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Conserved domains on  [gi|163847779|ref|YP_001635823|]
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stage II sporulation E family protein [Chloroflexus aurantiacus J-10-fl]

Protein Classification

GAF_2 and SpoIIE domain-containing protein (domain architecture ID 10588047)

protein containing domains GAF_2, FhlA, and SpoIIE

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
401-589 2.23e-64

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: 284611  Cd Length: 190  Bit Score: 211.34  E-value: 2.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  401 RFGVVIADVTDKGVPAALFMALSRTLLRASAIDGRSPVAVLERANRLILADSRAGLFVTCFYALIDPATGRVTYANGGHN 480
Cdd:pfam07228   3 RVALVIGDVMGHGLPAALLMGMLRTALRALAAEGLDPAEVLKRLNRLLQRNLEEDMFATAVLAVYDPETGTLEYANAGHP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  481 YPLLYRQATGQVIPLAAQGIVLGIIPDPHFVPGEIVLDPGDILLFYTDGITEAMNPQRDLFGDERLAAVLRASHQHAPGD 560
Cdd:pfam07228  83 PPLLLRPDGGVVELLESTGLPLGILPDADYEVVELELEPGDTLLLYTDGLTEARDPDGELFGLERLLALLAERHGLPPEE 162
                         170       180
                  ....*....|....*....|....*....
gi 163847779  561 IVDAVLAAVREFtGDTPQTDDMTMVVIKR 589
Cdd:pfam07228 163 LLDALLEALLRL-GGGELEDDITLLVLRV 190
GAF_2 pfam13185
GAF domain;
26-164 2.72e-11

GAF domain;


:

Pssm-ID: 289928  Cd Length: 140  Bit Score: 61.34  E-value: 2.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779   26 TLNLRSALDAALIHILELTGQEAGWIYLRDEGDQFI-LAARQRLPPALTYPGTIWQGECVCQEACRTGQirqePILMP-- 102
Cdd:pfam13185   1 ALDLEELLEAILEAAVELGASEFGFILLVDEDGRLLeLAAWGGPAEELGAELRRPPGEGLVGQALRTGR----PVIVNdl 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163847779  103 --CSRLRGAVGDKRGLTHHISVELRDSSRPVGILNLATTQWAKLEAVDQQLIAAIGDLLGTAIA 164
Cdd:pfam13185  77 aeDPRAKGLPAGHAGLKSLLSVPLVSDGRVIGVLALASREPGAFDEEDLELLELLAEQIAIAIE 140
FhlA COG2203
GAF domain [Signal transduction mechanisms];
178-341 1.63e-09

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 225113  Cd Length: 175  Bit Score: 56.52  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 178 QERRALLSLSQELLVTDDLEPTIQRLVRIGARLLDADACAFIEADEAG---GRALLRACHGWELPTV-SAWPLILDENHP 253
Cdd:COG2203    1 SEEALLNELAAKIAQDLDLEEILQAALELLAELLGADRGLIYLLDEDGlldGALVAEAAEAGLEQLIdELFGLVILPACL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 254 HLWYLPERSSQLAADA-----LMRLPILLRRQSFQGHLLAPVELGGVQIGLLMV-NTINPRSFLDSEAELLGLLASQLAQ 327
Cdd:COG2203   81 IGIALREGRPVVVEDIlqdprFRDNPLVLLEPPIRSYLGVPLIAQGELLGLLCVhDSEPRRQWSEEELELLEELAEQVAI 160
                        170
                 ....*....|....
gi 163847779 328 MIDRERLYQEALAR 341
Cdd:COG2203  161 AIERARLYEELQEA 174
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
320-590 9.50e-73

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


:

Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 239.61  E-value: 9.50e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 320 LLASQLAQMIDRERLYQEALARQRLERELDLASEIQASFLPDCCPFVPGLQIEAFYQAARQVGGDFYDFIEIpattpdGQ 399
Cdd:COG2208  100 LVEINRAVGLVSAHNELLLLEQNNISAELEVARQIQQNLLPKALPLFPGIDIEAILVPASEVGGDYYDFIQL------GE 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 400 SRFGVVIADVTDKGVPAALFMALSRTLLRASAI-DGRSPVAVLERANRLILADSRAGLFVTCFYALIDPATGRVTYANGG 478
Cdd:COG2208  174 KRLRIGIGDVSGKGVPAALLMLMPKLALRLLLEsGPLDPADVLETLNRVLKQNLEEDMFVTLFLGVYDLDSGELTYSNAG 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 479 HNYPLLYRQAT-GQVIPLAAQGIVLGIIPDPHFVPGEIVLDPGDILLFYTDGITEAMNPQRDLFGDERLAAVLRASHQHA 557
Cdd:COG2208  254 HEPALILSADGeIEVEDLTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTEARNSDGEFFGLERLLKILGRLLGQP 333
                        250       260       270
                 ....*....|....*....|....*....|...
gi 163847779 558 PGDIVDAVLAAVREFTGDTPQTDDMTMVVIKRV 590
Cdd:COG2208  334 AEEILEAILESLEELQGDQIQDDDITLLVLKVK 366
 
Name Accession Description Interval E-value
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
401-589 2.23e-64

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: 284611  Cd Length: 190  Bit Score: 211.34  E-value: 2.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  401 RFGVVIADVTDKGVPAALFMALSRTLLRASAIDGRSPVAVLERANRLILADSRAGLFVTCFYALIDPATGRVTYANGGHN 480
Cdd:pfam07228   3 RVALVIGDVMGHGLPAALLMGMLRTALRALAAEGLDPAEVLKRLNRLLQRNLEEDMFATAVLAVYDPETGTLEYANAGHP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  481 YPLLYRQATGQVIPLAAQGIVLGIIPDPHFVPGEIVLDPGDILLFYTDGITEAMNPQRDLFGDERLAAVLRASHQHAPGD 560
Cdd:pfam07228  83 PPLLLRPDGGVVELLESTGLPLGILPDADYEVVELELEPGDTLLLYTDGLTEARDPDGELFGLERLLALLAERHGLPPEE 162
                         170       180
                  ....*....|....*....|....*....
gi 163847779  561 IVDAVLAAVREFtGDTPQTDDMTMVVIKR 589
Cdd:pfam07228 163 LLDALLEALLRL-GGGELEDDITLLVLRV 190
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
366-571 1.10e-50

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 174.46  E-value: 1.10e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779   366 VPGLQIEAFYQAARQVGGDFYDFIEIPAttpdgqSRFGVVIADVTDKGVPAALFMALSRTLLRASAIDGRSPVAVLERAN 445
Cdd:smart00331   1 DDGGLIAQYYEDATQVGGDFYDVVKLPE------GRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLN 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779   446 RLILADSRAGLFVTCFYALIDPATGRVTYANGGHNYPLLYRQATGQVIPLAAQGIVLGIIPDPHFVPGEIVLDPGDILLF 525
Cdd:smart00331  75 RAIYENGEDGMFATLFLALYDFAGGTLSYANAGHSPPYLLRADGGLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLLL 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 163847779   526 YTDGITEAMNPqrdlfgdERLAAVLRASHQHAPGDIVDAVLAAVRE 571
Cdd:smart00331 155 YTDGLTEARNP-------ERLEELLEELLGSPPAEIAQRILEELLE 193
GAF_2 pfam13185
GAF domain;
26-164 2.72e-11

GAF domain;


