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Conserved domains on  [gi|182434519|ref|YP_001822238|]
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hypothetical protein SGR_726 [Streptomyces griseus subsp. griseus NBRC 13350]

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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 ...
28-130 1.74e-07

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: 49.94  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  28 MGSFDWDLDTGLMHMDRTALDVFDLTEDEYDDRpdSLAPRVPTDEAQRLDALVSHALkSGRTEYGAYFRIQRRDGTLRWT 107
Cdd:cd00130    3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGK--SLLDLIHPEDREELRERLENLL-SGGEPVTLEVRLRRKDGSVIWV 79
                         90       100
                 ....*....|....*....|...
gi 182434519 108 HTQGFVRRDGAGRPHRIIGIVRD 130
Cdd:cd00130   80 LVSLTPIRDEGGEVIGLLGVVRD 102
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
363-551 3.98e-48

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: 167.85  E-value: 3.98e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  363 PGGRVGAVIGDVQGHDTHAAAVMGQLRIVLRAYAAEGHSPATVMARA-SVFLHELDTDRFATCTYAEVDLTTGVVQLVRA 441
Cdd:pfam07228   1 PDGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLnRALQRNLEGERFATAVLAVYDPETGTLEYANA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  442 GHVDPLVRDVDGSCRRMPSEGGLPLGLSAEfgrLEYPVGTVELDPGQTMVLFTDGLVELPGSD--LDEGMQHLTALVTNG 519
Cdd:pfam07228  81 GHPPPLLLRPDGGVVELLESPGLPLGVLPD---APYETAEFPLEPGDTLLLYTDGLTEARDPDgeLFGLERLLALLAERH 157
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 182434519  520 PRDLQELADRLCDTVDERGGQ---DDVAVLLLRRR 551
Cdd:pfam07228 158 GLSPEELLDALLEDLLRLGGGeleDDITLLVLRVR 192
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
570-682 5.85e-14

Histidine kinase-like ATPase domain;


:

Pssm-ID: 257897  Cd Length: 126  Bit Score: 69.58  E-value: 5.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  570 DPEALRSSRHMIRAAVRAWG-AKDRADEIELAADELITNALMHT---DGGAVVTIRVLAGPeRRLRVDVEDR-------S 638
Cdd:pfam13581   4 DLEALRAARRFVAAFLARAGlSEERLEEIELAVEEALTNAVEHAyreDPGGPVRVRLEIDG-DGLVVEVRDSgpgfdplE 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 182434519  639 SALPRRRDAGESGVSGRGLMLVDRLADVWGVESRGSGKCVWCEF 682
Cdd:pfam13581  83 LPDPDLTEPDDLPEGGRGLFLIRQLMDEVEYERGDGGNVLRLTK 126
GAF_2 pfam13185
GAF domain;
227-307 4.64e-08

GAF domain;


:

Pssm-ID: 257553  Cd Length: 150  Bit Score: 51.83  E-value: 4.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  227 EVVRTLTPRFIEsadDFATSYPILWRD-ISHLEITSAAYMPLIAQARPIGALGLLYRDKGGFTEDERNLLMALGTSIAQS 305
Cdd:pfam13185  72 GALRTGKPVIIN---DVASDPSGAGGLpAGHEGLRSFLSVPLISGGRVIGVLALGSKEPGAFDEEDLELLELLAEQIAIA 148

                  ..
gi 182434519  306 LQ 307
Cdd:pfam13185 149 IE 150
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
40-128 8.28e-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: 254805 [Multi-domain]  Cd Length: 90  Bit Score: 62.40  E-value: 8.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519   40 MHMDRTALDVFDLTEDEYDDRPDSLAPRVPTDEAQRLDALVSHALKSGRTEYGAYFRIQRRDGTLRWTHTQGFVRRDGAG 119
Cdd:pfam08447   2 IYWSPRFEEILGYTPEELKSSYEGWLDLVHPEDRERVRRALQELLLKKGEPYSGEYRIRRKDGSYRWVEARGRPIRDENG 81

                  ....*....
gi 182434519  120 RPHRIIGIV 128
Cdd:pfam08447  82 KPVRVIGVA 90
 
Name Accession Description Interval E-value
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
28-130 1.74e-07

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: 49.94  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  28 MGSFDWDLDTGLMHMDRTALDVFDLTEDEYDDRpdSLAPRVPTDEAQRLDALVSHALkSGRTEYGAYFRIQRRDGTLRWT 107
Cdd:cd00130    3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGK--SLLDLIHPEDREELRERLENLL-SGGEPVTLEVRLRRKDGSVIWV 79
                         90       100
                 ....*....|....*....|...
gi 182434519 108 HTQGFVRRDGAGRPHRIIGIVRD 130
Cdd:cd00130   80 LVSLTPIRDEGGEVIGLLGVVRD 102
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
363-551 3.98e-48

