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Conserved domains on  [gi|261420837|ref|YP_003254519|]
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PAS/PAC sensor protein [Geobacillus sp. Y412MC61]

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List of domain hits

Name Accession Description Interval E-value
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
272-380 3.49e-10

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


:

Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 57.64  E-value: 3.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 272 LGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVslagPDGDKwdwKQLRRVVKRLKSGEVIRVEEEPFRRRD 351
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLI----HPEDR---EELRERLENLLSGGEPVTLEVRLRRKD 73
                         90       100       110
                 ....*....|....*....|....*....|
gi 261420837 352 GVCLPVGYTLAPVL-ENGALAGLVAVLRDM 380
Cdd:cd00130   74 GSVIWVLVSLTPIRdEGGEVIGLLGVVRDI 103
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
449-636 9.55e-47

Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.


:

Pssm-ID: 254114  Cd Length: 192  Bit Score: 163.62  E-value: 9.55e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  449 VSVGIADVSGKGIPAAMLMTLMKFILDRTVHYGTQPHVYLDLLNRFACDYTEPSMFVTMFVGNYNEKTHTFSYACAGHEP 528
Cdd:pfam07228   5 VALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRNLEGERFATAVLAVYDPETGTLEYANAGHPP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  529 ALWYRAKTKQCVPLGAKGCALGLFPQFSFETKSVVLEPGDFVLLYTDGVTEKRTEeaDDDFSVLAAM--VARVNLDQPAP 606
Cdd:pfam07228  85 PLLLRPDGGVVELLESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDP--DGELFGLERLlaLLAERHGLSPE 162
                         170       180       190
                  ....*....|....*....|....*....|
gi 261420837  607 EIVRELYEHIQAYHQYEQKDDQTLLLLRRR 636
Cdd:pfam07228 163 ELLDALLEDLLRLGGGELEDDITLLVLRVR 192
Cytochrome_b_N super family cl00859
Cytochrome b (N-terminus)/b6/petB: Cytochrome b is a subunit of cytochrome bc1, an 11-subunit ...
1-137 8.81e-04

Cytochrome b (N-terminus)/b6/petB: Cytochrome b is a subunit of cytochrome bc1, an 11-subunit mitochondrial respiratory enzyme. Cytochrome b spans the mitochondrial membrane with 8 transmembrane helices (A-H) in eukaryotes. In plants and cyanobacteria, cytochrome b6 is analogous to eukaryote cytochrome b, containing two chains: helices A-D are encoded by the petB gene and helices E-H are encoded by the petD gene in these organisms. Cytochrome b/b6 contains two bound hemes and two ubiquinol/ubiquinone binding sites. The C-terminal portion of cytochrome b is described in a separate CD.


The actual alignment was detected with superfamily member COG3038:

Pssm-ID: 260663  Cd Length: 181  Bit Score: 39.59  E-value: 8.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837   1 MNEYERYGLV--RLHSAMAVLAAGMFVLLLFAaGRLPVSLEFYHS---IHLSLGLAVMVVcwLVAVQGWAVF----PHTL 71
Cdd:COG3038    2 TNTENRYGLVqiALHWLMALLVIGAFALGELM-GFLPRGPGLYFLlyeLHKSIGILVLAL--MVLRLLWRLRnpapPIVP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  72 SLERLMMGALFFSSGLLFSLHVVLSFA------SDGAEAPLFSL------------------AARLTLAWGLLFL----- 122
Cdd:COG3038   79 GPPPWQRKAAKLGHLALYLLMLALPLSgyllstASGRPISVFGLftvpatllpnpaladlakAIHETLAWLLYALiglha 158
                        170       180
                 ....*....|....*....|..
gi 261420837 123 -------FSRRDEVMERRSGQR 137
Cdd:COG3038  159 aaalkhhFIDKDNTLRRMLPRR 180
PAS_9 pfam13426
PAS domain;
274-381 1.17e-13

PAS domain;


:

Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 67.79  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  274 EGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVslagpdGDKWDWKQLRRVVKRLKSGEVIRVEEEpFRRRDGV 353
Cdd:pfam13426   2 DGILVLDPEGRIVYANPAALRLLGYTREELLGKSIRDLF------GPGTDEEAVARLREALRNGGEVEVELE-LRRKDGE 74
                          90       100
                  ....*....|....*....|....*....
gi 261420837  354 CLPVGYTLAPVL-ENGALAGLVAVLRDMT 381
Cdd:pfam13426  75 PFPVLVSASPVRdEDGEVVGIVGILRDIT 103
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
335-636 1.60e-52

Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / Transcription]


:

Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 185.68  E-value: 1.60e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 335 KSGEVIRVEEEPFRRRDGVCLPVGYTLAPVLENGALAGLVAVLRDmtekkekerlerEREQLDFELSLAANMQRSLLqtS 414
Cdd:COG2208   75 VSGKLRALSEEIKHWRGGLPLVAELLVEINRAVGLVSAHNELLLL------------EQNNISAELEVARQIQQNLL--P 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 415 SKVNLPSYIDIGVLSVPARVLSGDFYHFAVHQTS-VSVGIADVSGKGIPAAMLMTLMKFILDRT-VHYGTQPHVYLDLLN 492
Cdd:COG2208  141 KALPLFPGIDIEAILVPASEVGGDYYDFIQLGEKrLRIGIGDVSGKGVPAALLMLMPKLALRLLlESGPLDPADVLETLN 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 493 RFACDYTEPSMFVTMFVGNYNEKTHTFSYACAGHEPALWYRAKTKQCV-PLGAKGCALGLFPQFSFETKSVVLEPGDFVL 571
Cdd:COG2208  221 RVLKQNLEEDMFVTLFLGVYDLDSGELTYSNAGHEPALILSADGEIEVeDLTALGLPIGLLPDYQYEVASLQLEPGDLLV 300
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261420837 572 LYTDGVTEKRTEEADD-DFSVLAAMVARvNLDQPAPEIVRELYEHIQAYHQY-EQKDDQTLLLLRRR 636
Cdd:COG2208  301 LYTDGVTEARNSDGEFfGLERLLKILGR-LLGQPAEEILEAILESLEELQGDqIQDDDITLLVLKVK 366
 
Name Accession Description Interval E-value
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
272-380 3.49e-10

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 57.64  E-value: 3.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 272 LGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVslagPDGDKwdwKQLRRVVKRLKSGEVIRVEEEPFRRRD 351
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLI----HPEDR---EELRERLENLLSGGEPVTLEVRLRRKD 73
                         90       100       110
                 ....*....|....*....|....*....|
gi 261420837 352 GVCLPVGYTLAPVL-ENGALAGLVAVLRDM 380
Cdd:cd00130   74 GSVIWVLVSLTPIRdEGGEVIGLLGVVRDI 103
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
449-636 9.55e-47

Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.


Pssm-ID: 254114  Cd Length: 192  Bit Score: 163.62  E-value: 9.55e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  449 VSVGIADVSGKGIPAAMLMTLMKFILDRTVHYGTQPHVYLDLLNRFACDYTEPSMFVTMFVGNYNEKTHTFSYACAGHEP 528
Cdd:pfam07228   5 VALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRNLEGERFATAVLAVYDPETGTLEYANAGHPP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  529 ALWYRAKTKQCVPLGAKGCALGLFPQFSFETKSVVLEPGDFVLLYTDGVTEKRTEeaDDDFSVLAAM--VARVNLDQPAP 606
Cdd:pfam07228  85 PLLLRPDGGVVELLESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDP--DGELFGLERLlaLLAERHGLSPE 162
                         170       180       190
                  ....*....|....*....|....*....|
gi 261420837  607 EIVRELYEHIQAYHQYEQKDDQTLLLLRRR 636
Cdd:pfam07228 163 ELLDALLEDLLRLGGGELEDDITLLVLRVR 192
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
422-614 1.87e-36

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 135.17  E-value: 1.87e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837   422 YIDIGVLSVPARVLSGDFYHF-AVHQTSVSVGIADVSGKGIPAAMLMTLMKFILDRTVHYGTQPHVYLDLLNRFACDYTE 500
Cdd:smart00331   3 GGLIAQYYEDATQVGGDFYDVvKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRAIYENGE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837   501 PSMFVTMFVGNYNEKTHTFSYACAGHEPALWYRAKTKQCVPLGAKGCALGLFPQFSFETKSVVLEPGDFVLLYTDGVTEK 580
Cdd:smart00331  83 DGMFATLFLALYDFAGGTLSYANAGHSPPYLLRADGGLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTDGLTEA 162
                          170       180       190
                   ....*....|....*....|....*....|....
gi 261420837   581 RTEEADDDfsVLAAmvarvNLDQPAPEIVRELYE 614
Cdd:smart00331 163 RNPERLEE--LLEE-----LLGSPPAEIAQRILE 189
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
263-312 2.59e-08

