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Conserved domains on  [gi|57116853|ref|YP_177802|]
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sigma factor regulatory protein [Mycobacterium tuberculosis H37Rv]

Protein Classification

RsbW and STAS_anti-anti-sigma_factors domain-containing protein (domain architecture ID 11799363)

protein containing domains PAS, RsbU, RsbW, and STAS_anti-anti-sigma_factors

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RsbU super family cl26706
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
133-397 9.59e-40

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


The actual alignment was detected with superfamily member COG2208:

Pssm-ID: 331527  Cd Length: 367  Bit Score: 150.24  E-value: 9.59e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 133 RVRARQAAEARVEELSERYRNVRDSATV---MQQALLAASVPVVPGADIAAEYLVAAEdtaAGGDWFDALALGD-RLVLV 208
Cdd:COG2208 103 INRAVGLVSAHNELLLLEQNNISAELEVarqIQQNLLPKALPLFPGIDIEAILVPASE---VGGDYYDFIQLGEkRLRIG 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 209 VGDVVGHGVEAAAVMSQLRTALRMQISAG-YTVVEALEAVDRFHKQV-PGSKSATMCVGSLDFTSGEFQYCTAGHPPPLL 286
Cdd:COG2208 180 IGDVSGKGVPAALLMLMPKLALRLLLESGpLDPADVLETLNRVLKQNlEEDMFVTLFLGVYDLDSGELTYSNAGHEPALI 259
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 287 VTADASA---RYVEPTGAGPLGSGTGFPVRSEVLNIGDAILFYTDGLIErpgrpLEASTAEFADLAASIASGSGgfVLDA 363
Cdd:COG2208 260 LSADGEIeveDLTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTE-----ARNSDGEFFGLERLLKILGR--LLGQ 332
                       250       260       270
                ....*....|....*....|....*....|....
gi 57116853 364 PARPIDRLCSDTLELLLRSTGYNDDVTLLAMQRR 397
Cdd:COG2208 333 PAEEILEAILESLEELQGDQIQDDDITLLVLKVK 366
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
401-541 5.02e-23

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


:

Pssm-ID: 225083  Cd Length: 146  Bit Score: 97.06  E-value: 5.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 401 PPLHIT---LDATINAARTVRAQLREWLAEIGADHSDIADIVHAISEFVENAVEHGYATDVSKGIVVAAALAGDGNVRAS 477
Cdd:COG2172   1 MTNHITdlvLPAKLSAVGTARLTLREFARELGLTYVDIADLAIAVSEALTNAVKHAYKLDPSEGEIRIEVSLDDGKLEIR 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57116853 478 VIDRGqwKDHRDGARGRGRGLAMAEALVSEARIMHGAGGTTATLTHRLSRPAR--FVTDTMVRRAA 541
Cdd:COG2172  81 IWDQG--PGIEDLEESLGPGDTTAEGLQEGGLGLFLAKRLMDEFSYERSEDGRnrLTKITLRKRLA 144
SpoIIAA COG1366
Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction ...
544-653 2.82e-13

Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction mechanisms];


:

Pssm-ID: 224285  Cd Length: 117  Bit Score: 68.21  E-value: 2.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 544 QTIDSEFVSLVESGRIV-VRGDVDSTTAATLDRQIAVESR-SGIAPVTIDLSAVTHLGSAGVGALAAACDRARKQGTECV 621
Cdd:COG1366   1 MELSIPIIKIVDGILVLpLIGELDAARAPALKETLLEVIAaSGARGLVIDLSGVDFMDSAGLGVLVALLKSARLRGVELV 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 57116853 622 LVAPPGSPAHHVLSLVQLPV-VGADTEDIFAQE 653
Cdd:COG1366  81 LVGIQPEVARTLELTGLDKSfIITPTELEAALA 113
PAS super family cl25988
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
18-139 2.92e-09

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.


