NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|29826978|ref|NP_821612|]
View 

magnesium or manganese-dependent protein phosphatase [Streptomyces avermitilis MA-4680 = NBRC 14893]

Graphical summary

show options »

Show site features     Horizontal zoom: ×

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 ...
21-105 2.00e-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 [Multi-domain]  Cd Length: 103  Bit Score: 40.69  E-value: 2.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978  21 VLLDACGRVAAWGPGAQQMLGCPAREAVGRSADEFLyDPADAADIVRRWEKGARRGSLV-----LRQRSGKPLAAQIWVR 95
Cdd:cd00130   6 IVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLI-HPEDREELRERLENLLSGGEPVtlevrLRRKDGSVIWVLVSLT 84
                        90
                ....*....|
gi 29826978  96 ALTSANGDPQ 105
Cdd:cd00130  85 PIRDEGGEVI 94
HATPase_c cd00075
Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: ...
726-790 1.73e-03

Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: histidine kinase, DNA gyrase B, topoisomerases, heat shock protein HSP90, phytochrome-like ATPases and DNA mismatch repair proteins


:

Pssm-ID: 238030  Cd Length: 103  Bit Score: 37.63  E-value: 1.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978 726 IVSELVTNAIRYGEEP---ITLRLILDRN-VICEVSD-GSSTSP---------HVRRAQDTDEGGR--GLYLITQLTRSW 789
Cdd:cd00075   4 VLLNLLSNAIKHTPEGggrITISVERDGDhLEIRVEDnGPGIPEedleriferFSDGSRSRKGGGTglGLSIVKKLVELH 83

                .
gi 29826978 790 G 790
Cdd:cd00075  84 G 84
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
487-680 4.08e-44

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: 157.84  E-value: 4.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   487 SGARVALVVGDVTGHDLQSAVTMGRLRSAVRTLADLDLAPDELLTHLDDQMNRFLDErsdegplATGATCLYAVYDPVSR 566
Cdd:pfam07228   1 PDGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRNLEG-------ERFATAVLAVYDPETG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   567 RCLLARAGHPPPAVLSVNGAVDFVELPGGPPL-GLGGIVFEKREIAMDDGDVLVLYTNGLLQprAQDLDAGLHRMRDTLS 645
Cdd:pfam07228  74 TLEYANAGHPPPLLLRPDGGVVELLESPGLPLgVLPDAPYETAEFPLEPGDTLLLYTDGLTE--ARDPDGELFGLERLLA 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 29826978   646 --RTPPSATPQEVCDTLVRELLPTC---HKDDVAVLTARV 680
Cdd:pfam07228 152 llAERHGLSPEELLDALLEDLLRLGggeLEDDITLLVLRV 191
GAF super family cl17456
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
349-440 1.60e-05

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.


The actual alignment was detected with superfamily member smart00065:

Pssm-ID: 266697  Cd Length: 149  Bit Score: 44.29  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978    349 ALTKGESVLLADdqLQNCPaaVGLRHSPDDGPKIHSWLLVPMFARGVVLGAVVFLRSGNPRRFEPDDVLLAEEIVTRAAV 428
Cdd:smart00065  62 VAETGRPLNIPD--VEADP--LFAEDLLGRYQGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAI 137
                           90
                   ....*....|..
gi 29826978    429 CVDNASRYHRER 440
Cdd:smart00065 138 ALANAQLYEELR 149
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
130-245 6.05e-19

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


:

Pssm-ID: 254806 [Multi-domain]  Cd Length: 110  Bit Score: 84.00  E-value: 6.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   130 FTDSPFNIDIFDTQLRFVGLNIAERRAGVFQGTEYSGHTMREMAPPGllDVDALEARQRRVLETGKALIDTEVVGHPvan 209
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPE--DAARLERALRRALEGEEPIDFLEELLLN--- 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 29826978   210 sPREYVWSESILPLRDPSGRVIALGHVVSDVTQRVR 245
Cdd:pfam08448  76 -GEERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
PAS_9 pfam13426
PAS domain;
21-108 1.58e-06

PAS domain;


:

Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 46.99  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978    21 VLLDACGRVAAWGPGAQQMLGCPAREAVGRSADeFLYDPADAADIVRRWEKGARRGS-----LVLRQRSGKPLAAQIWVR 95
Cdd:pfam13426   5 LVLDPEGRIVYANPAALRLLGYTREELLGKSIR-DLFGPGTDEEAVARLREALRNGGeveveLELRRKDGEPFPVLVSAS 83
                          90
                  ....*....|...
gi 29826978    96 ALTSANGDPQWLV 108
Cdd:pfam13426  84 PVRDEDGEVVGIV 96
 
Name Accession Description Interval E-value
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
21-105 2.00e-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 [Multi-domain]  Cd Length: 103  Bit Score: 40.69  E-value: 2.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978  21 VLLDACGRVAAWGPGAQQMLGCPAREAVGRSADEFLyDPADAADIVRRWEKGARRGSLV-----LRQRSGKPLAAQIWVR 95
Cdd:cd00130   6 IVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLI-HPEDREELRERLENLLSGGEPVtlevrLRRKDGSVIWVLVSLT 84
                        90
                ....*....|
gi 29826978  96 ALTSANGDPQ 105
Cdd:cd00130  85 PIRDEGGEVI 94
HATPase_c cd00075
Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: ...
726-790 1.73e-03

Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: histidine kinase, DNA gyrase B, topoisomerases, heat shock protein HSP90, phytochrome-like ATPases and DNA mismatch repair proteins


Pssm-ID: 238030  Cd Length: 103  Bit Score: 37.63  E-value: 1.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978 726 IVSELVTNAIRYGEEP---ITLRLILDRN-VICEVSD-GSSTSP---------HVRRAQDTDEGGR--GLYLITQLTRSW 789
Cdd:cd00075   4 VLLNLLSNAIKHTPEGggrITISVERDGDhLEIRVEDnGPGIPEedleriferFSDGSRSRKGGGTglGLSIVKKLVELH 83

                .
gi 29826978 790 G 790
Cdd:cd00075  84 G 84
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
487-680 4.08e-44

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: 157.84  E-value: 4.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   487 SGARVALVVGDVTGHDLQSAVTMGRLRSAVRTLADLDLAPDELLTHLDDQMNRFLDErsdegplATGATCLYAVYDPVSR 566
Cdd:pfam07228   1 PDGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRNLEG-------ERFATAVLAVYDPETG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   567 RCLLARAGHPPPAVLSVNGAVDFVELPGGPPL-GLGGIVFEKREIAMDDGDVLVLYTNGLLQprAQDLDAGLHRMRDTLS 645
Cdd:pfam07228  74 TLEYANAGHPPPLLLRPDGGVVELLESPGLPLgVLPDAPYETAEFPLEPGDTLLLYTDGLTE--ARDPDGELFGLERLLA 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 29826978   646 --RTPPSATPQEVCDTLVRELLPTC---HKDDVAVLTARV 680
Cdd:pfam07228 152 llAERHGLSPEELLDALLEDLLRLGggeLEDDITLLVLRV 191
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
461-665 8.44e-23

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 97.42  E-value: 8.44e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978    461 VRTASCYLPASGHTGLGGDWFDVIPLSGARVALVVGDVTGHDLQSAVTMGRLRSAVRTLADLDLAPDELLTHLddqmNRF 540
Cdd:smart00331   1 DDGGLIAQYYEDATQVGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERL----NRA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978    541 LDERSDEGplaTGATCLYAVYDPVSRRCLLARAGHPPPAVLSVNG-AVDFVELPGGPPLGLGGIVFEKREIAMDDGDVLV 619
Cdd:smart00331  77 IYENGEDG---MFATLFLALYDFAGGTLSYANAGHSPPYLLRADGgLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLL 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 29826978    620 LYTNGLlqPRAQDLDAGLHRMRDTLSRtppsaTPQEVCDTLVRELL 665
Cdd:smart00331 154 LYTDGL--TEARNPERLEELLEELLGS-----PPAEIAQRILEELL 192
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
693-801 8.89e-14

Histidine kinase-like ATPase domain;