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: 167.85  E-value: 3.98e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  363 PGGRVGAVIGDVQGHDTHAAAVMGQLRIVLRAYAAEGHSPATVMARA-SVFLHELDTDRFATCTYAEVDLTTGVVQLVRA 441
Cdd:pfam07228   1 PDGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLnRALQRNLEGERFATAVLAVYDPETGTLEYANA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  442 GHVDPLVRDVDGSCRRMPSEGGLPLGLSAEfgrLEYPVGTVELDPGQTMVLFTDGLVELPGSD--LDEGMQHLTALVTNG 519
Cdd:pfam07228  81 GHPPPLLLRPDGGVVELLESPGLPLGVLPD---APYETAEFPLEPGDTLLLYTDGLTEARDPDgeLFGLERLLALLAERH 157
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 182434519  520 PRDLQELADRLCDTVDERGGQ---DDVAVLLLRRR 551
Cdd:pfam07228 158 GLSPEELLDALLEDLLRLGGGeleDDITLLVLRVR 192
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
334-531 1.17e-26

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 107.82  E-value: 1.17e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519   334 VPGAQVAVRYRSARLgrdIGGDWYDLIPLPGGRVGAVIGDVQGHDTHAAAVMGQLRIVLRAYAAEGHSPATVMARA-SVF 412
Cdd:smart00331   1 DDGGLIAQYYEDATQ---VGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLnRAI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519   413 LHELDTDRFATCTYAEVDLTTGVVQLVRAGHVDP-LVRDVDGSCRRMPSEgGLPLGLSAEFgrlEYPVGTVELDPGQTMV 491
Cdd:smart00331  78 YENGEDGMFATLFLALYDFAGGTLSYANAGHSPPyLLRADGGLVEDLDDL-GAPLGLEPDV---EVDVRELTLEPGDLLL 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 182434519   492 LFTDGLVELPGSDLDEGMqhLTALVTNGPRDL-QELADRLC 531
Cdd:smart00331 154 LYTDGLTEARNPERLEEL--LEELLGSPPAEIaQRILEELL 192
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
570-682 5.85e-14

Histidine kinase-like ATPase domain;


Pssm-ID: 257897  Cd Length: 126  Bit Score: 69.58  E-value: 5.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  570 DPEALRSSRHMIRAAVRAWG-AKDRADEIELAADELITNALMHT---DGGAVVTIRVLAGPeRRLRVDVEDR-------S 638
Cdd:pfam13581   4 DLEALRAARRFVAAFLARAGlSEERLEEIELAVEEALTNAVEHAyreDPGGPVRVRLEIDG-DGLVVEVRDSgpgfdplE 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 182434519  639 SALPRRRDAGESGVSGRGLMLVDRLADVWGVESRGSGKCVWCEF 682
Cdd:pfam13581  83 LPDPDLTEPDDLPEGGRGLFLIRQLMDEVEYERGDGGNVLRLTK 126
GAF_2 pfam13185
GAF domain;
227-307 4.64e-08

GAF domain;


Pssm-ID: 257553  Cd Length: 150  Bit Score: 51.83  E-value: 4.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  227 EVVRTLTPRFIEsadDFATSYPILWRD-ISHLEITSAAYMPLIAQARPIGALGLLYRDKGGFTEDERNLLMALGTSIAQS 305
Cdd:pfam13185  72 GALRTGKPVIIN---DVASDPSGAGGLpAGHEGLRSFLSVPLISGGRVIGVLALGSKEPGAFDEEDLELLELLAEQIAIA 148

                  ..
gi 182434519  306 LQ 307
Cdd:pfam13185 149 IE 150
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
94-134 1.60e-07

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


Pssm-ID: 197509  Cd Length: 43  Bit Score: 48.72  E-value: 1.60e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 182434519    94 YFRIQRRDGTLRWTHTQGFVRRDGAGRPHRIIGIVRDATQE 134
Cdd:smart00086   3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
FhlA COG2203
FOG: GAF domain [Signal transduction mechanisms]
249-315 2.39e-07

FOG: GAF domain [Signal transduction mechanisms]