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 51.63  E-value: 2.59e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 261420837   263 QQLEMMANALGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFV 312
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELI 50
PAS_8 pfam13188
PAS domain;
263-324 7.23e-04

PAS domain;


Pssm-ID: 257556  Cd Length: 66  Bit Score: 38.36  E-value: 7.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261420837  263 QQLEMMANALGEGLMMLNRDGRIVWMNPEAGRLLGLdpEKAKGKPLFSFVSLAGPDGDKWDW 324
Cdd:pfam13188   1 ERLRALFENAPDGILVLDRGGRILYANPAALELLGY--EELLGELLGELLDDLEALAEEALE 60
CybB COG3038
Cytochrome B561 [Energy production and conversion]
1-137 8.81e-04

Cytochrome B561 [Energy production and conversion]


Pssm-ID: 225580  Cd Length: 181  Bit Score: 39.59  E-value: 8.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837   1 MNEYERYGLV--RLHSAMAVLAAGMFVLLLFAaGRLPVSLEFYHS---IHLSLGLAVMVVcwLVAVQGWAVF----PHTL 71
Cdd:COG3038    2 TNTENRYGLVqiALHWLMALLVIGAFALGELM-GFLPRGPGLYFLlyeLHKSIGILVLAL--MVLRLLWRLRnpapPIVP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  72 SLERLMMGALFFSSGLLFSLHVVLSFA------SDGAEAPLFSL------------------AARLTLAWGLLFL----- 122
Cdd:COG3038   79 GPPPWQRKAAKLGHLALYLLMLALPLSgyllstASGRPISVFGLftvpatllpnpaladlakAIHETLAWLLYALiglha 158
                        170       180
                 ....*....|....*....|..
gi 261420837 123 -------FSRRDEVMERRSGQR 137
Cdd:COG3038  159 aaalkhhFIDKDNTLRRMLPRR 180
PTC1 COG0631
Serine/threonine protein phosphatase [Signal transduction mechanisms]
548-636 8.59e-03

Serine/threonine protein phosphatase [Signal transduction mechanisms]


Pssm-ID: 223704  Cd Length: 262  Bit Score: 36.95  E-value: 8.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 548 ALGLFPQFSFETKSVVLEPGDFVLLYTDGVTEKRTEEADDDFsvlaamvarVNLDQPAPEIVRELYEHIQAYHqyeQKDD 627
Cdd:COG0631  176 ALGDFDLLEPDITELELEPGDFLLLCSDGLWDVVSDDEIVDI---------LKNSETPQEAADKLIELALEGG---GPDN 243

                 ....*....
gi 261420837 628 QTLLLLRRR 636
Cdd:COG0631  244 ITVVLVRLN 252
PAS_9 pfam13426
PAS domain;
274-381 1.17e-13

PAS domain;


Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 67.79  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  274 EGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVslagpdGDKWDWKQLRRVVKRLKSGEVIRVEEEpFRRRDGV 353
Cdd:pfam13426   2 DGILVLDPEGRIVYANPAALRLLGYTREELLGKSIRDLF------GPGTDEEAVARLREALRNGGEVEVELE-LRRKDGE 74
                          90       100
                  ....*....|....*....|....*....
gi 261420837  354 CLPVGYTLAPVL-ENGALAGLVAVLRDMT 381
Cdd:pfam13426  75 PFPVLVSASPVRdEDGEVVGIVGILRDIT 103
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
335-636 1.60e-52

Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / Transcription]