The actual alignment was detected with superfamily member TIGR00229:

Pssm-ID: 330809  Cd Length: 124  Bit Score: 56.53  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853    18 RRIFEHIPA--ILVGLEGpdhRFVAVNAAYR---GFSPLlDTVGQPAREVYPELEGQQIYEMLDRvYQTGEPQSGSEWRL 92
Cdd:TIGR00229   6 RAIFESSPDaiIVIDLEG---NILYVNPAFEeifGYSAE-ELIGRNVLELIPEEDREEVRERIER-RLEGEPEPVSEERR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 57116853    93 QTDYDGSgveERYFDFVVTPRRrADGSIEGVQLIVDDVTSRVRARQA 139
Cdd:TIGR00229  81 VRRKDGS---EIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEA 123
 
Name Accession Description Interval E-value
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
133-397 9.59e-40

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


Pssm-ID: 225118  Cd Length: 367  Bit Score: 150.24  E-value: 9.59e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 133 RVRARQAAEARVEELSERYRNVRDSATV---MQQALLAASVPVVPGADIAAEYLVAAEdtaAGGDWFDALALGD-RLVLV 208
Cdd:COG2208 103 INRAVGLVSAHNELLLLEQNNISAELEVarqIQQNLLPKALPLFPGIDIEAILVPASE---VGGDYYDFIQLGEkRLRIG 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 209 VGDVVGHGVEAAAVMSQLRTALRMQISAG-YTVVEALEAVDRFHKQV-PGSKSATMCVGSLDFTSGEFQYCTAGHPPPLL 286
Cdd:COG2208 180 IGDVSGKGVPAALLMLMPKLALRLLLESGpLDPADVLETLNRVLKQNlEEDMFVTLFLGVYDLDSGELTYSNAGHEPALI 259
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 287 VTADASA---RYVEPTGAGPLGSGTGFPVRSEVLNIGDAILFYTDGLIErpgrpLEASTAEFADLAASIASGSGgfVLDA 363
Cdd:COG2208 260 LSADGEIeveDLTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTE-----ARNSDGEFFGLERLLKILGR--LLGQ 332
                       250       260       270
                ....*....|....*....|....*....|....
gi 57116853 364 PARPIDRLCSDTLELLLRSTGYNDDVTLLAMQRR 397
Cdd:COG2208 333 PAEEILEAILESLEELQGDQIQDDDITLLVLKVK 366
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
216-396 1.48e-30

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: 119.66  E-value: 1.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853   216 GVEAAAVMSQLRTALRMQISAGYTVVEALEAVDRF-HKQVPGSKSATMCVGSLDFTSGEFQYCTAGHPPPLLVTADASAR 294
Cdd:pfam07228  15 GLPAALLMGMLRTALRALAAEGLDPAEVLKRLNRLlQRNLEEDMFATAVLAVYDPETGTLEYANAGHPPPLLLRPDGGVV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853   295 YVEPTGAGPLG--SGTGFPVRSEVLNIGDAILFYTDGLIERpgRPLEASTAEFADLAASIASgsggfvldAPARPIDRLC 372
Cdd:pfam07228  95 ELLESTGLPLGilPDADYEVVELELEPGDTLLLYTDGLTEA--RDPDGELFGLERLLALLAE--------RHGLPPEELL 164
                         170       180
                  ....*....|....*....|....*.
gi 57116853   373 SDTLELLLRSTGYN--DDVTLLAMQR 396
Cdd:pfam07228 165 DALLEALLRLGGGEleDDITLLVLRV 190
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
173-332 6.12e-26

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 106.66  E-value: 6.12e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853    173 VPGADIAAEYLvaaEDTAAGGDWFDALALGD-RLVLVVGDVVGHGVEAAAVMSQLRTALRMQISAGYTVVEALEAVDR-F 250
Cdd:smart00331   1 DDGGLIAQYYE---DATQVGGDFYDVVKLPEgRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRaI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853    251 HKQVPGSKSATMCVGSLDFTSGEFQYCTAGHPPPLLVTADasARYVEPTGA--GPLGSGTGFP--VRSEVLNIGDAILFY 326
Cdd:smart00331  78 YENGEDGMFATLFLALYDFAGGTLSYANAGHSPPYLLRAD--GGLVEDLDDlgAPLGLEPDVEvdVRELTLEPGDLLLLY 155

                   ....*.
gi 57116853    327 TDGLIE 332
Cdd:smart00331 156 TDGLTE 161
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
401-541 5.02e-23