Pssm-ID: 225113  Cd Length: 175  Bit Score: 49.98  E-value: 2.39e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 182434519 249 ILWRDISHLEITSAAYMPLIAQARPIGALGLLYRDKGG-FTEDERNLLMALGTSIAQSLQRAMLYEQE 315
Cdd:COG2203  104 DNPLVLLEPPIRSYLGVPLIAQGELLGLLCVHDSEPRRqWSEEELELLEELAEQVAIAIERARLYEEL 171
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
227-316 2.21e-06

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500  Cd Length: 149  Bit Score: 46.61  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519   227 EVVRTLTPRFIE-SADDFATSYPILWRdisHLEITSAAYMPLIAQARPIGALGLLYRDKGG-FTEDERNLLMALGTSIAQ 304
Cdd:smart00065  61 RVAETGRPLNIPdVEADPLFAEDLLGR---YQGVRSFLAVPLVADGELVGVLALHNKKSPRpFTEEDEELLQALANQLAI 137
                           90
                   ....*....|..
gi 182434519   305 SLQRAMLYEQEH 316
Cdd:smart00065 138 ALANAQLYEELR 149
PTC1 COG0631
Serine/threonine protein phosphatase [Signal transduction mechanisms]
456-551 4.14e-05

Serine/threonine protein phosphatase [Signal transduction mechanisms]


Pssm-ID: 223704  Cd Length: 262  Bit Score: 44.27  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519 456 RRMPSEGGLPLG----LSAEFGRLEYP---VGTVELDPGQTMVLFTDGLVE-LPGSDLDEgmqhltaLVTNgPRDLQELA 527
Cdd:COG0631  157 GIITPEEARSHPrrnaLTRALGDFDLLepdITELELEPGDFLLLCSDGLWDvVSDDEIVD-------ILKN-SETPQEAA 228
                         90       100
                 ....*....|....*....|....
gi 182434519 528 DRLCDTVDERGGQDDVAVLLLRRR 551
Cdd:COG0631  229 DKLIELALEGGGPDNITVVLVRLN 252
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms]
565-665 1.89e-04

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


Pssm-ID: 225083  Cd Length: 146  Bit Score: 40.82  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519 565 HVAQNDPEALRSSRHMIRAAVRAWGA-----KDRADEIELAADELITNALMHTDGGAV----VTIRVLAGPErRLRVDVE 635
Cdd:COG2172    4 HITDLVLPAKLSAVGTARLTLREFARelgltYVDIADLAIAVSEALTNAVKHAYKLDPsegeIRIEVSLDDG-KLEIRIW 82
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 182434519 636 DRSSALPRRR--------DAGESGVSGRGLMLVDRLAD 665
Cdd:COG2172   83 DQGPGIEDLEeslgpgdtTAEGLQEGGLGLFLAKRLMD 120
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
594-670 4.59e-03

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


Pssm-ID: 214643  Cd Length: 111  Bit Score: 36.09  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519   594 ADEIEL--AADELITNALMHTDGGAVVTIRVLAGPErRLRVDVEDR----------------SSALPRRRDAGESGVsgr 655
Cdd:smart00387   1 GDPDRLrqVLSNLLDNAIKYTPEGGRITVTLERDGD-HVEITVEDNgpgippedlekifepfFRTDKRSRKIGGTGL--- 76
                           90
                   ....*....|....*
gi 182434519   656 GLMLVDRLADVWGVE 670
Cdd:smart00387  77 GLSIVKKLVELHGGE 91
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
40-128 8.28e-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: 254805 [Multi-domain]  Cd Length: 90  Bit Score: 62.40  E-value: 8.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519   40 MHMDRTALDVFDLTEDEYDDRPDSLAPRVPTDEAQRLDALVSHALKSGRTEYGAYFRIQRRDGTLRWTHTQGFVRRDGAG 119
Cdd:pfam08447   2 IYWSPRFEEILGYTPEELKSSYEGWLDLVHPEDRERVRRALQELLLKKGEPYSGEYRIRRKDGSYRWVEARGRPIRDENG 81

                  ....*....
gi 182434519  120 RPHRIIGIV 128
Cdd:pfam08447  82 KPVRVIGVA 90
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
267-551 4.04e-33