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 185.68  E-value: 1.60e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 335 KSGEVIRVEEEPFRRRDGVCLPVGYTLAPVLENGALAGLVAVLRDmtekkekerlerEREQLDFELSLAANMQRSLLqtS 414
Cdd:COG2208   75 VSGKLRALSEEIKHWRGGLPLVAELLVEINRAVGLVSAHNELLLL------------EQNNISAELEVARQIQQNLL--P 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 415 SKVNLPSYIDIGVLSVPARVLSGDFYHFAVHQTS-VSVGIADVSGKGIPAAMLMTLMKFILDRT-VHYGTQPHVYLDLLN 492
Cdd:COG2208  141 KALPLFPGIDIEAILVPASEVGGDYYDFIQLGEKrLRIGIGDVSGKGVPAALLMLMPKLALRLLlESGPLDPADVLETLN 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 493 RFACDYTEPSMFVTMFVGNYNEKTHTFSYACAGHEPALWYRAKTKQCV-PLGAKGCALGLFPQFSFETKSVVLEPGDFVL 571
Cdd:COG2208  221 RVLKQNLEEDMFVTLFLGVYDLDSGELTYSNAGHEPALILSADGEIEVeDLTALGLPIGLLPDYQYEVASLQLEPGDLLV 300
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261420837 572 LYTDGVTEKRTEEADD-DFSVLAAMVARvNLDQPAPEIVRELYEHIQAYHQY-EQKDDQTLLLLRRR 636
Cdd:COG2208  301 LYTDGVTEARNSDGEFfGLERLLKILGR-LLGQPAEEILEAILESLEELQGDqIQDDDITLLVLKVK 366
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
262-381 2.84e-12

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


Pssm-ID: 232884 [Multi-domain]  Cd Length: 124  Bit Score: 64.23  E-value: 2.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  262 EQQLEMMANALGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVSlagPDgdkwDWKQLRRVVKRLKSGE-VI 340
Cdd:TIGR00229   2 EERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIP---EE----DREEVRERIERRLEGErEP 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 261420837  341 RVEEEPFRRRDGVCLPVGYTLAPVLENGALAGLVAVLRDMT 381
Cdd:TIGR00229  75 VSEERRVRRKDGSEIWVEVSVSPIRTNGGELGVVGIVRDIT 115
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
165-381 6.57e-11

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 61.40  E-value: 6.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 165 DGTSRWPFWWKAGEGMIGL-----------LDAGAALLVWRRWRQGSSRSFLYWLLALWLFALGQWLLMLGGGHVLWGQL 233
Cdd:COG2202    6 DRDGRIIYANEAAEELLGYsaeellglllaLHPEDRDRLRELLRRLLAGEELLSEELRLVRKDGEERWVELSAAPLRDGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 234 YEMAGFLYIVRAMYVETVEKpyvELKQHEQQLEMMANALGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVS 313
Cdd:COG2202   86 GRVLGLLGLRDITERKRAEE---ALRESEERLRALLEASPDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSDLIH 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261420837 314 LAGPdgdkwDWKQLRRVVKRLKSGEVIRVEEEPFRRRDG-VCLPVGYTLAPVLENGALAGLVAVLRDMT 381
Cdd:COG2202  163 PEDE-----ERRELELARALAEGRGGPLEIEYRVRRKDGeRVRWILSRISPVRDDGEIVGVVGIARDIT 226
PRK11360 PRK11360
sensory histidine kinase AtoS; Provisional
267-381 1.18e-04

sensory histidine kinase AtoS; Provisional


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 43.80  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 267 MMANAlGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVSLAGPdgdkwdwkqLRRVVKR-LKSGEVIRVEEE 345
Cdd:PRK11360 267 ILESI-ADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTP---------FASPLLDtLEHGTEHVDLEI 336
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 261420837 346 PFRRRDG-VCLPVGYTLapvLEN--GALAGLVAVLRDMT 381
Cdd:PRK11360 337 SFPGRDRtIELSVSTSL---LHNthGEMIGALVIFSDLT 372
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
544-634 2.21e-04

stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane spanning protein with two separable functions. It plays a role in the switch to polar cell division during sporulation. By means of it protein phosphatase activity, located in the C-terminal region, it activates sigma-F. All proteins that score above the trusted cutoff to this model are found in endospore-forming Gram-positive bacteria. Surprisingly, a sequence from the Cyanobacterium-like (and presumably non-spore-forming) photosynthesizer Heliobacillus mobilis is homologous, and scores between the trusted and noise cutoffs [Cellular processes, Sporulation and germination].


Pssm-ID: 234038 [Multi-domain]  Cd Length: 764  Bit Score: 42.76  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  544 AKGCALGLFPQFSFETKSVVLEPGDFVLLYTDGVTEKRTEEADDDFSVLAAMvARVNLDQPApEIVRELYEHIQAYHQYE 623
Cdd:TIGR02865 674 SSNLPIGILDEVDVELVRKKLKNGDLIVMVSDGVLEGEKEVEGKVLWLVRKL-KETNTNDPE-EIAEYLLEKAKELRSGK 751
                          90
                  ....*....|.
gi 261420837  624 QKDDQTLLLLR 634
Cdd:TIGR02865 752 IKDDMTVIVAK 762
 
Name Accession Description Interval E-value
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
272-380 3.49e-10

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 57.64  E-value: 3.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 272 LGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVslagPDGDKwdwKQLRRVVKRLKSGEVIRVEEEPFRRRD 351
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLI----HPEDR---EELRERLENLLSGGEPVTLEVRLRRKD 73
                         90       100       110
                 ....*....|....*....|....*....|
gi 261420837 352 GVCLPVGYTLAPVL-ENGALAGLVAVLRDM 380
Cdd:cd00130   74 GSVIWVLVSLTPIRdEGGEVIGLLGVVRDI 103
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
449-636 9.55e-47

Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.