Pssm-ID: 289928  Cd Length: 140  Bit Score: 61.34  E-value: 2.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779   26 TLNLRSALDAALIHILELTGQEAGWIYLRDEGDQFI-LAARQRLPPALTYPGTIWQGECVCQEACRTGQirqePILMP-- 102
Cdd:pfam13185   1 ALDLEELLEAILEAAVELGASEFGFILLVDEDGRLLeLAAWGGPAEELGAELRRPPGEGLVGQALRTGR----PVIVNdl 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163847779  103 --CSRLRGAVGDKRGLTHHISVELRDSSRPVGILNLATTQWAKLEAVDQQLIAAIGDLLGTAIA 164
Cdd:pfam13185  77 aeDPRAKGLPAGHAGLKSLLSVPLVSDGRVIGVLALASREPGAFDEEDLELLELLAEQIAIAIE 140
FhlA COG2203
GAF domain [Signal transduction mechanisms];
178-341 1.63e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 225113  Cd Length: 175  Bit Score: 56.52  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 178 QERRALLSLSQELLVTDDLEPTIQRLVRIGARLLDADACAFIEADEAG---GRALLRACHGWELPTV-SAWPLILDENHP 253
Cdd:COG2203    1 SEEALLNELAAKIAQDLDLEEILQAALELLAELLGADRGLIYLLDEDGlldGALVAEAAEAGLEQLIdELFGLVILPACL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 254 HLWYLPERSSQLAADA-----LMRLPILLRRQSFQGHLLAPVELGGVQIGLLMV-NTINPRSFLDSEAELLGLLASQLAQ 327
Cdd:COG2203   81 IGIALREGRPVVVEDIlqdprFRDNPLVLLEPPIRSYLGVPLIAQGELLGLLCVhDSEPRRQWSEEELELLEELAEQVAI 160
                        170
                 ....*....|....
gi 163847779 328 MIDRERLYQEALAR 341
Cdd:COG2203  161 AIERARLYEELQEA 174
FhlA COG2203
GAF domain [Signal transduction mechanisms];
15-171 8.30e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 225113  Cd Length: 175  Bit Score: 54.21  E-value: 8.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  15 ALRLLAQTLNQTLNLRSALDAALIHILELTGQEAGWIYLRDEGD----QFILAARQRLPPALTYP--GTIWQGECVCQEA 88
Cdd:COG2203    5 LLNELAAKIAQDLDLEEILQAALELLAELLGADRGLIYLLDEDGlldgALVAEAAEAGLEQLIDElfGLVILPACLIGIA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  89 CRTGQIR--QEPILMPCSRLRGAVGDKRGLTHHISVELRDSSRPVGILNLATTQWA-KLEAVDQQLIAAIGDLLGTAIAR 165
Cdd:COG2203   85 LREGRPVvvEDILQDPRFRDNPLVLLEPPIRSYLGVPLIAQGELLGLLCVHDSEPRrQWSEEELELLEELAEQVAIAIER 164

                 ....*.
gi 163847779 166 AHLYEE 171
Cdd:COG2203  165 ARLYEE 170
GAF_3 pfam13492
GAF domain;
195-331 1.33e-07

GAF domain;


Pssm-ID: 290227  Cd Length: 129  Bit Score: 50.05  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  195 DLEPTIQRLVRIGARLLDADACAFIEADEagGRALLRACHGWELPTVSAWPLILDENHPHLWYLP-ERSSQLAADALMRL 273
Cdd:pfam13492   1 SLDEILEALLKLLVDLLDAEVGAVYLLDE--DGLKLQVAAGWDGKPDPEEALDIDSLLARRALGSgEPISALGSAGEDNL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 163847779  274 PillrrqsFQGHLLAPVELGGVQIGLLMVNTINPRSFLDSEAELLGLLASQLAQMIDR 331
Cdd:pfam13492  79 P-------LGKALAVPLQTPDRVIGVLALYSPGPEAFDDEDLRLLKALARQIATAIEN 129
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
195-337 5.85e-07