Pssm-ID: 257897  Cd Length: 126  Bit Score: 69.20  E-value: 8.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   693 IEAQDELVGRARDLTTQQMARWGLEEES-FTTELIVSELVTNAIRYG-----EEPITLRLILD-RNVICEVSD-GSSTSP 764
Cdd:pfam13581   1 FPADLEALRAARRFVAAFLARAGLSEERlEEIELAVEEALTNAVEHAyredpGGPVRVRLEIDgDGLVVEVRDsGPGFDP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 29826978   765 H------VRRAQDTDEGGRGLYLITQLTRSWGTRYGERGKTIW 801
Cdd:pfam13581  81 LelpdpdLTEPDDLPEGGRGLFLIRQLMDEVEYERGDGGNVLR 123
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
349-440 1.60e-05

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: 44.29  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978    349 ALTKGESVLLADdqLQNCPaaVGLRHSPDDGPKIHSWLLVPMFARGVVLGAVVFLRSGNPRRFEPDDVLLAEEIVTRAAV 428
Cdd:smart00065  62 VAETGRPLNIPD--VEADP--LFAEDLLGRYQGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAI 137
                           90
                   ....*....|..
gi 29826978    429 CVDNASRYHRER 440
Cdd:smart00065 138 ALANAQLYEELR 149
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
353-430 2.52e-05

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: 43.73  E-value: 2.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29826978   353 GESVLLADDQLQNCPAAVGLRHSPDDGPKIHSWLLVPMFARGVVLGAVVFLRSGnPRRFEPDDVLLAEEIVTRAAVCV 430
Cdd:pfam01590  70 VVPDVQDDPRFRDLTALASDLPHFLRGLGIRSCLAVPLKGGGELIGVLVLHSTS-PRAFTEEELELLQALADQVAIAL 146
FhlA COG2203
FOG: GAF domain [Signal transduction mechanisms]
356-440 3.75e-04

FOG: GAF domain [Signal transduction mechanisms]


Pssm-ID: 225113  Cd Length: 175  Bit Score: 40.73  E-value: 3.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978 356 VLLADDQLQNCPAAvgLRHSPDDGPKIHSWLLVPMFARGVVLGAVVFLRSGNPRRFEPDDVLLAEEIVTRAAVCVDNASR 435
Cdd:COG2203  90 PVVVEDILQDPRFR--DNPLVLLEPPIRSYLGVPLIAQGELLGLLCVHDSEPRRQWSEEELELLEELAEQVAIAIERARL 167

                ....*
gi 29826978 436 YHRER 440
Cdd:COG2203 168 YEELQ 172
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms]
724-786 4.73e-04

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


Pssm-ID: 225083  Cd Length: 146  Bit Score: 40.05  E-value: 4.73e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29826978 724 ELIVSELVTNAIRYGEE------PITLRLILDRNVIC-EVSD-GSSTSPHVRRAQDTD-------EGGRGLYLITQLT 786
Cdd:COG2172  42 AIAVSEALTNAVKHAYKldpsegEIRIEVSLDDGKLEiRIWDqGPGIEDLEESLGPGDttaeglqEGGLGLFLAKRLM 119
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
726-758 5.86e-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: 5.86e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 29826978    726 IVSELVTNAIRYGEEPITLRLILDR---NVICEVSD 758
Cdd:smart00387   9 VLSNLLDNAIKYTPEGGRITVTLERdgdHVEITVED 44
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
130-245 6.05e-19

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


Pssm-ID: 254806 [Multi-domain]  Cd Length: 110  Bit Score: 84.00  E-value: 6.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   130 FTDSPFNIDIFDTQLRFVGLNIAERRAGVFQGTEYSGHTMREMAPPGllDVDALEARQRRVLETGKALIDTEVVGHPvan 209
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPE--DAARLERALRRALEGEEPIDFLEELLLN--- 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 29826978   210 sPREYVWSESILPLRDPSGRVIALGHVVSDVTQRVR 245
Cdd:pfam08448  76 -GEERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
438-680 1.15e-28