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


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 130.60  E-value: 4.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519 267 LIAQARPIGALGLLYRDKGGFTeDERNLLMALGTSIAQSLQRA-MLYEQEHDLAEGLQQAMLPRRIPAVPGAQVAVRYRS 345
Cdd:COG2208   79 LRALSEEIKHWRGGLPLVAELL-VEINRAVGLVSAHNELLLLEqNNISAELEVARQIQQNLLPKALPLFPGIDIEAILVP 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519 346 ARlgrDIGGDWYDLIPLPGGRVGAVIGDVQGHDTHAAAVMGQLRIVLRAY-AAEGHSPATVMARASVFLHE-LDTDRFAT 423
Cdd:COG2208  158 AS---EVGGDYYDFIQLGEKRLRIGIGDVSGKGVPAALLMLMPKLALRLLlESGPLDPADVLETLNRVLKQnLEEDMFVT 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519 424 CTYAEVDLTTGVVQLVRAGHVDPLVRDVDGSCRRMPSEG-GLPLGLSAEFgrlEYPVGTVELDPGQTMVLFTDGLVELPG 502
Cdd:COG2208  235 LFLGVYDLDSGELTYSNAGHEPALILSADGEIEVEDLTAlGLPIGLLPDY---QYEVASLQLEPGDLLVLYTDGVTEARN 311
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 182434519 503 SDLD----EGMQH-LTALVTNGPRDL-QELADRLCDTVDERGGQDDVAVLLLRRR 551
Cdd:COG2208  312 SDGEffglERLLKiLGRLLGQPAEEIlEAILESLEELQGDQIQDDDITLLVLKVK 366
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
344-549 4.17e-06

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: 48.53  E-value: 4.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  344 RSARLGRDIGGDWYDLIPLPGGRVGAVIGDVQGHDTHAAAVMGQLRIVLRAYAAEGHSPATVM-ARASVFLHELDTDRFA 422
Cdd:TIGR02865 558 RAAKDGELVSGDSYSFGKLSAGKYAVAISDGMGSGPEAAQESSACVRLLEKFLESGFDREVAIkTVNSILSLRSTDEKFS 637
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  423 TCTYAEVDLTTGVVQLVRAGHVDPLVRDvDGSCRRMPSEgGLPLGLSAEFgrlEYPVGTVELDPGQTMVLFTDGLVElpG 502
Cdd:TIGR02865 638 TLDLSVIDLYTGQAEFVKVGAVPSFIKR-GAKVEVIRSS-NLPIGILDEV---DVELVRKKLKNGDLIVMVSDGVLE--G 710
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 182434519  503 SDLDEG-----MQHLTALVTNGPrdlQELADRLCDTVDE-RGGQ--DDVAVLLLR 549
Cdd:TIGR02865 711 EKEVEGkvlwlVRKLKETNTNDP---EEIAEYLLEKAKElRSGKikDDMTVIVAK 762
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
68-133 8.84e-05

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: 41.50  E-value: 8.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 182434519   68 VPTDEAQRLDALVSHALKSGRTEYGAYFRIQRRDGTLRWTHTQGFVRRDGAGRPHrIIGIVRDATQ 133
Cdd:TIGR00229  52 IPEEDREEVRERIERRLEGEREPVSEERRVRRKDGSEIWVEVSVSPIRTNGGELG-VVGIVRDITE 116
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
29-133 5.29e-04

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 41.97  E-value: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519   29 GSFDWDLDTGLMHMDRTALDVFDL---TEDEYDDRPDSLAPrvptDEAQRLDALVSHALkSGRTEYGAYFRIQRRDGTlR 105
Cdd:PRK09776  422 GIWEWDLKPNIISWDKRMFELYEIpphIKPTWQVWYACLHP----EDRQRVEKEIRDAL-QGRSPFKLEFRIVVKDGV-R 495
                          90       100
                  ....*....|....*....|....*...
gi 182434519  106 WTHTQGFVRRDGAGRPHRIIGIVRDATQ 133
Cdd:PRK09776  496 HIRALANRVLNKDGEVERLLGINMDMTE 523
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
27-134 6.66e-04

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 40.60  E-value: 6.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  27 RMGSFDWDLDTGLMHMDRTALDVFDLTEDEYDDRPDSLAPRVPTDEAQRLDALVSHALKSGRTEYGaYFRIQRRDGTLRW 106
Cdd:COG2202  122 PDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSDLIHPEDEERRELELARALAEGRGGPLEI-EYRVRRKDGERVR 200
                         90       100
                 ....*....|....*....|....*...
gi 182434519 107 THTQGFVRRDGAGRPHRIIGIVRDATQE 134
Cdd:COG2202  201 WILSRISPVRDDGEIVGVVGIARDITER 228
 
Name Accession Description Interval E-value
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
28-130 1.74e-07

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: 49.94  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  28 MGSFDWDLDTGLMHMDRTALDVFDLTEDEYDDRpdSLAPRVPTDEAQRLDALVSHALkSGRTEYGAYFRIQRRDGTLRWT 107
Cdd:cd00130    3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGK--SLLDLIHPEDREELRERLENLL-SGGEPVTLEVRLRRKDGSVIWV 79
                         90       100
                 ....*....|....*....|...
gi 182434519 108 HTQGFVRRDGAGRPHRIIGIVRD 130
Cdd:cd00130   80 LVSLTPIRDEGGEVIGLLGVVRD 102
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
363-551 3.98e-48