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: 48.15  E-value: 5.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779   195 DLEPTIQRLVRIGARLLDADACAFIEADEAGGRAL-LRACHGWELPTVS-AWPLildeNHPHLWYL-----PERSSQLAA 267
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELvLVAADGLTLPTLGiRFPL----DEGLAGRVaetgrPLNIPDVEA 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163847779   268 DALMRLPILLRRQSFQGHLLAPVELGGVQIGLLMV-NTINPRSFLDSEAELLGLLASQLAQMIDRERLYQE 337
Cdd:smart00065  77 DPLFAEDLLGRYQGVRSFLAVPLVADGELVGVLALhNKKSPRPFTEEDEELLQALANQLAIALANAQLYEE 147
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
28-172 1.40e-04

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: 41.21  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779    28 NLRSALDAALIHILELTGQEAGWIYLRDEGDQFILAARQ-RLPPALTYPGTIWQGECVCQEACRTGQIRQEPILMPC-SR 105
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELVLVAaDGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADpLF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163847779   106 LRGAVGDKRGLTHHISVELRDSSRPVGILNLA-TTQWAKLEAVDQQLIAAIGDLLGTAIARAHLYEEF 172
Cdd:smart00065  81 AEDLLGRYQGVRSFLAVPLVADGELVGVLALHnKKSPRPFTEEDEELLQALANQLAIALANAQLYEEL 148
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
320-590 9.50e-73

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


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 239.61  E-value: 9.50e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 320 LLASQLAQMIDRERLYQEALARQRLERELDLASEIQASFLPDCCPFVPGLQIEAFYQAARQVGGDFYDFIEIpattpdGQ 399
Cdd:COG2208  100 LVEINRAVGLVSAHNELLLLEQNNISAELEVARQIQQNLLPKALPLFPGIDIEAILVPASEVGGDYYDFIQL------GE 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 400 SRFGVVIADVTDKGVPAALFMALSRTLLRASAI-DGRSPVAVLERANRLILADSRAGLFVTCFYALIDPATGRVTYANGG 478
Cdd:COG2208  174 KRLRIGIGDVSGKGVPAALLMLMPKLALRLLLEsGPLDPADVLETLNRVLKQNLEEDMFVTLFLGVYDLDSGELTYSNAG 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 479 HNYPLLYRQAT-GQVIPLAAQGIVLGIIPDPHFVPGEIVLDPGDILLFYTDGITEAMNPQRDLFGDERLAAVLRASHQHA 557
Cdd:COG2208  254 HEPALILSADGeIEVEDLTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTEARNSDGEFFGLERLLKILGRLLGQP 333
                        250       260       270
                 ....*....|....*....|....*....|...
gi 163847779 558 PGDIVDAVLAAVREFTGDTPQTDDMTMVVIKRV 590
Cdd:COG2208  334 AEEILEAILESLEELQGDQIQDDDITLLVLKVK 366
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
380-588 1.26e-10

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: 274328 [Multi-domain]  Cd Length: 764  Bit Score: 62.79  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  380 QVGGDFYDFIEIpattpdGQSRFGVVIADVTDKGVPAAlfmALSRT---LLRASAIDGRSPVAVLERANRLILADSRAGL 456
Cdd:TIGR02865 565 LVSGDSYSFGKL------SAGKYAVAISDGMGSGPEAA---QESSAcvrLLEKFLESGFDREVAIKTVNSILSLRSTDEK 635
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  457 FVTCFYALIDPATGRVTYANGGHNYPLLYRQatGQVIPLAAQGIVLGIIPDPHFVPGEIVLDPGDILLFYTDGITEAmnP 536
Cdd:TIGR02865 636 FSTLDLSVIDLYTGQAEFVKVGAVPSFIKRG--AKVEVIRSSNLPIGILDEVDVELVRKKLKNGDLIVMVSDGVLEG--E 711
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 163847779  537 QRDLFGDERLAAVLRASHQHAPGDIVDAVLAAVREFTGDTPqTDDMTMVVIK 588
Cdd:TIGR02865 712 KEVEGKVLWLVRKLKETNTNDPEEIAEYLLEKAKELRSGKI-KDDMTVIVAK 762
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
195-381 2.39e-04

Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];


Pssm-ID: 226133 [Multi-domain]  Cd Length: 756  Bit Score: 42.78  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 195 DLEPTIQRLVRIGARLLDADACAFIEADEAGGRALLRACHGWELPTV-----------------SAWPLILDE--NHPHL 255
Cdd:COG3605   17 ELQEALDIIVRDIALAMVTEVCSVYLLRADRRVLELMATEGLNKPAVhlvqlafgeglvglvgrSAEPLNLADaqSHPSF 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 256 WYLPERSSQLAAdALMRLPILLRRQSfqghllapvelggvqIGLLMVNTINPRSFLDSEAELLGLLASQLAQMIDRERLy 335
Cdd:COG3605   97 KYLPETGEERYH-SFLGVPIIRRGRL---------------LGVLVVQQRELRQYDEDEVEFLVTLAMQLAEIVAQSQL- 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 163847779 336 QEALARQRLERELDLASEIQASflpdccPFVPGLQIEAFYQAARQV 381
Cdd:COG3605  160 TGATRGGYRELDLIRQTRIRGL------PAAPGVAIGEVVLHEPRP 199
 
Name Accession Description Interval E-value
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
401-589 2.23e-64

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: 284611  Cd Length: 190  Bit Score: 211.34  E-value: 2.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  401 RFGVVIADVTDKGVPAALFMALSRTLLRASAIDGRSPVAVLERANRLILADSRAGLFVTCFYALIDPATGRVTYANGGHN 480
Cdd:pfam07228   3 RVALVIGDVMGHGLPAALLMGMLRTALRALAAEGLDPAEVLKRLNRLLQRNLEEDMFATAVLAVYDPETGTLEYANAGHP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  481 YPLLYRQATGQVIPLAAQGIVLGIIPDPHFVPGEIVLDPGDILLFYTDGITEAMNPQRDLFGDERLAAVLRASHQHAPGD 560
Cdd:pfam07228  83 PPLLLRPDGGVVELLESTGLPLGILPDADYEVVELELEPGDTLLLYTDGLTEARDPDGELFGLERLLALLAERHGLPPEE 162
                         170       180
                  ....*....|....*....|....*....
gi 163847779  561 IVDAVLAAVREFtGDTPQTDDMTMVVIKR 589
Cdd:pfam07228 163 LLDALLEALLRL-GGGELEDDITLLVLRV 190
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
366-571 1.10e-50

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 174.46  E-value: 1.10e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779   366 VPGLQIEAFYQAARQVGGDFYDFIEIPAttpdgqSRFGVVIADVTDKGVPAALFMALSRTLLRASAIDGRSPVAVLERAN 445
Cdd:smart00331   1 DDGGLIAQYYEDATQVGGDFYDVVKLPE------GRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLN 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779   446 RLILADSRAGLFVTCFYALIDPATGRVTYANGGHNYPLLYRQATGQVIPLAAQGIVLGIIPDPHFVPGEIVLDPGDILLF 525
Cdd:smart00331  75 RAIYENGEDGMFATLFLALYDFAGGTLSYANAGHSPPYLLRADGGLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLLL 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 163847779   526 YTDGITEAMNPqrdlfgdERLAAVLRASHQHAPGDIVDAVLAAVRE 571
Cdd:smart00331 155 YTDGLTEARNP-------ERLEELLEELLGSPPAEIAQRILEELLE 193
GAF_2 pfam13185
GAF domain;
26-164 2.72e-11

GAF domain;


Pssm-ID: 289928  Cd Length: 140  Bit Score: 61.34  E-value: 2.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779   26 TLNLRSALDAALIHILELTGQEAGWIYLRDEGDQFI-LAARQRLPPALTYPGTIWQGECVCQEACRTGQirqePILMP-- 102
Cdd:pfam13185   1 ALDLEELLEAILEAAVELGASEFGFILLVDEDGRLLeLAAWGGPAEELGAELRRPPGEGLVGQALRTGR----PVIVNdl 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163847779  103 --CSRLRGAVGDKRGLTHHISVELRDSSRPVGILNLATTQWAKLEAVDQQLIAAIGDLLGTAIA 164
Cdd:pfam13185  77 aeDPRAKGLPAGHAGLKSLLSVPLVSDGRVIGVLALASREPGAFDEEDLELLELLAEQIAIAIE 140
FhlA COG2203
GAF domain [Signal transduction mechanisms];
178-341 1.63e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 225113  Cd Length: 175  Bit Score: 56.52  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 178 QERRALLSLSQELLVTDDLEPTIQRLVRIGARLLDADACAFIEADEAG---GRALLRACHGWELPTV-SAWPLILDENHP 253
Cdd:COG2203    1 SEEALLNELAAKIAQDLDLEEILQAALELLAELLGADRGLIYLLDEDGlldGALVAEAAEAGLEQLIdELFGLVILPACL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 254 HLWYLPERSSQLAADA-----LMRLPILLRRQSFQGHLLAPVELGGVQIGLLMV-NTINPRSFLDSEAELLGLLASQLAQ 327
Cdd:COG2203   81 IGIALREGRPVVVEDIlqdprFRDNPLVLLEPPIRSYLGVPLIAQGELLGLLCVhDSEPRRQWSEEELELLEELAEQVAI 160
                        170
                 ....*....|....
gi 163847779 328 MIDRERLYQEALAR 341
Cdd:COG2203  161 AIERARLYEELQEA 174
FhlA COG2203
GAF domain [Signal transduction mechanisms];
15-171 8.30e-09

GAF domain [Signal transduction mechanisms];


Pssm-ID: 225113  Cd Length: 175  Bit Score: 54.21  E-value: 8.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  15 ALRLLAQTLNQTLNLRSALDAALIHILELTGQEAGWIYLRDEGD----QFILAARQRLPPALTYP--GTIWQGECVCQEA 88
Cdd:COG2203    5 LLNELAAKIAQDLDLEEILQAALELLAELLGADRGLIYLLDEDGlldgALVAEAAEAGLEQLIDElfGLVILPACLIGIA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  89 CRTGQIR--QEPILMPCSRLRGAVGDKRGLTHHISVELRDSSRPVGILNLATTQWA-KLEAVDQQLIAAIGDLLGTAIAR 165
Cdd:COG2203   85 LREGRPVvvEDILQDPRFRDNPLVLLEPPIRSYLGVPLIAQGELLGLLCVHDSEPRrQWSEEELELLEELAEQVAIAIER 164

                 ....*.
gi 163847779 166 AHLYEE 171
Cdd:COG2203  165 ARLYEE 170
GAF_3 pfam13492
GAF domain;
195-331 1.33e-07

GAF domain;


Pssm-ID: 290227  Cd Length: 129  Bit Score: 50.05  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  195 DLEPTIQRLVRIGARLLDADACAFIEADEagGRALLRACHGWELPTVSAWPLILDENHPHLWYLP-ERSSQLAADALMRL 273
Cdd:pfam13492   1 SLDEILEALLKLLVDLLDAEVGAVYLLDE--DGLKLQVAAGWDGKPDPEEALDIDSLLARRALGSgEPISALGSAGEDNL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 163847779  274 PillrrqsFQGHLLAPVELGGVQIGLLMVNTINPRSFLDSEAELLGLLASQLAQMIDR 331
Cdd:pfam13492  79 P-------LGKALAVPLQTPDRVIGVLALYSPGPEAFDDEDLRLLKALARQIATAIEN 129
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
195-337 5.85e-07