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


Pssm-ID: 225083  Cd Length: 146  Bit Score: 97.06  E-value: 5.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 401 PPLHIT---LDATINAARTVRAQLREWLAEIGADHSDIADIVHAISEFVENAVEHGYATDVSKGIVVAAALAGDGNVRAS 477
Cdd:COG2172   1 MTNHITdlvLPAKLSAVGTARLTLREFARELGLTYVDIADLAIAVSEALTNAVKHAYKLDPSEGEIRIEVSLDDGKLEIR 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57116853 478 VIDRGqwKDHRDGARGRGRGLAMAEALVSEARIMHGAGGTTATLTHRLSRPAR--FVTDTMVRRAA 541
Cdd:COG2172  81 IWDQG--PGIEDLEESLGPGDTTAEGLQEGGLGLFLAKRLMDEFSYERSEDGRnrLTKITLRKRLA 144
SpoIIAA COG1366
Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction ...
544-653 2.82e-13

Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction mechanisms];


Pssm-ID: 224285  Cd Length: 117  Bit Score: 68.21  E-value: 2.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 544 QTIDSEFVSLVESGRIV-VRGDVDSTTAATLDRQIAVESR-SGIAPVTIDLSAVTHLGSAGVGALAAACDRARKQGTECV 621
Cdd:COG1366   1 MELSIPIIKIVDGILVLpLIGELDAARAPALKETLLEVIAaSGARGLVIDLSGVDFMDSAGLGVLVALLKSARLRGVELV 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 57116853 622 LVAPPGSPAHHVLSLVQLPV-VGADTEDIFAQE 653
Cdd:COG1366  81 LVGIQPEVARTLELTGLDKSfIITPTELEAALA 113
STAS pfam01740
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
551-632 7.59e-12

STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding function.


Pssm-ID: 307726  Cd Length: 106  Bit Score: 63.79  E-value: 7.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853   551 VSLVESGRIVV---RGDVDSTTAATLDRQIA-VESRSGIAPVTIDLSAVTHLGSAGVGALAAACDRARKQGTECVLVAPP 626
Cdd:pfam01740   2 PEAEEIDGILIlrlDGPLDFANAESLRERLLrALEEGEIRHVVLDLSAVPFIDSSGLGVLVELYKELRRRGVELVLVGPS 81

                  ....*.
gi 57116853   627 GSPAHH 632
Cdd:pfam01740  82 PEVART 87
STAS_anti-anti-sigma_factors cd07043
Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key ...
559-639 7.88e-12

Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key regulators of anti-sigma factors by phosphorylation; Anti-anti-sigma factors play an important role in the regulation of several sigma factors and their corresponding anti-sigma factors. Upon dephosphorylation they bind the anti-sigma factor and induce the release of the sigma factor from the anti-sigma factor. In a feedback mechanism the anti-anti-sigma factor can be inactivated via phosphorylation by the anti-sigma factor. Well studied examples from Bacillus subtilis are SpoIIAA (regulating sigmaF and sigmaC which play an important role in sporulation) and RsbV (regulating sigmaB involved in the general stress response). The STAS domain is also found in the C- terminal region of sulphate transporters and stressosomes.


Pssm-ID: 132914  Cd Length: 99  Bit Score: 63.69  E-value: 7.88e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 559 IVVRGDVDSTTAATLDRQIAVESRSGIAPVTIDLSAVTHLGSAGVGALAAACDRARKQGTECVLVAPPGsPAHHVLSLVQ 638
Cdd:cd07043  12 VRLSGELDAATAPELREALEELLAEGPRRLVLDLSGVTFIDSSGLGVLLGAYKRARAAGGRLVLVNVSP-AVRRVLELTG 90

                .
gi 57116853 639 L 639
Cdd:cd07043  91 L 91
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
407-522 3.10e-10

Histidine kinase-like ATPase domain;


Pssm-ID: 316137  Cd Length: 126  Bit Score: 59.23  E-value: 3.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853   407 LDATINAARTVRAQLREWLAEIGADHSDIADIVHAISEFVENAVEHGYATDVSKGIVVAAALAGDGnVRASVIDRGQWKD 486
Cdd:pfam13581   1 FPADLEQLRTARRVLAAVLRRAGLSEELLDEVELAVGEACTNAVRHAYREGPGGPVRVRLTLDGGA-LTVEVADSGPPFD 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 57116853   487 HRDGARGRGRG----------LAMAEALVSEARIMHGAGGTTATLT 522
Cdd:pfam13581  80 PLAAPPPDVTPeedrpeggrgLFLIRGLMDDVEYRRGPGGNTLTLR 125
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
18-139 2.92e-09