Pssm-ID: 254114  Cd Length: 192  Bit Score: 163.62  E-value: 9.55e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  449 VSVGIADVSGKGIPAAMLMTLMKFILDRTVHYGTQPHVYLDLLNRFACDYTEPSMFVTMFVGNYNEKTHTFSYACAGHEP 528
Cdd:pfam07228   5 VALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRNLEGERFATAVLAVYDPETGTLEYANAGHPP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  529 ALWYRAKTKQCVPLGAKGCALGLFPQFSFETKSVVLEPGDFVLLYTDGVTEKRTEeaDDDFSVLAAM--VARVNLDQPAP 606
Cdd:pfam07228  85 PLLLRPDGGVVELLESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDP--DGELFGLERLlaLLAERHGLSPE 162
                         170       180       190
                  ....*....|....*....|....*....|
gi 261420837  607 EIVRELYEHIQAYHQYEQKDDQTLLLLRRR 636
Cdd:pfam07228 163 ELLDALLEDLLRLGGGELEDDITLLVLRVR 192
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
422-614 1.87e-36

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 135.17  E-value: 1.87e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837   422 YIDIGVLSVPARVLSGDFYHF-AVHQTSVSVGIADVSGKGIPAAMLMTLMKFILDRTVHYGTQPHVYLDLLNRFACDYTE 500
Cdd:smart00331   3 GGLIAQYYEDATQVGGDFYDVvKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRAIYENGE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837   501 PSMFVTMFVGNYNEKTHTFSYACAGHEPALWYRAKTKQCVPLGAKGCALGLFPQFSFETKSVVLEPGDFVLLYTDGVTEK 580
Cdd:smart00331  83 DGMFATLFLALYDFAGGTLSYANAGHSPPYLLRADGGLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTDGLTEA 162
                          170       180       190
                   ....*....|....*....|....*....|....
gi 261420837   581 RTEEADDDfsVLAAmvarvNLDQPAPEIVRELYE 614
Cdd:smart00331 163 RNPERLEE--LLEE-----LLGSPPAEIAQRILE 189
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
263-312 2.59e-08

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 51.63  E-value: 2.59e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 261420837   263 QQLEMMANALGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFV 312
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELI 50
PAS_8 pfam13188
PAS domain;
263-324 7.23e-04

PAS domain;


Pssm-ID: 257556  Cd Length: 66  Bit Score: 38.36  E-value: 7.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261420837  263 QQLEMMANALGEGLMMLNRDGRIVWMNPEAGRLLGLdpEKAKGKPLFSFVSLAGPDGDKWDW 324
Cdd:pfam13188   1 ERLRALFENAPDGILVLDRGGRILYANPAALELLGY--EELLGELLGELLDDLEALAEEALE 60
CybB COG3038
Cytochrome B561 [Energy production and conversion]
1-137 8.81e-04

Cytochrome B561 [Energy production and conversion]


Pssm-ID: 225580  Cd Length: 181  Bit Score: 39.59  E-value: 8.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837   1 MNEYERYGLV--RLHSAMAVLAAGMFVLLLFAaGRLPVSLEFYHS---IHLSLGLAVMVVcwLVAVQGWAVF----PHTL 71
Cdd:COG3038    2 TNTENRYGLVqiALHWLMALLVIGAFALGELM-GFLPRGPGLYFLlyeLHKSIGILVLAL--MVLRLLWRLRnpapPIVP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  72 SLERLMMGALFFSSGLLFSLHVVLSFA------SDGAEAPLFSL------------------AARLTLAWGLLFL----- 122
Cdd:COG3038   79 GPPPWQRKAAKLGHLALYLLMLALPLSgyllstASGRPISVFGLftvpatllpnpaladlakAIHETLAWLLYALiglha 158
                        170       180
                 ....*....|....*....|..
gi 261420837 123 -------FSRRDEVMERRSGQR 137
Cdd:COG3038  159 aaalkhhFIDKDNTLRRMLPRR 180
PTC1 COG0631
Serine/threonine protein phosphatase [Signal transduction mechanisms]
548-636 8.59e-03