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


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 118.27  E-value: 1.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978 438 RERTTALTLQRSLLPQRLPSASAVRTASCYLPASGhtgLGGDWFDVIPLSGARVALVVGDVTGHDLQSAVTMGRLRSAVR 517
Cdd:COG2208 126 AELEVARQIQQNLLPKALPLFPGIDIEAILVPASE---VGGDYYDFIQLGEKRLRIGIGDVSGKGVPAALLMLMPKLALR 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978 518 TLADLDLA-PDELLTHLddqmNRFLDERSDEGPLATGatcLYAVYDPVSRRCLLARAGHPPPAVLSVNGAVDFVELPGGP 596
Cdd:COG2208 203 LLLESGPLdPADVLETL----NRVLKQNLEEDMFVTL---FLGVYDLDSGELTYSNAGHEPALILSADGEIEVEDLTALG 275
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978 597 PL--GLGGIVFEKREIAMDDGDVLVLYTNGLLQPRAQDLDA-GLHRMRDTLSRTPPSaTPQEVCDTLVRELL----PTCH 669
Cdd:COG2208 276 LPigLLPDYQYEVASLQLEPGDLLVLYTDGVTEARNSDGEFfGLERLLKILGRLLGQ-PAEEILEAILESLEelqgDQIQ 354
                       250
                ....*....|.
gi 29826978 670 KDDVAVLTARV 680
Cdd:COG2208 355 DDDITLLVLKV 365
PAS_9 pfam13426
PAS domain;
21-108 1.58e-06

PAS domain;


Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 46.99  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978    21 VLLDACGRVAAWGPGAQQMLGCPAREAVGRSADeFLYDPADAADIVRRWEKGARRGS-----LVLRQRSGKPLAAQIWVR 95
Cdd:pfam13426   5 LVLDPEGRIVYANPAALRLLGYTREELLGKSIR-DLFGPGTDEEAVARLREALRNGGeveveLELRRKDGEPFPVLVSAS 83
                          90
                  ....*....|...
gi 29826978    96 ALTSANGDPQWLV 108
Cdd:pfam13426  84 PVRDEDGEVVGIV 96
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
21-247 3.10e-06

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 47.92  E-value: 3.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978  21 VLLDACGRVAAWGPGAQQMLGCPAREAVGRSADEFLYDPADAADIVRRWEKGARRGSLVLRQR--SGKPLAAQIWVRALT 98
Cdd:COG2202   3 LVLDRDGRIIYANEAAEELLGYSAEELLGLLLALHPEDRDRLRELLRRLLAGEELLSEELRLVrkDGEERWVELSAAPLR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978  99 SANGDPQWLV----QAARTAVLRTYEYGRALLKGLFTDSPFNIDIFDTQLRFVGLN-IAERRAGVFQGtEYSGHTMREMA 173
Cdd:COG2202  83 DGEGRVLGLLglrdITERKRAEEALRESEERLRALLEASPDGIWVLDEDGRILYANpAAEELLGYSPE-EELGRGLSDLI 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29826978 174 PPGLLDVDALEARQRRVLETGKALIDTEVVGHPvanSPREYVWSESILPLRDPSGRVIALGHVVSDVTQRVRSR 247
Cdd:COG2202 162 HPEDEERRELELARALAEGRGGPLEIEYRVRRK---DGERVRWILSRISPVRDDGEIVGVVGIARDITERKQAE 232
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
19-253 9.68e-04

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 41.29  E-value: 9.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   19 ADVLLDACGRVAAWGPGAQQMLGCPAREAVGRSADEFLYDPADAA--DIVRRWEKGARRG------SLVLRQRSGkplaA 90
Cdd:PRK11359  24 GAVLINENDEVLFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAhpEYIRHNREGGKARvegmsrELQLEKKDG----S 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   91 QIWVR-ALT--SANGDPQWLVQAARTAV-LRTYEYGRALLKGL-FTDSPfnIDIFDTQLRFVGLNIAerragvFqgTEYS 165
Cdd:PRK11359 100 KIWTRfALSkvSAEGKVYYLALVRDASVeMAQKEQTRQLIIAVdHLDRP--VIVLDPERRIVQCNRA------F--TEMF 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978  166 GHTMRE---MAPPGLLDVDALEARQRRVLET---GKALIDTEVVghpVANSPREYVWSE-SILPLRDPSGRVIALGHVVS 238
Cdd:PRK11359 170 GYCISEasgMQPDTLLNIPEFPADNRIRLQQllwKTARDQDEFL---LLTRTGEKIWIKaSISPVYDVLAHLQNLVMTFS 246
                        250
                 ....*....|....*..
gi 29826978  239 DVT--QRVRSRERLVLT 253
Cdd:PRK11359 247 DITeeRQIRQLEGNILA 263
 