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: 48.15  E-value: 5.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779   195 DLEPTIQRLVRIGARLLDADACAFIEADEAGGRAL-LRACHGWELPTVS-AWPLildeNHPHLWYL-----PERSSQLAA 267
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELvLVAADGLTLPTLGiRFPL----DEGLAGRVaetgrPLNIPDVEA 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163847779   268 DALMRLPILLRRQSFQGHLLAPVELGGVQIGLLMV-NTINPRSFLDSEAELLGLLASQLAQMIDRERLYQE 337
Cdd:smart00065  77 DPLFAEDLLGRYQGVRSFLAVPLVADGELVGVLALhNKKSPRPFTEEDEELLQALANQLAIALANAQLYEE 147
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
28-172 1.40e-04

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: 41.21  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779    28 NLRSALDAALIHILELTGQEAGWIYLRDEGDQFILAARQ-RLPPALTYPGTIWQGECVCQEACRTGQIRQEPILMPC-SR 105
Cdd:smart00065   1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELVLVAaDGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADpLF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163847779   106 LRGAVGDKRGLTHHISVELRDSSRPVGILNLA-TTQWAKLEAVDQQLIAAIGDLLGTAIARAHLYEEF 172
Cdd:smart00065  81 AEDLLGRYQGVRSFLAVPLVADGELVGVLALHnKKSPRPFTEEDEELLQALANQLAIALANAQLYEEL 148
GAF_3 pfam13492
GAF domain;
33-165 1.76e-04

GAF domain;


Pssm-ID: 290227  Cd Length: 129  Bit Score: 40.42  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779   33 LDAALIHILELTGQEAGWIYLRDEGDQFILAARQrLPPALTYPGTIWQGECVCQEAcrtgQIRQEPIlmpcSRLRGAVGD 112
Cdd:pfam13492   6 LEALLKLLVDLLDAEVGAVYLLDEDGLKLQVAAG-WDGKPDPEEALDIDSLLARRA----LGSGEPI----SALGSAGED 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 163847779  113 KRGLTHHISVELRDSSRPVGILNLATTQWAKLEAVDQQLIAAIGDLLGTAIAR 165
Cdd:pfam13492  77 NLPLGKALAVPLQTPDRVIGVLALYSPGPEAFDDEDLRLLKALARQIATAIEN 129
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
195-329 9.57e-04

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze 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 catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes 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: 279871  Cd Length: 133  Bit Score: 38.23  E-value: 9.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  195 DLEPTIQRLVRIGARLLDADACAFIEADEAG------GRALLRACHGWELPTVSAW------PLILDENHPHLWYLPERS 262
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGleylpaGARWLKAAGLEIPPGTGVTvlrtgrPLVVPDAAGDPRFLDPLL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163847779  263 sqlaadalmrlpiLLRRQSFQGHLLAPVELGGVQIGLLMVntINPRS-FLDSEAELLGLLASQLAQMI 329
Cdd:pfam01590  81 -------------LLRNLGIRSLLAVPIIDDGELLGVLVL--HHPRPpFTEEELELLEVLADQVAIAL 133
GAF_2 pfam13185
GAF domain;
193-330 5.86e-03

GAF domain;


Pssm-ID: 289928  Cd Length: 140  Bit Score: 36.30  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  193 TDDLEPTIQRLVRIGARLlDADACAFIEADEAGGRALLRACHGWELPTVSAWPLILDENHPHLWYLPERSSQLAADAL-- 270
Cdd:pfam13185   1 ALDLEELLEAILEAAVEL-GASEFGFILLVDEDGRLLELAAWGGPAEELGAELRRPPGEGLVGQALRTGRPVIVNDLAed 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163847779  271 -MRLPILLRRQSFQGHLLAPVELGGVQIGLLMVNTINPRSFLDSEAELLGLLASQLAQMID 330
Cdd:pfam13185  80 pRAKGLPAGHAGLKSLLSVPLVSDGRVIGVLALASREPGAFDEEDLELLELLAEQIAIAIE 140
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
320-590 9.50e-73