Serine/threonine protein phosphatase [Signal transduction mechanisms]


Pssm-ID: 223704  Cd Length: 262  Bit Score: 36.95  E-value: 8.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 548 ALGLFPQFSFETKSVVLEPGDFVLLYTDGVTEKRTEEADDDFsvlaamvarVNLDQPAPEIVRELYEHIQAYHqyeQKDD 627
Cdd:COG0631  176 ALGDFDLLEPDITELELEPGDFLLLCSDGLWDVVSDDEIVDI---------LKNSETPQEAADKLIELALEGG---GPDN 243

                 ....*....
gi 261420837 628 QTLLLLRRR 636
Cdd:COG0631  244 ITVVLVRLN 252
PAS_9 pfam13426
PAS domain;
274-381 1.17e-13

PAS domain;


Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 67.79  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  274 EGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVslagpdGDKWDWKQLRRVVKRLKSGEVIRVEEEpFRRRDGV 353
Cdd:pfam13426   2 DGILVLDPEGRIVYANPAALRLLGYTREELLGKSIRDLF------GPGTDEEAVARLREALRNGGEVEVELE-LRRKDGE 74
                          90       100
                  ....*....|....*....|....*....
gi 261420837  354 CLPVGYTLAPVL-ENGALAGLVAVLRDMT 381
Cdd:pfam13426  75 PFPVLVSASPVRdEDGEVVGIVGILRDIT 103
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
335-636 1.60e-52

Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / Transcription]


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 185.68  E-value: 1.60e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 335 KSGEVIRVEEEPFRRRDGVCLPVGYTLAPVLENGALAGLVAVLRDmtekkekerlerEREQLDFELSLAANMQRSLLqtS 414
Cdd:COG2208   75 VSGKLRALSEEIKHWRGGLPLVAELLVEINRAVGLVSAHNELLLL------------EQNNISAELEVARQIQQNLL--P 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 415 SKVNLPSYIDIGVLSVPARVLSGDFYHFAVHQTS-VSVGIADVSGKGIPAAMLMTLMKFILDRT-VHYGTQPHVYLDLLN 492
Cdd:COG2208  141 KALPLFPGIDIEAILVPASEVGGDYYDFIQLGEKrLRIGIGDVSGKGVPAALLMLMPKLALRLLlESGPLDPADVLETLN 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 493 RFACDYTEPSMFVTMFVGNYNEKTHTFSYACAGHEPALWYRAKTKQCV-PLGAKGCALGLFPQFSFETKSVVLEPGDFVL 571
Cdd:COG2208  221 RVLKQNLEEDMFVTLFLGVYDLDSGELTYSNAGHEPALILSADGEIEVeDLTALGLPIGLLPDYQYEVASLQLEPGDLLV 300
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261420837 572 LYTDGVTEKRTEEADD-DFSVLAAMVARvNLDQPAPEIVRELYEHIQAYHQY-EQKDDQTLLLLRRR 636
Cdd:COG2208  301 LYTDGVTEARNSDGEFfGLERLLKILGR-LLGQPAEEILEAILESLEELQGDqIQDDDITLLVLKVK 366
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
262-381 2.84e-12

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


Pssm-ID: 232884 [Multi-domain]  Cd Length: 124  Bit Score: 64.23  E-value: 2.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  262 EQQLEMMANALGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVSlagPDgdkwDWKQLRRVVKRLKSGE-VI 340
Cdd:TIGR00229   2 EERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIP---EE----DREEVRERIERRLEGErEP 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 261420837  341 RVEEEPFRRRDGVCLPVGYTLAPVLENGALAGLVAVLRDMT 381
Cdd:TIGR00229  75 VSEERRVRRKDGSEIWVEVSVSPIRTNGGELGVVGIVRDIT 115
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
263-380 4.40e-11

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


Pssm-ID: 250275 [Multi-domain]  Cd Length: 111  Bit Score: 60.49  E-value: 4.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  263 QQLEMMANALGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVSlagPDgdkwDWKQLRRVVKRLKSGEVIRV 342
Cdd:pfam00989   1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIP---EE----DDAVAELLRQALLQGEESRG 73
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 261420837  343 EEEPFRRRDGVCLPVGYTLAPVLENGALAGLVAVLRDM 380
Cdd:pfam00989  74 FEVSFRVRDGRPRHVEVRASPVRDAGGEIGFLGVLRDI 111
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
165-381 6.57e-11

