18e-04

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: 41.03  E-value: 5.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDV--ADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGI---RELE 881
Cdd:COG2197     4 VLIVDDHPLVREGLRALLEAEPDIEVVgeAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRLltpRERE 76
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
544-625 5.77e-04

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: 40.35  E-value: 5.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 544 LTIDEIEKNDYVSnvnFKISDNGIGINKENQQNLFKP-FTQAERSTTRKygGTGLGLAICGKLSNLMGGRITLTSELNLG 622
Cdd:cd16948    27 IEIYSETNEQGVV---LSIKDFGIGIPEEDLPRVFDKgFTGENGRNFQE--STGMGLYLVKKLCDKLGHKIDVESEVGEG 101

                  ...
gi 1709973135 623 STF 625
Cdd:cd16948   102 TTF 104
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
814-918 6.36e-04

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: 40.34  E-value: 6.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIReleavhNKTAIPIVA 893
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIR------QISNVPIIF 74
                          90       100
                  ....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd18159    75 ISSRDDNMDQVMAINMGGDDYITKP 99
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
814-928 8.19e-04

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: 40.12  E-value: 8.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhnKTAIPIVA 893
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRA------RSDVPIII 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1709973135 894 VTG-AAMTGDSQHCYDSGMNDFVSKPIqqsDLRTIL 928
Cdd:cd17594    76 ISGdRRDEIDRVVGLELGADDYLAKPF---GLRELL 108
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
814-930 1.01e-03

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 41.73  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYH--CDVADNGDDGkIKW-QSGDYKLIITDCHMPIMDGYEMTRGIRELEAvhnktAIP 890
Cdd:COG3279     4 ILIVDDEPLARERLERLLEKYPDLevVGEASNGEEA-LELlEEHKPDLVFLDIQMPGLDGFELARQLRELDP-----PPP 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1709973135 891 IVAVtgaamTGDSQHCYDS-GMN--DFVSKPIQQSDLRTILKK 930
Cdd:COG3279    78 IIFT-----TAYDEYALEAfEVNavDYLLKPIDEERLAKALEK 115
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
15-203 1.10e-03

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 43.12  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135   15 MLLIDSKGLIKAVNSALTKFLNVSADDIEQKYL--LEYFTPLENNPK---NTItnNSQIYIYASESRNINKimrlningn 89
Cdd:PRK09776   296 MALVGTEGQWLQVNKALCQFLGYSQEELRGLTFqqLTWPEDLNKDLQqveKLL--SGEINSYSMEKRYYRR--------- 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135   90 iSGQFYWVLLT----KEKNWQHDY---------------WEIEKSLSRLTDTISATNFGIWEYNINEKEATFSNKFKEII 150
Cdd:PRK09776   365 -DGEVVWALLAvslvRDTDGTPLYfiaqiedinelkrteQVNERLMERITLANEAGGIGIWEWDLKPNIISWDKRMFELY 443
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1709973135  151 QINTEQQLTWKMFINAIYIEDQLLFSNNLKTHINSLTPLNFEFRMLLENEIHW 203
Cdd:PRK09776   444 EIPPHIKPTWQVWYACLHPEDRQRVEKEIRDALQGRSPFKLEFRIVVKDGVRH 496
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
814-879 1.60e-03

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: 39.02  E-value: 1.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRE 879
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKE 66
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
519-630 1.81e-03

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: 39.09  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 519 QILFNLIGNALkftTTTKEKKGVVTLTIDEIEKNDYVSnvnfkISDNGIGINKENQQNLFKPFtQAERSTTRKYG-GTGL 597
Cdd:cd16953     3 QVLRNLIGNAI---SFSPPDTGRITVSAMPTGKMVTIS-----VEDEGPGIPQEKLESIFDRF-YTERPANEAFGqHSGL 73
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1709973135 598 GLAICGKLSNLMGGriTLTSELN------LGSTFDVDIP 630
Cdd:cd16953    74 GLSISRQIIEAHGG--ISVAENHnqpgqvIGARFTVQLP 110
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
814-918 1.84e-03

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 41.40  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYH--CDVADNGDDG--KIKWQSGDykLIITDCHMPIMDGYEMTRGIRELeavhnkTAI 889
Cdd:PRK12555    3 IGIVNDSPLAVEALRRALARDPDHevVWVATDGAQAveRCAAQPPD--VILMDLEMPRMDGVEATRRIMAE------RPC 74
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1709973135 890 PIVAVTgAAMTGDSQHCYDS---GMNDFVSKP 918
Cdd:PRK12555   75 PILIVT-SLTERNASRVFEAmgaGALDAVDTP 105
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
814-924 2.92e-03

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: 38.34  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELeavhnKTAIPIVA 893
Cdd:cd17537     3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLAR-----GSNIPIIF 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1709973135 894 VTG---AAMTGDsqhCYDSGMNDFVSKPIQQSDL 924
Cdd:cd17537    78 ITGhgdVPMAVE---AMKAGAVDFLEKPFRDQVL 108
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
814-879 3.36e-03

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 40.01  E-value: 3.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709973135 814 ILVVEDNPMNQK----LITM--QLKNIGYhcdvADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRE 879
Cdd:PRK10651    9 ILLIDDHPMLRTgvkqLISMapDITVVGE----ASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLRE 76
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
814-884 4.69e-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: 38.19  E-value: 4.69e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGY-HCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVH 884
Cdd:cd17530     3 VLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNA 74
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
814-918 5.42e-03

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: 37.42  E-value: 5.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDGKIKWQSGDYKLIITDCHMPIMDGYEMTRGIREleavhnKTAIPIVA 893
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQ------KSTLPVIF 74
                          90       100
                  ....*....|....*....|....*
gi 1709973135 894 VTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd19936    75 LTSKDDEIDEVFGLRMGADDYITKP 99
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
814-918 5.75e-03

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 37.38  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709973135 814 ILVVEDNPMNQKLITMQLKNIGYHCDVADNGDDG--KIKWQSGDYKLIITDCHMPIMDGYEMTRGIRELEAVHNktaIPI 891
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAwdVLEDEQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKN---IPV 77
                          90       100
                  ....*....|....*....|....*..
gi 1709973135 892 VAVTGAAMTGDSQHCYDSGMNDFVSKP 918
Cdd:cd17582    78 IMMSSQDSVGVVFKCLSKGAADYLVKP 104
 
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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