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


Pssm-ID: 272971  Cd Length: 124  Bit Score: 56.53  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853    18 RRIFEHIPA--ILVGLEGpdhRFVAVNAAYR---GFSPLlDTVGQPAREVYPELEGQQIYEMLDRvYQTGEPQSGSEWRL 92
Cdd:TIGR00229   6 RAIFESSPDaiIVIDLEG---NILYVNPAFEeifGYSAE-ELIGRNVLELIPEEDREEVRERIER-RLEGEPEPVSEERR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 57116853    93 QTDYDGSgveERYFDFVVTPRRrADGSIEGVQLIVDDVTSRVRARQA 139
Cdd:TIGR00229  81 VRRKDGS---EIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEA 123
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
21-135 2.30e-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: 312075  Cd Length: 110  Bit Score: 53.57  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853    21 FEHIPAILVGLeGPDHRFVAVNAAYRGFS--PLLDTVGQPAREVYPELEGQQIYEMLDRVYQTGEPQSGsewrlQTDYDG 98
Cdd:pfam08448   1 LDSLPDALAVL-DPDGRVRYANAAAAELFglPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDF-----LEELLL 74
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 57116853    99 SGvEERYFDFVVTPRRRADGSIEGVQLIVDDVTSRVR 135
Cdd:pfam08448  75 NG-EERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
34-130 1.16e-04

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  Cd Length: 103  Bit Score: 42.24  E-value: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853  34 PDHRFVAVNAAYR---GFSPLlDTVGQPAREVYPELEGQQIYEMLDRVYQTGEPQSgSEWRLQTdYDGSgveERYFDFVV 110
Cdd:cd00130  10 LDGRILYANPAAEqllGYSPE-ELIGKSLLDLIHPEDREELRERLENLLSGGEPVT-LEVRLRR-KDGS---VIWVLVSL 83
                        90       100
                ....*....|....*....|
gi 57116853 111 TPRRRADGSIEGVQLIVDDV 130
Cdd:cd00130  84 TPIRDEGGEVIGLLGVVRDI 103
ant_ant_sig TIGR00377
anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to ...
561-625 1.90e-04

anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to SpoIIAA of Bacillus subtilis, an anti-anti-sigma factor. SpoIIAA can bind to and inhibit the anti-sigma F factor SpoIIAB. Also, it can be phosphorylated by SpoIIAB on a Ser residue at position 59 of the seed alignment. A similar arrangement is inferred for RsbV, an anti-anti-sigma factor for sigma B. This Ser is fairly well conserved within a motif resembling MXS[STA]G[VIL]X[VIL][VILF] among homologous known or predicted anti-anti-sigma factors. Regions similar to SpoIIAA and apparently homologous, but differing considerably near the phosphorlated Ser of SpoIIAA, appear in a single copy in several longer proteins. [Regulatory functions, Protein interactions]


Pssm-ID: 273042  Cd Length: 108  Bit Score: 41.44  E-value: 1.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57116853   561 VRGDVDSTTAATLDRQI-AVESRSGIAPVTIDLSAVTHLGSAGVGALAAACDRARKQGTECVLVAP 625
Cdd:TIGR00377  18 LSGELDAHTAPLLREKVtPAAERTGIRPIVLDLEDLEFMDSSGLGVLLGRYKQVRRVGGQLVLVSV 83
PRK03660 PRK03660
anti-sigma F factor; Provisional
434-482 3.70e-03

anti-sigma F factor; Provisional


Pssm-ID: 179626  Cd Length: 146  Bit Score: 37.99  E-value: 3.70e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 57116853  434 DIADIVHAISEFVENAVEHGYATDVSKGIVVAAALAGDGnVRASVIDRG 482
Cdd:PRK03660  36 ELTEIKTAVSEAVTNAIIHGYENNPDGVVYIEVEIEEEE-LEITVRDEG 83
spIIAB TIGR01925
anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates ...
418-482 8.80e-03

anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates spore development in B subtilis. SpoIIAB binds to sigma F, preventing formation of the transcription complex at the promoter. SpoIIAA (anti-anti-sigma F factor) binds to SpoIIAB to inhibit association with sigma F, however SpoIIAB can phosphorylate SpoIIAA, causing disassociation of the SpoIIAA/B complex. The SpoIIE phosphatase dephosphorylates SpoIIAA. [Regulatory functions, Protein interactions, Cellular processes, Sporulation and germination]