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 61.40  E-value: 6.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 165 DGTSRWPFWWKAGEGMIGL-----------LDAGAALLVWRRWRQGSSRSFLYWLLALWLFALGQWLLMLGGGHVLWGQL 233
Cdd:COG2202    6 DRDGRIIYANEAAEELLGYsaeellglllaLHPEDRDRLRELLRRLLAGEELLSEELRLVRKDGEERWVELSAAPLRDGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 234 YEMAGFLYIVRAMYVETVEKpyvELKQHEQQLEMMANALGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVS 313
Cdd:COG2202   86 GRVLGLLGLRDITERKRAEE---ALRESEERLRALLEASPDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSDLIH 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261420837 314 LAGPdgdkwDWKQLRRVVKRLKSGEVIRVEEEPFRRRDG-VCLPVGYTLAPVLENGALAGLVAVLRDMT 381
Cdd:COG2202  163 PEDE-----ERRELELARALAEGRGGPLEIEYRVRRKDGeRVRWILSRISPVRDDGEIVGVVGIARDIT 226
RocR COG3829
Transcriptional regulator containing PAS, AAA-type ATPase, and DNA-binding domains ...
239-381 2.66e-09

Transcriptional regulator containing PAS, AAA-type ATPase, and DNA-binding domains [Transcription / Signal transduction mechanisms]


Pssm-ID: 226350 [Multi-domain]  Cd Length: 560  Bit Score: 58.47  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 239 FLYIVRAMyvETVEkpyVELKQHEQQLEMMANALGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVSLAGPd 318
Cdd:COG3829   98 FLDISEAL--ELIE---ENLRQLRQRLEAILDSIDDGLLVVDEDGIIIYYNKAYAKLLGLSPEEVLGKHLLDVVSAGED- 171
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261420837 319 gdkwdwKQLRRVvkrLKSGEVIRVEEEPFRRRDGVClpvgyTLAPVLENGALAGLVAVLRDMT 381
Cdd:COG3829  172 ------STLLEV---LRTGKPIRDVVQTYNGNKIIV-----NVAPVYADGQLIGVVGISKDVS 220
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
270-381 1.31e-08

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: 254806 [Multi-domain]  Cd Length: 110  Bit Score: 53.19  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  270 NALGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVSLAGPDgdkwdwkQLRRVVKRLKSGEViRVEEEPFRR 349
Cdd:pfam08448   2 DSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAA-------RLERALRRALEGEE-PIDFLEELL 73
                          90       100       110
                  ....*....|....*....|....*....|...
gi 261420837  350 RDGVCLPVGYTLAPVL-ENGALAGLVAVLRDMT 381
Cdd:pfam08448  74 LNGEERHYELRLTPLRdPDGEVIGVLVISRDIT 106
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
262-309 2.29e-05

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: 234074 [Multi-domain]  Cd Length: 333  Bit Score: 45.66  E-value: 2.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 261420837  262 EQQLEMM---ANALGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLF 309
Cdd:TIGR02966   2 SALLSRFraaAQALPDAVVVLDEEGQIEWCNPAAERLLGLRWPDDLGQRIT 52
PRK11360 PRK11360
sensory histidine kinase AtoS; Provisional
267-381 1.18e-04

sensory histidine kinase AtoS; Provisional


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 43.80  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 267 MMANAlGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVSLAGPdgdkwdwkqLRRVVKR-LKSGEVIRVEEE 345
Cdd:PRK11360 267 ILESI-ADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTP---------FASPLLDtLEHGTEHVDLEI 336
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 261420837 346 PFRRRDG-VCLPVGYTLapvLEN--GALAGLVAVLRDMT 381
Cdd:PRK11360 337 SFPGRDRtIELSVSTSL---LHNthGEMIGALVIFSDLT 372
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
544-634 2.21e-04

stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane spanning protein with two separable functions. It plays a role in the switch to polar cell division during sporulation. By means of it protein phosphatase activity, located in the C-terminal region, it activates sigma-F. All proteins that score above the trusted cutoff to this model are found in endospore-forming Gram-positive bacteria. Surprisingly, a sequence from the Cyanobacterium-like (and presumably non-spore-forming) photosynthesizer Heliobacillus mobilis is homologous, and scores between the trusted and noise cutoffs [Cellular processes, Sporulation and germination].