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


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 239.61  E-value: 9.50e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 320 LLASQLAQMIDRERLYQEALARQRLERELDLASEIQASFLPDCCPFVPGLQIEAFYQAARQVGGDFYDFIEIpattpdGQ 399
Cdd:COG2208  100 LVEINRAVGLVSAHNELLLLEQNNISAELEVARQIQQNLLPKALPLFPGIDIEAILVPASEVGGDYYDFIQL------GE 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 400 SRFGVVIADVTDKGVPAALFMALSRTLLRASAI-DGRSPVAVLERANRLILADSRAGLFVTCFYALIDPATGRVTYANGG 478
Cdd:COG2208  174 KRLRIGIGDVSGKGVPAALLMLMPKLALRLLLEsGPLDPADVLETLNRVLKQNLEEDMFVTLFLGVYDLDSGELTYSNAG 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 479 HNYPLLYRQAT-GQVIPLAAQGIVLGIIPDPHFVPGEIVLDPGDILLFYTDGITEAMNPQRDLFGDERLAAVLRASHQHA 557
Cdd:COG2208  254 HEPALILSADGeIEVEDLTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTEARNSDGEFFGLERLLKILGRLLGQP 333
                        250       260       270
                 ....*....|....*....|....*....|...
gi 163847779 558 PGDIVDAVLAAVREFTGDTPQTDDMTMVVIKRV 590
Cdd:COG2208  334 AEEILEAILESLEELQGDQIQDDDITLLVLKVK 366
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
380-588 1.26e-10

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: 274328 [Multi-domain]  Cd Length: 764  Bit Score: 62.79  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  380 QVGGDFYDFIEIpattpdGQSRFGVVIADVTDKGVPAAlfmALSRT---LLRASAIDGRSPVAVLERANRLILADSRAGL 456
Cdd:TIGR02865 565 LVSGDSYSFGKL------SAGKYAVAISDGMGSGPEAA---QESSAcvrLLEKFLESGFDREVAIKTVNSILSLRSTDEK 635
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779  457 FVTCFYALIDPATGRVTYANGGHNYPLLYRQatGQVIPLAAQGIVLGIIPDPHFVPGEIVLDPGDILLFYTDGITEAmnP 536
Cdd:TIGR02865 636 FSTLDLSVIDLYTGQAEFVKVGAVPSFIKRG--AKVEVIRSSNLPIGILDEVDVELVRKKLKNGDLIVMVSDGVLEG--E 711
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 163847779  537 QRDLFGDERLAAVLRASHQHAPGDIVDAVLAAVREFTGDTPqTDDMTMVVIK 588
Cdd:TIGR02865 712 KEVEGKVLWLVRKLKETNTNDPEEIAEYLLEKAKELRSGKI-KDDMTVIVAK 762
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
195-381 2.39e-04

Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];


Pssm-ID: 226133 [Multi-domain]  Cd Length: 756  Bit Score: 42.78  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 195 DLEPTIQRLVRIGARLLDADACAFIEADEAGGRALLRACHGWELPTV-----------------SAWPLILDE--NHPHL 255
Cdd:COG3605   17 ELQEALDIIVRDIALAMVTEVCSVYLLRADRRVLELMATEGLNKPAVhlvqlafgeglvglvgrSAEPLNLADaqSHPSF 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163847779 256 WYLPERSSQLAAdALMRLPILLRRQSfqghllapvelggvqIGLLMVNTINPRSFLDSEAELLGLLASQLAQMIDRERLy 335
Cdd:COG3605   97 KYLPETGEERYH-SFLGVPIIRRGRL---------------LGVLVVQQRELRQYDEDEVEFLVTLAMQLAEIVAQSQL- 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 163847779 336 QEALARQRLERELDLASEIQASflpdccPFVPGLQIEAFYQAARQV 381
Cdd:COG3605  160 TGATRGGYRELDLIRQTRIRGL------PAAPGVAIGEVVLHEPRP 199
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • 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, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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