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: 167.85  E-value: 3.98e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  363 PGGRVGAVIGDVQGHDTHAAAVMGQLRIVLRAYAAEGHSPATVMARA-SVFLHELDTDRFATCTYAEVDLTTGVVQLVRA 441
Cdd:pfam07228   1 PDGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLnRALQRNLEGERFATAVLAVYDPETGTLEYANA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  442 GHVDPLVRDVDGSCRRMPSEGGLPLGLSAEfgrLEYPVGTVELDPGQTMVLFTDGLVELPGSD--LDEGMQHLTALVTNG 519
Cdd:pfam07228  81 GHPPPLLLRPDGGVVELLESPGLPLGVLPD---APYETAEFPLEPGDTLLLYTDGLTEARDPDgeLFGLERLLALLAERH 157
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 182434519  520 PRDLQELADRLCDTVDERGGQ---DDVAVLLLRRR 551
Cdd:pfam07228 158 GLSPEELLDALLEDLLRLGGGeleDDITLLVLRVR 192
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
334-531 1.17e-26

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 107.82  E-value: 1.17e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519   334 VPGAQVAVRYRSARLgrdIGGDWYDLIPLPGGRVGAVIGDVQGHDTHAAAVMGQLRIVLRAYAAEGHSPATVMARA-SVF 412
Cdd:smart00331   1 DDGGLIAQYYEDATQ---VGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLnRAI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519   413 LHELDTDRFATCTYAEVDLTTGVVQLVRAGHVDP-LVRDVDGSCRRMPSEgGLPLGLSAEFgrlEYPVGTVELDPGQTMV 491
Cdd:smart00331  78 YENGEDGMFATLFLALYDFAGGTLSYANAGHSPPyLLRADGGLVEDLDDL-GAPLGLEPDV---EVDVRELTLEPGDLLL 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 182434519   492 LFTDGLVELPGSDLDEGMqhLTALVTNGPRDL-QELADRLC 531
Cdd:smart00331 154 LYTDGLTEARNPERLEEL--LEELLGSPPAEIaQRILEELL 192
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
570-682 5.85e-14

Histidine kinase-like ATPase domain;


Pssm-ID: 257897  Cd Length: 126  Bit Score: 69.58  E-value: 5.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  570 DPEALRSSRHMIRAAVRAWG-AKDRADEIELAADELITNALMHT---DGGAVVTIRVLAGPeRRLRVDVEDR-------S 638
Cdd:pfam13581   4 DLEALRAARRFVAAFLARAGlSEERLEEIELAVEEALTNAVEHAyreDPGGPVRVRLEIDG-DGLVVEVRDSgpgfdplE 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 182434519  639 SALPRRRDAGESGVSGRGLMLVDRLADVWGVESRGSGKCVWCEF 682
Cdd:pfam13581  83 LPDPDLTEPDDLPEGGRGLFLIRQLMDEVEYERGDGGNVLRLTK 126
GAF_2 pfam13185
GAF domain;
227-307 4.64e-08

GAF domain;


Pssm-ID: 257553  Cd Length: 150  Bit Score: 51.83  E-value: 4.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  227 EVVRTLTPRFIEsadDFATSYPILWRD-ISHLEITSAAYMPLIAQARPIGALGLLYRDKGGFTEDERNLLMALGTSIAQS 305
Cdd:pfam13185  72 GALRTGKPVIIN---DVASDPSGAGGLpAGHEGLRSFLSVPLISGGRVIGVLALGSKEPGAFDEEDLELLELLAEQIAIA 148

                  ..
gi 182434519  306 LQ 307
Cdd:pfam13185 149 IE 150
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
94-134 1.60e-07

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


Pssm-ID: 197509  Cd Length: 43  Bit Score: 48.72  E-value: 1.60e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 182434519    94 YFRIQRRDGTLRWTHTQGFVRRDGAGRPHRIIGIVRDATQE 134
Cdd:smart00086   3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
FhlA COG2203
FOG: GAF domain [Signal transduction mechanisms]
249-315 2.39e-07

FOG: GAF domain [Signal transduction mechanisms]