Name Accession Description Interval E-value
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
21-105 2.00e-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 [Multi-domain]  Cd Length: 103  Bit Score: 40.69  E-value: 2.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978  21 VLLDACGRVAAWGPGAQQMLGCPAREAVGRSADEFLyDPADAADIVRRWEKGARRGSLV-----LRQRSGKPLAAQIWVR 95
Cdd:cd00130   6 IVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLI-HPEDREELRERLENLLSGGEPVtlevrLRRKDGSVIWVLVSLT 84
                        90
                ....*....|
gi 29826978  96 ALTSANGDPQ 105
Cdd:cd00130  85 PIRDEGGEVI 94
HATPase_c cd00075
Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: ...
726-790 1.73e-03

Histidine kinase-like ATPases; This family includes several ATP-binding proteins for example: histidine kinase, DNA gyrase B, topoisomerases, heat shock protein HSP90, phytochrome-like ATPases and DNA mismatch repair proteins


Pssm-ID: 238030  Cd Length: 103  Bit Score: 37.63  E-value: 1.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978 726 IVSELVTNAIRYGEEP---ITLRLILDRN-VICEVSD-GSSTSP---------HVRRAQDTDEGGR--GLYLITQLTRSW 789
Cdd:cd00075   4 VLLNLLSNAIKHTPEGggrITISVERDGDhLEIRVEDnGPGIPEedleriferFSDGSRSRKGGGTglGLSIVKKLVELH 83

                .
gi 29826978 790 G 790
Cdd:cd00075  84 G 84
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
487-680 4.08e-44

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: 157.84  E-value: 4.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   487 SGARVALVVGDVTGHDLQSAVTMGRLRSAVRTLADLDLAPDELLTHLDDQMNRFLDErsdegplATGATCLYAVYDPVSR 566
Cdd:pfam07228   1 PDGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRNLEG-------ERFATAVLAVYDPETG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   567 RCLLARAGHPPPAVLSVNGAVDFVELPGGPPL-GLGGIVFEKREIAMDDGDVLVLYTNGLLQprAQDLDAGLHRMRDTLS 645
Cdd:pfam07228  74 TLEYANAGHPPPLLLRPDGGVVELLESPGLPLgVLPDAPYETAEFPLEPGDTLLLYTDGLTE--ARDPDGELFGLERLLA 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 29826978   646 --RTPPSATPQEVCDTLVRELLPTC---HKDDVAVLTARV 680
Cdd:pfam07228 152 llAERHGLSPEELLDALLEDLLRLGggeLEDDITLLVLRV 191
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
461-665 8.44e-23

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 97.42  E-value: 8.44e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978    461 VRTASCYLPASGHTGLGGDWFDVIPLSGARVALVVGDVTGHDLQSAVTMGRLRSAVRTLADLDLAPDELLTHLddqmNRF 540
Cdd:smart00331   1 DDGGLIAQYYEDATQVGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERL----NRA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978    541 LDERSDEGplaTGATCLYAVYDPVSRRCLLARAGHPPPAVLSVNG-AVDFVELPGGPPLGLGGIVFEKREIAMDDGDVLV 619
Cdd:smart00331  77 IYENGEDG---MFATLFLALYDFAGGTLSYANAGHSPPYLLRADGgLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLL 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 29826978    620 LYTNGLlqPRAQDLDAGLHRMRDTLSRtppsaTPQEVCDTLVRELL 665
Cdd:smart00331 154 LYTDGL--TEARNPERLEELLEELLGS-----PPAEIAQRILEELL 192
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
693-801 8.89e-14

Histidine kinase-like ATPase domain;


Pssm-ID: 257897  Cd Length: 126  Bit Score: 69.20  E-value: 8.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   693 IEAQDELVGRARDLTTQQMARWGLEEES-FTTELIVSELVTNAIRYG-----EEPITLRLILD-RNVICEVSD-GSSTSP 764
Cdd:pfam13581   1 FPADLEALRAARRFVAAFLARAGLSEERlEEIELAVEEALTNAVEHAyredpGGPVRVRLEIDgDGLVVEVRDsGPGFDP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 29826978   765 H------VRRAQDTDEGGRGLYLITQLTRSWGTRYGERGKTIW 801
Cdd:pfam13581  81 LelpdpdLTEPDDLPEGGRGLFLIRQLMDEVEYERGDGGNVLR 123
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
349-440 1.60e-05