Pssm-ID: 130980  Cd Length: 137  Bit Score: 36.82  E-value: 8.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57116853   418 RAQLREWLAEIGADHSDIADIVHAISEFVENAVEHGYATDVSKGIVVAAALAgDGNVRASVIDRG 482
Cdd:TIGR01925  20 RVTVASFIAQLDPTMEELTDIKTAVSEAVTNAIIHGYEENCEGVVYISATIE-DHEVYITVRDEG 83
 
Name Accession Description Interval E-value
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
133-397 9.59e-40

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


Pssm-ID: 225118  Cd Length: 367  Bit Score: 150.24  E-value: 9.59e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 133 RVRARQAAEARVEELSERYRNVRDSATV---MQQALLAASVPVVPGADIAAEYLVAAEdtaAGGDWFDALALGD-RLVLV 208
Cdd:COG2208 103 INRAVGLVSAHNELLLLEQNNISAELEVarqIQQNLLPKALPLFPGIDIEAILVPASE---VGGDYYDFIQLGEkRLRIG 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 209 VGDVVGHGVEAAAVMSQLRTALRMQISAG-YTVVEALEAVDRFHKQV-PGSKSATMCVGSLDFTSGEFQYCTAGHPPPLL 286
Cdd:COG2208 180 IGDVSGKGVPAALLMLMPKLALRLLLESGpLDPADVLETLNRVLKQNlEEDMFVTLFLGVYDLDSGELTYSNAGHEPALI 259
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 287 VTADASA---RYVEPTGAGPLGSGTGFPVRSEVLNIGDAILFYTDGLIErpgrpLEASTAEFADLAASIASGSGgfVLDA 363
Cdd:COG2208 260 LSADGEIeveDLTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTE-----ARNSDGEFFGLERLLKILGR--LLGQ 332
                       250       260       270
                ....*....|....*....|....*....|....
gi 57116853 364 PARPIDRLCSDTLELLLRSTGYNDDVTLLAMQRR 397
Cdd:COG2208 333 PAEEILEAILESLEELQGDQIQDDDITLLVLKVK 366
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
216-396 1.48e-30

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: 119.66  E-value: 1.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853   216 GVEAAAVMSQLRTALRMQISAGYTVVEALEAVDRF-HKQVPGSKSATMCVGSLDFTSGEFQYCTAGHPPPLLVTADASAR 294
Cdd:pfam07228  15 GLPAALLMGMLRTALRALAAEGLDPAEVLKRLNRLlQRNLEEDMFATAVLAVYDPETGTLEYANAGHPPPLLLRPDGGVV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853   295 YVEPTGAGPLG--SGTGFPVRSEVLNIGDAILFYTDGLIERpgRPLEASTAEFADLAASIASgsggfvldAPARPIDRLC 372
Cdd:pfam07228  95 ELLESTGLPLGilPDADYEVVELELEPGDTLLLYTDGLTEA--RDPDGELFGLERLLALLAE--------RHGLPPEELL 164
                         170       180
                  ....*....|....*....|....*.
gi 57116853   373 SDTLELLLRSTGYN--DDVTLLAMQR 396
Cdd:pfam07228 165 DALLEALLRLGGGEleDDITLLVLRV 190
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
173-332 6.12e-26

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 106.66  E-value: 6.12e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853    173 VPGADIAAEYLvaaEDTAAGGDWFDALALGD-RLVLVVGDVVGHGVEAAAVMSQLRTALRMQISAGYTVVEALEAVDR-F 250
Cdd:smart00331   1 DDGGLIAQYYE---DATQVGGDFYDVVKLPEgRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRaI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853    251 HKQVPGSKSATMCVGSLDFTSGEFQYCTAGHPPPLLVTADasARYVEPTGA--GPLGSGTGFP--VRSEVLNIGDAILFY 326
Cdd:smart00331  78 YENGEDGMFATLFLALYDFAGGTLSYANAGHSPPYLLRAD--GGLVEDLDDlgAPLGLEPDVEvdVRELTLEPGDLLLLY 155