Pssm-ID: 225113  Cd Length: 175  Bit Score: 49.98  E-value: 2.39e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 182434519 249 ILWRDISHLEITSAAYMPLIAQARPIGALGLLYRDKGG-FTEDERNLLMALGTSIAQSLQRAMLYEQE 315
Cdd:COG2203  104 DNPLVLLEPPIRSYLGVPLIAQGELLGLLCVHDSEPRRqWSEEELELLEELAEQVAIAIERARLYEEL 171
GAF_3 pfam13492
GAF domain;
251-308 1.94e-06

GAF domain;


Pssm-ID: 257816  Cd Length: 129  Bit Score: 46.67  E-value: 1.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 182434519  251 WRDISHLEITSAAYMPLIAQARPIGALGLLYRDKGGFTEDERNLLMALGTSIAQSLQR 308
Cdd:pfam13492  72 GDNRDLLPSESLLAVPLRAGGEVIGVLVLESTPEEAFTPEDLELLELLASQIAIALEN 129
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
227-316 2.21e-06

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500  Cd Length: 149  Bit Score: 46.61  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519   227 EVVRTLTPRFIE-SADDFATSYPILWRdisHLEITSAAYMPLIAQARPIGALGLLYRDKGG-FTEDERNLLMALGTSIAQ 304
Cdd:smart00065  61 RVAETGRPLNIPdVEADPLFAEDLLGR---YQGVRSFLAVPLVADGELVGVLALHNKKSPRpFTEEDEELLQALANQLAI 137
                           90
                   ....*....|..
gi 182434519   305 SLQRAMLYEQEH 316
Cdd:smart00065 138 ALANAQLYEELR 149
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
594-682 5.81e-06

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: 251347  Cd Length: 111  Bit Score: 45.00  E-value: 5.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  594 ADEIELAADELITNALMHTDGGAVVTIRVLAGPErRLRVDVEDRSSALP-----------RRRDAGESGVSGR--GLMLV 660
Cdd:pfam02518   3 EDRLRQVLSNLLDNAIKHAPAGGEIEVTLERDGG-RLRITVEDNGIGIPpedlpkifepfFRTDGSRSKVGGTglGLSIV 81
                          90       100
                  ....*....|....*....|....*..
gi 182434519  661 DRLADVWGVE-----SRGSGKCVWCEF 682
Cdd:pfam02518  82 RKLVELHGGTitvesEPGGGTTFTLTL 108
PTC1 COG0631
Serine/threonine protein phosphatase [Signal transduction mechanisms]
456-551 4.14e-05

Serine/threonine protein phosphatase [Signal transduction mechanisms]


Pssm-ID: 223704  Cd Length: 262  Bit Score: 44.27  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519 456 RRMPSEGGLPLG----LSAEFGRLEYP---VGTVELDPGQTMVLFTDGLVE-LPGSDLDEgmqhltaLVTNgPRDLQELA 527
Cdd:COG0631  157 GIITPEEARSHPrrnaLTRALGDFDLLepdITELELEPGDFLLLCSDGLWDvVSDDEIVD-------ILKN-SETPQEAA 228
                         90       100
                 ....*....|....*....|....
gi 182434519 528 DRLCDTVDERGGQDDVAVLLLRRR 551
Cdd:COG0631  229 DKLIELALEGGGPDNITVVLVRLN 252
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms]
565-665 1.89e-04

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


Pssm-ID: 225083  Cd Length: 146  Bit Score: 40.82  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519 565 HVAQNDPEALRSSRHMIRAAVRAWGA-----KDRADEIELAADELITNALMHTDGGAV----VTIRVLAGPErRLRVDVE 635
Cdd:COG2172    4 HITDLVLPAKLSAVGTARLTLREFARelgltYVDIADLAIAVSEALTNAVKHAYKLDPsegeIRIEVSLDDG-KLEIRIW 82
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 182434519 636 DRSSALPRRR--------DAGESGVSGRGLMLVDRLAD 665
Cdd:COG2172   83 DQGPGIEDLEeslgpgdtTAEGLQEGGLGLFLAKRLMD 120
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
189-306 6.32e-04

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyse ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalysed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyses the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54.