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: 44.29  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978    349 ALTKGESVLLADdqLQNCPaaVGLRHSPDDGPKIHSWLLVPMFARGVVLGAVVFLRSGNPRRFEPDDVLLAEEIVTRAAV 428
Cdd:smart00065  62 VAETGRPLNIPD--VEADP--LFAEDLLGRYQGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAI 137
                           90
                   ....*....|..
gi 29826978    429 CVDNASRYHRER 440
Cdd:smart00065 138 ALANAQLYEELR 149
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
353-430 2.52e-05

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: 43.73  E-value: 2.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29826978   353 GESVLLADDQLQNCPAAVGLRHSPDDGPKIHSWLLVPMFARGVVLGAVVFLRSGnPRRFEPDDVLLAEEIVTRAAVCV 430
Cdd:pfam01590  70 VVPDVQDDPRFRDLTALASDLPHFLRGLGIRSCLAVPLKGGGELIGVLVLHSTS-PRAFTEEELELLQALADQVAIAL 146
GAF_2 pfam13185
GAF domain;
348-431 2.61e-04

GAF domain;


Pssm-ID: 257553  Cd Length: 150  Bit Score: 40.65  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   348 DALTKGESVLLADDQLQNcpaaVGLRHSPDDGPKIHSWLLVPMFARGVVLGaVVFLRSGNPRRFEPDDVLLAEEIVTRAA 427
Cdd:pfam13185  72 GALRTGKPVIINDVASDP----SGAGGLPAGHEGLRSFLSVPLISGGRVIG-VLALGSKEPGAFDEEDLELLELLAEQIA 146

                  ....
gi 29826978   428 VCVD 431
Cdd:pfam13185 147 IAIE 150
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
726-807 3.06e-04

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: 40.00  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   726 IVSELVTNAIRYGEE--PITLRLILDRN-VICEVSD-GSSTSPHVR------------RAQDTDEGGRGLYLITQLTRSW 789
Cdd:pfam02518   9 VLSNLLDNAIKHAPAggEIEVTLERDGGrLRITVEDnGIGIPPEDLpkifepffrtdgSRSKVGGTGLGLSIVRKLVELH 88
                          90       100
                  ....*....|....*....|...
gi 29826978   790 G-----TRYGERGKTIWAEQPLR 807
Cdd:pfam02518  89 GgtitvESEPGGGTTFTLTLPLE 111
FhlA COG2203
FOG: GAF domain [Signal transduction mechanisms]
356-440 3.75e-04

FOG: GAF domain [Signal transduction mechanisms]


Pssm-ID: 225113  Cd Length: 175  Bit Score: 40.73  E-value: 3.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978 356 VLLADDQLQNCPAAvgLRHSPDDGPKIHSWLLVPMFARGVVLGAVVFLRSGNPRRFEPDDVLLAEEIVTRAAVCVDNASR 435
Cdd:COG2203  90 PVVVEDILQDPRFR--DNPLVLLEPPIRSYLGVPLIAQGELLGLLCVHDSEPRRQWSEEELELLEELAEQVAIAIERARL 167

                ....*
gi 29826978 436 YHRER 440
Cdd:COG2203 168 YEELQ 172
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms]
724-786 4.73e-04

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


Pssm-ID: 225083  Cd Length: 146  Bit Score: 40.05  E-value: 4.73e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29826978 724 ELIVSELVTNAIRYGEE------PITLRLILDRNVIC-EVSD-GSSTSPHVRRAQDTD-------EGGRGLYLITQLT 786
Cdd:COG2172  42 AIAVSEALTNAVKHAYKldpsegEIRIEVSLDDGKLEiRIWDqGPGIEDLEESLGPGDttaeglqEGGLGLFLAKRLM 119
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
726-758 5.86e-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: 5.86e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 29826978    726 IVSELVTNAIRYGEEPITLRLILDR---NVICEVSD 758
Cdd:smart00387   9 VLSNLLDNAIKYTPEGGRITVTLERdgdHVEITVED 44
GAF_3 pfam13492
GAF domain;
377-432 6.57e-03

GAF domain;


Pssm-ID: 257816  Cd Length: 129  Bit Score: 36.27  E-value: 6.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 29826978   377 DDGPKIHSWLLVPMFARGVVLGaVVFLRSGNPRRFEPDDVLLAEEIVTRAAVCVDN 432
Cdd:pfam13492  75 RDLLPSESLLAVPLRAGGEVIG-VLVLESTPEEAFTPEDLELLELLASQIAIALEN 129
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
130-245 6.05e-19