                   ....*.
gi 57116853    327 TDGLIE 332
Cdd:smart00331 156 TDGLTE 161
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
401-541 5.02e-23

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


Pssm-ID: 225083  Cd Length: 146  Bit Score: 97.06  E-value: 5.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 401 PPLHIT---LDATINAARTVRAQLREWLAEIGADHSDIADIVHAISEFVENAVEHGYATDVSKGIVVAAALAGDGNVRAS 477
Cdd:COG2172   1 MTNHITdlvLPAKLSAVGTARLTLREFARELGLTYVDIADLAIAVSEALTNAVKHAYKLDPSEGEIRIEVSLDDGKLEIR 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57116853 478 VIDRGqwKDHRDGARGRGRGLAMAEALVSEARIMHGAGGTTATLTHRLSRPAR--FVTDTMVRRAA 541
Cdd:COG2172  81 IWDQG--PGIEDLEESLGPGDTTAEGLQEGGLGLFLAKRLMDEFSYERSEDGRnrLTKITLRKRLA 144
SpoIIAA COG1366
Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction ...
544-653 2.82e-13

Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction mechanisms];


Pssm-ID: 224285  Cd Length: 117  Bit Score: 68.21  E-value: 2.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 544 QTIDSEFVSLVESGRIV-VRGDVDSTTAATLDRQIAVESR-SGIAPVTIDLSAVTHLGSAGVGALAAACDRARKQGTECV 621
Cdd:COG1366   1 MELSIPIIKIVDGILVLpLIGELDAARAPALKETLLEVIAaSGARGLVIDLSGVDFMDSAGLGVLVALLKSARLRGVELV 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 57116853 622 LVAPPGSPAHHVLSLVQLPV-VGADTEDIFAQE 653
Cdd:COG1366  81 LVGIQPEVARTLELTGLDKSfIITPTELEAALA 113
STAS pfam01740
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
551-632 7.59e-12

STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding function.


Pssm-ID: 307726  Cd Length: 106  Bit Score: 63.79  E-value: 7.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853   551 VSLVESGRIVV---RGDVDSTTAATLDRQIA-VESRSGIAPVTIDLSAVTHLGSAGVGALAAACDRARKQGTECVLVAPP 626
Cdd:pfam01740   2 PEAEEIDGILIlrlDGPLDFANAESLRERLLrALEEGEIRHVVLDLSAVPFIDSSGLGVLVELYKELRRRGVELVLVGPS 81

                  ....*.
gi 57116853   627 GSPAHH 632
Cdd:pfam01740  82 PEVART 87
STAS_anti-anti-sigma_factors cd07043
Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key ...
559-639 7.88e-12

Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key regulators of anti-sigma factors by phosphorylation; Anti-anti-sigma factors play an important role in the regulation of several sigma factors and their corresponding anti-sigma factors. Upon dephosphorylation they bind the anti-sigma factor and induce the release of the sigma factor from the anti-sigma factor. In a feedback mechanism the anti-anti-sigma factor can be inactivated via phosphorylation by the anti-sigma factor. Well studied examples from Bacillus subtilis are SpoIIAA (regulating sigmaF and sigmaC which play an important role in sporulation) and RsbV (regulating sigmaB involved in the general stress response). The STAS domain is also found in the C- terminal region of sulphate transporters and stressosomes.


Pssm-ID: 132914  Cd Length: 99  Bit Score: 63.69  E-value: 7.88e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 559 IVVRGDVDSTTAATLDRQIAVESRSGIAPVTIDLSAVTHLGSAGVGALAAACDRARKQGTECVLVAPPGsPAHHVLSLVQ 638
Cdd:cd07043  12 VRLSGELDAATAPELREALEELLAEGPRRLVLDLSGVTFIDSSGLGVLLGAYKRARAAGGRLVLVNVSP-AVRRVLELTG 90

                .
gi 57116853 639 L 639
Cdd:cd07043  91 L 91
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
407-522 3.10e-10

Histidine kinase-like ATPase domain;