Pssm-ID: 250726  Cd Length: 146  Bit Score: 39.49  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  189 LVMGLLESGRIHLVADGPKGSYVPGTRYTRVDEQYPMSEVVRTLTPRFIESADDFATSYPILWRD------ISHLEITSA 262
Cdd:pfam01590  23 AIYLADADGLLLYLVAGDGLSDIPLAARGLPLGGGVVGEVIAGGNPIVVPDVQDDPRFRDLTALAsdlphfLRGLGIRSC 102
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 182434519  263 AYMPLIAQARPIGALGLLYRDKGGFTEDERNLLMALGTSIAQSL 306
Cdd:pfam01590 103 LAVPLKGGGELIGVLVLHSTSPRAFTEEELELLQALADQVAIAL 146
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
594-670 4.59e-03

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


Pssm-ID: 214643  Cd Length: 111  Bit Score: 36.09  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519   594 ADEIEL--AADELITNALMHTDGGAVVTIRVLAGPErRLRVDVEDR----------------SSALPRRRDAGESGVsgr 655
Cdd:smart00387   1 GDPDRLrqVLSNLLDNAIKYTPEGGRITVTLERDGD-HVEITVEDNgpgippedlekifepfFRTDKRSRKIGGTGL--- 76
                           90
                   ....*....|....*
gi 182434519   656 GLMLVDRLADVWGVE 670
Cdd:smart00387  77 GLSIVKKLVELHGGE 91
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
40-128 8.28e-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: 254805 [Multi-domain]  Cd Length: 90  Bit Score: 62.40  E-value: 8.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519   40 MHMDRTALDVFDLTEDEYDDRPDSLAPRVPTDEAQRLDALVSHALKSGRTEYGAYFRIQRRDGTLRWTHTQGFVRRDGAG 119
Cdd:pfam08447   2 IYWSPRFEEILGYTPEELKSSYEGWLDLVHPEDRERVRRALQELLLKKGEPYSGEYRIRRKDGSYRWVEARGRPIRDENG 81

                  ....*....
gi 182434519  120 RPHRIIGIV 128
Cdd:pfam08447  82 KPVRVIGVA 90
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
267-551 4.04e-33

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


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 130.60  E-value: 4.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519 267 LIAQARPIGALGLLYRDKGGFTeDERNLLMALGTSIAQSLQRA-MLYEQEHDLAEGLQQAMLPRRIPAVPGAQVAVRYRS 345
Cdd:COG2208   79 LRALSEEIKHWRGGLPLVAELL-VEINRAVGLVSAHNELLLLEqNNISAELEVARQIQQNLLPKALPLFPGIDIEAILVP 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519 346 ARlgrDIGGDWYDLIPLPGGRVGAVIGDVQGHDTHAAAVMGQLRIVLRAY-AAEGHSPATVMARASVFLHE-LDTDRFAT 423
Cdd:COG2208  158 AS---EVGGDYYDFIQLGEKRLRIGIGDVSGKGVPAALLMLMPKLALRLLlESGPLDPADVLETLNRVLKQnLEEDMFVT 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519 424 CTYAEVDLTTGVVQLVRAGHVDPLVRDVDGSCRRMPSEG-GLPLGLSAEFgrlEYPVGTVELDPGQTMVLFTDGLVELPG 502
Cdd:COG2208  235 LFLGVYDLDSGELTYSNAGHEPALILSADGEIEVEDLTAlGLPIGLLPDY---QYEVASLQLEPGDLLVLYTDGVTEARN 311
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 182434519 503 SDLD----EGMQH-LTALVTNGPRDL-QELADRLCDTVDERGGQDDVAVLLLRRR 551
Cdd:COG2208  312 SDGEffglERLLKiLGRLLGQPAEEIlEAILESLEELQGDQIQDDDITLLVLKVK 366
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
344-549 4.17e-06

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: 48.53  E-value: 4.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  344 RSARLGRDIGGDWYDLIPLPGGRVGAVIGDVQGHDTHAAAVMGQLRIVLRAYAAEGHSPATVM-ARASVFLHELDTDRFA 422
Cdd:TIGR02865 558 RAAKDGELVSGDSYSFGKLSAGKYAVAISDGMGSGPEAAQESSACVRLLEKFLESGFDREVAIkTVNSILSLRSTDEKFS 637
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  423 TCTYAEVDLTTGVVQLVRAGHVDPLVRDvDGSCRRMPSEgGLPLGLSAEFgrlEYPVGTVELDPGQTMVLFTDGLVElpG 502
Cdd:TIGR02865 638 TLDLSVIDLYTGQAEFVKVGAVPSFIKR-GAKVEVIRSS-NLPIGILDEV---DVELVRKKLKNGDLIVMVSDGVLE--G 710
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 182434519  503 SDLDEG-----MQHLTALVTNGPrdlQELADRLCDTVDE-RGGQ--DDVAVLLLR 549
Cdd:TIGR02865 711 EKEVEGkvlwlVRKLKETNTNDP---EEIAEYLLEKAKElRSGKikDDMTVIVAK 762
PAS_9 pfam13426
PAS domain;
44-133 3.76e-05

PAS domain;


Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 42.76  E-value: 3.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519   44 RTALDVFDLTEDEYDDRP-DSLaprVPTDEAQRLDALVSHALKSGRtEYGAYFRIQRRDGTLRWTHTQGFVRRDGAGRPH 122
Cdd:pfam13426  18 PAALRLLGYTREELLGKSiRDL---FGPGTDEEAVARLREALRNGG-EVEVELELRRKDGEPFPVLVSASPVRDEDGEVV 93
                          90
                  ....*....|.
gi 182434519  123 RIIGIVRDATQ 133
Cdd:pfam13426  94 GIVGILRDITE 104
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
68-133 8.84e-05

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: 41.50  E-value: 8.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 182434519   68 VPTDEAQRLDALVSHALKSGRTEYGAYFRIQRRDGTLRWTHTQGFVRRDGAGRPHrIIGIVRDATQ 133
Cdd:TIGR00229  52 IPEEDREEVRERIERRLEGEREPVSEERRVRRKDGSEIWVEVSVSPIRTNGGELG-VVGIVRDITE 116
FhlA COG3604
Transcriptional regulator containing GAF, AAA-type ATPase, and DNA binding domains ...
120-328 3.17e-04

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


Pssm-ID: 226132 [Multi-domain]  Cd Length: 550  Bit Score: 42.32  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519 120 RPHRIIGIVRDATQELADSTARRELDEDRRRRTSLVEGTTAALAHAR---TVKDVIAVLKNSQGLAHlgatSLVMGLLES 196
Cdd:COG3604    2 LLNQSARIISVVTEQIQSREAQRVSLELLADIRILVELTNALLSPLRlerLLAEVAKELHSLFGCDA----SALLRLDSK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519 197 GRIHLVADGPKGSYVPGTRYTRVDEQYPMSEVVRTLTP-RFIESADDFATSYPILWRDISHLEITSAAYMPLIAQARPIG 275
Cdd:COG3604   78 NLIPLATDGLSKDHLGREQRFVVEGHPLLEQILKAGRPlVFHPADSLFPDPYDGLLPDTEGNKKHACIGVPLKSGDKLIG 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 182434519 276 ALGLLYRDKGGFTEDERNLLMALGTSIAQSLQRAMLYEQEHDLAEGLQQAMLP 328
Cdd:COG3604  158 ALTLDHTEPDQFDEDLDEELRFLAALAALAVANALLHRELSSLKERLEEENLA 210
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
29-133 5.29e-04

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 41.97  E-value: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519   29 GSFDWDLDTGLMHMDRTALDVFDL---TEDEYDDRPDSLAPrvptDEAQRLDALVSHALkSGRTEYGAYFRIQRRDGTlR 105
Cdd:PRK09776  422 GIWEWDLKPNIISWDKRMFELYEIpphIKPTWQVWYACLHP----EDRQRVEKEIRDAL-QGRSPFKLEFRIVVKDGV-R 495
                          90       100
                  ....*....|....*....|....*...
gi 182434519  106 WTHTQGFVRRDGAGRPHRIIGIVRDATQ 133
Cdd:PRK09776  496 HIRALANRVLNKDGEVERLLGINMDMTE 523
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
29-130 6.66e-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: 250275 [Multi-domain]  Cd Length: 111  Bit Score: 38.92  E-value: 6.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519   29 GSFDWDLDTGLMHMDRTALDVFDLTEDEYDDRpdSLAPRVPTDEAQRLDALVShALKSGRTEYGAYFRIQRRDGTLRWTH 108
Cdd:pfam00989  13 GIFVVDEDGRILYVNAAAEELLGLSREEVIGK--SLLDLIPEEDDAVAELLRQ-ALLQGEESRGFEVSFRVRDGRPRHVE 89
                          90       100
                  ....*....|....*....|..
gi 182434519  109 TQGFVRRDGAGRPHrIIGIVRD 130
Cdd:pfam00989  90 VRASPVRDAGGEIG-FLGVLRD 110
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
27-134 6.66e-04

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 40.60  E-value: 6.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182434519  27 RMGSFDWDLDTGLMHMDRTALDVFDLTEDEYDDRPDSLAPRVPTDEAQRLDALVSHALKSGRTEYGaYFRIQRRDGTLRW 106
Cdd:COG2202  122 PDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSDLIHPEDEERRELELARALAEGRGGPLEI-EYRVRRKDGERVR 200
                         90       100
                 ....*....|....*....|....*...
gi 182434519 107 THTQGFVRRDGAGRPHRIIGIVRDATQE 134
Cdd:COG2202  201 WILSRISPVRDDGEIVGVVGIARDITER 228
 
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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