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


Pssm-ID: 254806 [Multi-domain]  Cd Length: 110  Bit Score: 84.00  E-value: 6.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   130 FTDSPFNIDIFDTQLRFVGLNIAERRAGVFQGTEYSGHTMREMAPPGllDVDALEARQRRVLETGKALIDTEVVGHPvan 209
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPE--DAARLERALRRALEGEEPIDFLEELLLN--- 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 29826978   210 sPREYVWSESILPLRDPSGRVIALGHVVSDVTQRVR 245
Cdd:pfam08448  76 -GEERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
438-680 1.15e-28

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


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 118.27  E-value: 1.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978 438 RERTTALTLQRSLLPQRLPSASAVRTASCYLPASGhtgLGGDWFDVIPLSGARVALVVGDVTGHDLQSAVTMGRLRSAVR 517
Cdd:COG2208 126 AELEVARQIQQNLLPKALPLFPGIDIEAILVPASE---VGGDYYDFIQLGEKRLRIGIGDVSGKGVPAALLMLMPKLALR 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978 518 TLADLDLA-PDELLTHLddqmNRFLDERSDEGPLATGatcLYAVYDPVSRRCLLARAGHPPPAVLSVNGAVDFVELPGGP 596
Cdd:COG2208 203 LLLESGPLdPADVLETL----NRVLKQNLEEDMFVTL---FLGVYDLDSGELTYSNAGHEPALILSADGEIEVEDLTALG 275
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978 597 PL--GLGGIVFEKREIAMDDGDVLVLYTNGLLQPRAQDLDA-GLHRMRDTLSRTPPSaTPQEVCDTLVRELL----PTCH 669
Cdd:COG2208 276 LPigLLPDYQYEVASLQLEPGDLLVLYTDGVTEARNSDGEFfGLERLLKILGRLLGQ-PAEEILEAILESLEelqgDQIQ 354
                       250
                ....*....|.
gi 29826978 670 KDDVAVLTARV 680
Cdd:COG2208 355 DDDITLLVLKV 365
PAS_9 pfam13426
PAS domain;
21-108 1.58e-06

PAS domain;


Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 46.99  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978    21 VLLDACGRVAAWGPGAQQMLGCPAREAVGRSADeFLYDPADAADIVRRWEKGARRGS-----LVLRQRSGKPLAAQIWVR 95
Cdd:pfam13426   5 LVLDPEGRIVYANPAALRLLGYTREELLGKSIR-DLFGPGTDEEAVARLREALRNGGeveveLELRRKDGEPFPVLVSAS 83
                          90
                  ....*....|...
gi 29826978    96 ALTSANGDPQWLV 108
Cdd:pfam13426  84 PVRDEDGEVVGIV 96
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
21-247 3.10e-06

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 47.92  E-value: 3.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978  21 VLLDACGRVAAWGPGAQQMLGCPAREAVGRSADEFLYDPADAADIVRRWEKGARRGSLVLRQR--SGKPLAAQIWVRALT 98
Cdd:COG2202   3 LVLDRDGRIIYANEAAEELLGYSAEELLGLLLALHPEDRDRLRELLRRLLAGEELLSEELRLVrkDGEERWVELSAAPLR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978  99 SANGDPQWLV----QAARTAVLRTYEYGRALLKGLFTDSPFNIDIFDTQLRFVGLN-IAERRAGVFQGtEYSGHTMREMA 173
Cdd:COG2202  83 DGEGRVLGLLglrdITERKRAEEALRESEERLRALLEASPDGIWVLDEDGRILYANpAAEELLGYSPE-EELGRGLSDLI 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29826978 174 PPGLLDVDALEARQRRVLETGKALIDTEVVGHPvanSPREYVWSESILPLRDPSGRVIALGHVVSDVTQRVRSR 247
Cdd:COG2202 162 HPEDEERRELELARALAEGRGGPLEIEYRVRRK---DGERVRWILSRISPVRDDGEIVGVVGIARDITERKQAE 232
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
19-253 9.68e-04