Pssm-ID: 316137  Cd Length: 126  Bit Score: 59.23  E-value: 3.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853   407 LDATINAARTVRAQLREWLAEIGADHSDIADIVHAISEFVENAVEHGYATDVSKGIVVAAALAGDGnVRASVIDRGQWKD 486
Cdd:pfam13581   1 FPADLEQLRTARRVLAAVLRRAGLSEELLDEVELAVGEACTNAVRHAYREGPGGPVRVRLTLDGGA-LTVEVADSGPPFD 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 57116853   487 HRDGARGRGRG----------LAMAEALVSEARIMHGAGGTTATLT 522
Cdd:pfam13581  80 PLAAPPPDVTPeedrpeggrgLFLIRGLMDDVEYRRGPGGNTLTLR 125
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
18-139 2.92e-09

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


Pssm-ID: 272971  Cd Length: 124  Bit Score: 56.53  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853    18 RRIFEHIPA--ILVGLEGpdhRFVAVNAAYR---GFSPLlDTVGQPAREVYPELEGQQIYEMLDRvYQTGEPQSGSEWRL 92
Cdd:TIGR00229   6 RAIFESSPDaiIVIDLEG---NILYVNPAFEeifGYSAE-ELIGRNVLELIPEEDREEVRERIER-RLEGEPEPVSEERR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 57116853    93 QTDYDGSgveERYFDFVVTPRRrADGSIEGVQLIVDDVTSRVRARQA 139
Cdd:TIGR00229  81 VRRKDGS---EIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEA 123
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
21-135 2.30e-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: 312075  Cd Length: 110  Bit Score: 53.57  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853    21 FEHIPAILVGLeGPDHRFVAVNAAYRGFS--PLLDTVGQPAREVYPELEGQQIYEMLDRVYQTGEPQSGsewrlQTDYDG 98
Cdd:pfam08448   1 LDSLPDALAVL-DPDGRVRYANAAAAELFglPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDF-----LEELLL 74
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 57116853    99 SGvEERYFDFVVTPRRRADGSIEGVQLIVDDVTSRVR 135
Cdd:pfam08448  75 NG-EERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
STAS_2 pfam13466
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
559-639 4.33e-06

STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C-terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding function.


Pssm-ID: 316027  Cd Length: 80  Bit Score: 46.45  E-value: 4.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853   559 IVVRGDVDSTTAATLDRQIAVESRSGiAPVTIDLSAVTHLGSAGVGALAAACDRARKQGTECVLVAPPGspahHVLSLVQ 638
Cdd:pfam13466   1 LRLSGELDRDTAPALRAQLLAALAAG-SPVVVDLSGVERVDSAGLALLLALARRARARGKRLVLRGVPP----ALRRLLD 75

                  .
gi 57116853   639 L 639
Cdd:pfam13466  76 L 76
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
34-130 1.16e-04

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  Cd Length: 103  Bit Score: 42.24  E-value: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853  34 PDHRFVAVNAAYR---GFSPLlDTVGQPAREVYPELEGQQIYEMLDRVYQTGEPQSgSEWRLQTdYDGSgveERYFDFVV 110
Cdd:cd00130  10 LDGRILYANPAAEqllGYSPE-ELIGKSLLDLIHPEDREELRERLENLLSGGEPVT-LEVRLRR-KDGS---VIWVLVSL 83
                        90       100
                ....*....|....*....|
gi 57116853 111 TPRRRADGSIEGVQLIVDDV 130
Cdd:cd00130  84 TPIRDEGGEVIGLLGVVRDI 103
ant_ant_sig TIGR00377
anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to ...
561-625 1.90e-04

anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to SpoIIAA of Bacillus subtilis, an anti-anti-sigma factor. SpoIIAA can bind to and inhibit the anti-sigma F factor SpoIIAB. Also, it can be phosphorylated by SpoIIAB on a Ser residue at position 59 of the seed alignment. A similar arrangement is inferred for RsbV, an anti-anti-sigma factor for sigma B. This Ser is fairly well conserved within a motif resembling MXS[STA]G[VIL]X[VIL][VILF] among homologous known or predicted anti-anti-sigma factors. Regions similar to SpoIIAA and apparently homologous, but differing considerably near the phosphorlated Ser of SpoIIAA, appear in a single copy in several longer proteins. [Regulatory functions, Protein interactions]


Pssm-ID: 273042  Cd Length: 108  Bit Score: 41.44  E-value: 1.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57116853   561 VRGDVDSTTAATLDRQI-AVESRSGIAPVTIDLSAVTHLGSAGVGALAAACDRARKQGTECVLVAP 625
Cdd:TIGR00377  18 LSGELDAHTAPLLREKVtPAAERTGIRPIVLDLEDLEFMDSSGLGVLLGRYKQVRRVGGQLVLVSV 83
MlaB COG3113
ABC-type transporter Mla maintaining outer membrane lipid asymmetry, MlaB component, contains ...
560-639 9.67e-04

ABC-type transporter Mla maintaining outer membrane lipid asymmetry, MlaB component, contains STAS domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225655  Cd Length: 99  Bit Score: 39.24  E-value: 9.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116853 560 VVRGDVDSTTAATLDRQIAVESrSGIAPVTIDLSAVTHLGSAGVGALAAACDRARKQGTECVLVAPPGSpahhVLSLVQL 639
Cdd:COG3113  15 VLSGELDRDTLLPLWSQREAQL-KQLDTVRIDLSGVSRVDSAGLALLLHLIRLAKKQGNAVTLTGVPEQ----LRTLAEL 89
PRK03660 PRK03660
anti-sigma F factor; Provisional
434-482 3.70e-03

anti-sigma F factor; Provisional


Pssm-ID: 179626  Cd Length: 146  Bit Score: 37.99  E-value: 3.70e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 57116853  434 DIADIVHAISEFVENAVEHGYATDVSKGIVVAAALAGDGnVRASVIDRG 482
Cdd:PRK03660  36 ELTEIKTAVSEAVTNAIIHGYENNPDGVVYIEVEIEEEE-LEITVRDEG 83
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
434-482 5.54e-03

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: 308236  Cd Length: 109  Bit Score: 36.96  E-value: 5.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 57116853   434 DIADIVHAISEFVENAVEHGYATDVSkgIVVAAAlagDGNVRASVIDRG 482
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAKAGEIT--VTLSAD---GGDLELTVEDNG 45
STAS_SulP_like_sulfate_transporter cd07042
Sulphate Transporter and Anti-Sigma factor antagonist domain of SulP-like sulfate transporters, ...
569-629 7.02e-03

Sulphate Transporter and Anti-Sigma factor antagonist domain of SulP-like sulfate transporters, plays a role in the function and regulation of the transport activity, proposed general NTP binding function; The SulP family is a large and diverse family of anion transporters, with members from eubacteria, plants, fungi, and mammals. They contain 10 to 14 transmembrane helices which form the catalytic core of the protein and a C-terminal extension, the STAS (Sulphate Transporter and AntiSigma factor antagonist) domain which plays a role in the function and regulation of the transport activity. The STAS domain is found in the C-terminal region of sulphate transporters and bacterial anti-sigma factor antagonists. It has been suggested that this domain may have a general NTP binding function.


Pssm-ID: 132913  Cd Length: 107  Bit Score: 36.45  E-value: 7.02e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57116853 569 TAATLDRQI--AVESRSGIAPVTIDLSAVTHLGSAGVGALAAACDRARKQGTECVLVAPPGSP 629
Cdd:cd07042  23 NAEYFKDRLlrLVDEDPPLKVVILDLSAVNFIDSTAAEALEELVKDLRKRGVELYLAGLNPQV 85
spIIAB TIGR01925
anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates ...
418-482 8.80e-03

anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates spore development in B subtilis. SpoIIAB binds to sigma F, preventing formation of the transcription complex at the promoter. SpoIIAA (anti-anti-sigma F factor) binds to SpoIIAB to inhibit association with sigma F, however SpoIIAB can phosphorylate SpoIIAA, causing disassociation of the SpoIIAA/B complex. The SpoIIE phosphatase dephosphorylates SpoIIAA. [Regulatory functions, Protein interactions, Cellular processes, Sporulation and germination]


Pssm-ID: 130980  Cd Length: 137  Bit Score: 36.82  E-value: 8.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57116853   418 RAQLREWLAEIGADHSDIADIVHAISEFVENAVEHGYATDVSKGIVVAAALAgDGNVRASVIDRG 482
Cdd:TIGR01925  20 RVTVASFIAQLDPTMEELTDIKTAVSEAVTNAIIHGYEENCEGVVYISATIE-DHEVYITVRDEG 83
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
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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