Pssm-ID: 234038 [Multi-domain]  Cd Length: 764  Bit Score: 42.76  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837  544 AKGCALGLFPQFSFETKSVVLEPGDFVLLYTDGVTEKRTEEADDDFSVLAAMvARVNLDQPApEIVRELYEHIQAYHQYE 623
Cdd:TIGR02865 674 SSNLPIGILDEVDVELVRKKLKNGDLIVMVSDGVLEGEKEVEGKVLWLVRKL-KETNTNDPE-EIAEYLLEKAKELRSGK 751
                          90
                  ....*....|.
gi 261420837  624 QKDDQTLLLLR 634
Cdd:TIGR02865 752 IKDDMTVIVAK 762
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
257-314 3.96e-04

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 41.97  E-value: 3.96e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 261420837 257 ELKQHEQQLEMMANALGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVSL 314
Cdd:PRK11388 197 ESNRHLNQLNALLESMDDGVIAWDEQGNLQFLNAQAARLLRLDATASQGRAITELLTL 254
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
263-381 1.01e-03

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 40.67  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 263 QQLEMMANALGEGLMMLNRDGRIVWMNPEAGRLLGLdPEKAKGKPLFSFVSlagpdgdkwDWKQLRRVVKRLKSGEVIRV 342
Cdd:PRK11086 221 EQRQAMLQSIKEGVIAVDDRGEVTLINDEAKRLFNY-KKGLEDDPLGTDVE---------SWMPVSRLKEVLRTGTPRRD 290
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 261420837 343 EEEPFRRRDGVCLPVgytlaPVLENGALAGLVAVLRDMT 381
Cdd:PRK11086 291 EEININGRLLLTNTV-----PVRVNGEIIGAIATFRDKT 324
VicK COG5002
Signal transduction histidine kinase [Signal transduction mechanisms]
258-381 1.43e-03

Signal transduction histidine kinase [Signal transduction mechanisms]


Pssm-ID: 227335 [Multi-domain]  Cd Length: 459  Bit Score: 40.11  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 258 LKQHEQQLEMMANALGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVSLAgpdgdkwDWKQLRRVVKrlKSG 337
Cdd:COG5002  106 TEQERRKLDSVLAYMTDGVIATDRRGKIILINKPALKMLGVSKEDALGRSILELLKIE-------DTYTFEDLVE--KND 176
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 261420837 338 EV---IRVEEEPfrrrdgVCLPVGYTLApVLENGALAGLVAVLRDMT 381
Cdd:COG5002  177 SLlldSSDEEEG------YVLRVNFSVI-QRESGFISGLIAVLHDVT 216
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
275-383 2.01e-03

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 39.06  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 275 GLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGkplfsfvslAGPDGDKWDWKQLRRVVKRLKSGEVIRVEEEPFRRRDGVC 354
Cdd:COG2202    1 LILVLDRDGRIIYANEAAEELLGYSAEELLG---------LLLALHPEDRDRLRELLRRLLAGEELLSEELRLVRKDGEE 71
                         90       100
                 ....*....|....*....|....*....
gi 261420837 355 LPVGYTLAPVLENGALAGLVAVLRDMTEK 383
Cdd:COG2202   72 RWVELSAAPLRDGEGRVLGLLGLRDITER 100
NtrB COG3852
Signal transduction histidine kinase, nitrogen specific [Signal transduction mechanisms]
270-380 2.68e-03

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


Pssm-ID: 226370 [Multi-domain]  Cd Length: 363  Bit Score: 38.89  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261420837 270 NALGEGLMMLNRDGRIVWMNPEAGRLLGLDPEKAKGKPLFSFVSLAGPDGDkwdwkQLRRVVKRLKSGEVIRVEEEpfrr 349
Cdd:COG3852   14 NNLINPVLLVDDELAIHYANPAAEQLLAVSARRLAGTRLSELLPFGSLLLS-----LLDQVLERGQPVTEYEVTLV---- 84
                         90       100       110
                 ....*....|....*....|....*....|.
gi 261420837 350 RDGVCLPVGYTLAPVLENGALAGLVAVLRDM 380
Cdd:COG3852   85 ILGRSHIVDLTVAPVPEEPGSVLLEFHPRDM 115
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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