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 41.29  E-value: 9.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   19 ADVLLDACGRVAAWGPGAQQMLGCPAREAVGRSADEFLYDPADAA--DIVRRWEKGARRG------SLVLRQRSGkplaA 90
Cdd:PRK11359  24 GAVLINENDEVLFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAhpEYIRHNREGGKARvegmsrELQLEKKDG----S 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   91 QIWVR-ALT--SANGDPQWLVQAARTAV-LRTYEYGRALLKGL-FTDSPfnIDIFDTQLRFVGLNIAerragvFqgTEYS 165
Cdd:PRK11359 100 KIWTRfALSkvSAEGKVYYLALVRDASVeMAQKEQTRQLIIAVdHLDRP--VIVLDPERRIVQCNRA------F--TEMF 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978  166 GHTMRE---MAPPGLLDVDALEARQRRVLET---GKALIDTEVVghpVANSPREYVWSE-SILPLRDPSGRVIALGHVVS 238
Cdd:PRK11359 170 GYCISEasgMQPDTLLNIPEFPADNRIRLQQllwKTARDQDEFL---LLTRTGEKIWIKaSISPVYDVLAHLQNLVMTFS 246
                        250
                 ....*....|....*..
gi 29826978  239 DVT--QRVRSRERLVLT 253
Cdd:PRK11359 247 DITeeRQIRQLEGNILA 263
PRK11360 PRK11360
sensory histidine kinase AtoS; Provisional
188-259 1.16e-03

sensory histidine kinase AtoS; Provisional


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 41.11  E-value: 1.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29826978  188 RRVLETGKALIDTEVVGHpvaNSPREYVWSESILPLRDPSGRVIALGHVVSDVTQRVRSRERLVLTNE-AAIG 259
Cdd:PRK11360 322 LDTLEHGTEHVDLEISFP---GRDRTIELSVSTSLLHNTHGEMIGALVIFSDLTERKRLQRRVARQERlAALG 391
PRK13560 PRK13560
hypothetical protein; Provisional
1-428 5.88e-03

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 38.89  E-value: 5.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978    1 MHDITFRGDGEFPEPGseadvLLDACGRVAAWGP----GAQQMLgcpAREAVGRSADEFLYDPADAADIVRRWEKGARRG 76
Cdd:PRK13560  81 MFLFALDGDGTFSFPS-----LLDANGELAAIAKhdlmADKGLL---AMLIGGDDGDFFFANPFRSAETIAMALQSDDWQ 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978   77 SLVLRQRSGKPLAAQIWVRALTSANGDPQWL-----VQAARTAVLRTYEYGRaLLKGLFTDSPFNIDIFDTQLRFVGLNI 151
Cdd:PRK13560 153 EEEGHFRCGDGRFIDCCLRFERHAHADDQVDgfaedITERKRAEERIDEALH-FLQQLLDNIADPAFWKDEDAKVFGCND 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978  152 AERRAGVFQGTEYSGHTMREMAPPGLLDvDALEARQRRVLETGKALIDTEVVGHPVANSPREYVWSESilPLRDPSGRVI 231
Cdd:PRK13560 232 AACLACGFRREEIIGMSIHDFAPAQPAD-DYQEADAAKFDADGSQIIEAEFQNKDGRTRPVDVIFNHA--EFDDKENHCA 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978  232 ALGHVVSDVTQRVRSRERLVLTNE-----------AAIGI---GTTLDLWRTARElaevavpRFADICFVDLLDSVFPGR 297
Cdd:PRK13560 309 GLVGAITDISGRRAAERELLEKEDmlraiieaapiAAIGLdadGNICFVNNNAAE-------RMLGWSAAEVMGKPLPGM 381
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826978  298 EPTEGRpprpplfrraacsgaaedtgsdaagEVKVGDANLWaTAPGSPFLDALTKGESVLLADDQLQNCPAavgLRHSPD 377
Cdd:PRK13560 382 DPELNE-------------------------EFWCGDFQEW-YPDGRPMAFDACPMAKTIKGGKIFDGQEV---LIERED 432
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 29826978  378 DGPKIHSWLLVPMF-ARGVVLGAVVFLRSGNPRRFEPDDVLLAEEIVTRAAV 428
Cdd:PRK13560 433 DGPADCSAYAEPLHdADGNIIGAIALLVDITERKQVEEQLLLANLIVENSPL 484
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH